Full text data of PGD
PGD
(PGDH)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
6-phosphogluconate dehydrogenase, decarboxylating; 1.1.1.44
Note: presumably soluble (membrane word is not in UniProt keywords or features)
6-phosphogluconate dehydrogenase, decarboxylating; 1.1.1.44
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00219525
IPI00219525 6-phosphogluconate dehydrogenase, decarboxylating electron transporter activity, pentose-phosphate shunt, oxidative branch soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00219525 6-phosphogluconate dehydrogenase, decarboxylating electron transporter activity, pentose-phosphate shunt, oxidative branch soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P52209
ID 6PGD_HUMAN Reviewed; 483 AA.
AC P52209; A8K2Y9; Q9BWD8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 139.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=PGD; Synonyms=PGDH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8978909; DOI=10.1007/BF00554412;
RA Tsui S.K.W., Chan J.Y., Waye M.M.Y., Fung K.-P., Lee C.-Y.;
RT "Identification of a cDNA encoding 6-phosphogluconate dehydrogenase
RT from a human heart cDNA library.";
RL Biochem. Genet. 34:367-373(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59 AND LYS-309, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH NADP, AND
RP SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Structure of human phosphogluconate dehydrogenase in complex with
RT NADPH at 2.53 A.";
RL Submitted (SEP-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-
CC phosphogluconate to ribulose 5-phosphate and CO(2), with
CC concomitant reduction of NADP to NADPH (By similarity).
CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC 5-phosphate + CO(2) + NADPH.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC step 3/3.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC O95777:NAA38; NbExp=1; IntAct=EBI-372761, EBI-347779;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC family.
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DR EMBL; U30255; AAA75302.1; -; mRNA.
DR EMBL; AK290404; BAF83093.1; -; mRNA.
DR EMBL; AL139424; CAI95751.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71648.1; -; Genomic_DNA.
DR EMBL; BC000368; AAH00368.1; -; mRNA.
DR PIR; G01922; G01922.
DR RefSeq; NP_002622.2; NM_002631.2.
DR UniGene; Hs.464071; -.
DR PDB; 2JKV; X-ray; 2.53 A; A/B/C/D/E/F=1-483.
DR PDB; 4GWG; X-ray; 1.39 A; A=2-483.
DR PDB; 4GWK; X-ray; 1.53 A; A=2-483.
DR PDBsum; 2JKV; -.
DR PDBsum; 4GWG; -.
DR PDBsum; 4GWK; -.
DR ProteinModelPortal; P52209; -.
DR SMR; P52209; 2-470.
DR IntAct; P52209; 6.
DR MINT; MINT-1415782; -.
DR STRING; 9606.ENSP00000270776; -.
DR BindingDB; P52209; -.
DR ChEMBL; CHEMBL3404; -.
DR PhosphoSite; P52209; -.
DR DMDM; 20981679; -.
DR PaxDb; P52209; -.
DR PeptideAtlas; P52209; -.
DR PRIDE; P52209; -.
DR DNASU; 5226; -.
DR Ensembl; ENST00000270776; ENSP00000270776; ENSG00000142657.
DR GeneID; 5226; -.
DR KEGG; hsa:5226; -.
DR UCSC; uc001arc.3; human.
DR CTD; 5226; -.
DR GeneCards; GC01P010458; -.
DR HGNC; HGNC:8891; PGD.
DR HPA; HPA031314; -.
DR MIM; 172200; gene.
DR neXtProt; NX_P52209; -.
DR PharmGKB; PA33229; -.
DR eggNOG; COG0362; -.
DR HOGENOM; HOG000255147; -.
DR HOVERGEN; HBG000029; -.
DR InParanoid; P52209; -.
DR KO; K00033; -.
DR OMA; KQQIGVI; -.
DR PhylomeDB; P52209; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P52209; -.
DR UniPathway; UPA00115; UER00410.
DR ChiTaRS; PGD; human.
DR EvolutionaryTrace; P52209; -.
DR GenomeRNAi; 5226; -.
DR NextBio; 20204; -.
DR PRO; PR:P52209; -.
DR ArrayExpress; P52209; -.
DR Bgee; P52209; -.
DR CleanEx; HS_PGD; -.
DR Genevestigator; P52209; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019322; P:pentose biosynthetic process; IEA:Ensembl.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IDA:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR Gene3D; 1.20.5.320; -; 1.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_decarbox.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR006184; 6PGdom_BS.
DR InterPro; IPR013328; DH_multihelical.
DR InterPro; IPR012284; Fibritin/6PGD_C-extension.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 483 6-phosphogluconate dehydrogenase,
FT decarboxylating.
FT /FTId=PRO_0000090063.
FT NP_BIND 10 15 NADP.
FT NP_BIND 33 35 NADP.
FT NP_BIND 75 77 NADP.
FT NP_BIND 478 481 NADP; shared with dimeric partner.
FT REGION 129 131 Substrate binding (By similarity).
FT REGION 187 188 Substrate binding (By similarity).
FT ACT_SITE 184 184 Proton acceptor (By similarity).
FT ACT_SITE 191 191 Proton donor (By similarity).
FT BINDING 103 103 NADP.
FT BINDING 103 103 Substrate (By similarity).
FT BINDING 192 192 Substrate (By similarity).
FT BINDING 261 261 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 288 288 Substrate (By similarity).
FT BINDING 447 447 Substrate; shared with dimeric partner
FT (By similarity).
FT BINDING 453 453 Substrate; shared with dimeric partner
FT (By similarity).
FT MOD_RES 59 59 N6-acetyllysine.
FT MOD_RES 257 257 Phosphoserine (By similarity).
FT MOD_RES 263 263 Phosphothreonine (By similarity).
FT MOD_RES 267 267 Phosphothreonine (By similarity).
FT MOD_RES 270 270 Phosphoserine (By similarity).
FT MOD_RES 309 309 N6-acetyllysine.
FT VARIANT 268 268 A -> S (in dbSNP:rs11547610).
FT /FTId=VAR_048104.
FT CONFLICT 118 118 A -> G (in Ref. 1; AAA75302).
FT CONFLICT 135 135 A -> P (in Ref. 1; AAA75302).
FT STRAND 4 9
FT HELIX 13 24
FT STRAND 29 32
FT HELIX 37 44
FT TURN 45 49
FT HELIX 58 63
FT STRAND 70 73
FT HELIX 79 88
FT HELIX 89 91
FT STRAND 97 100
FT HELIX 106 118
FT STRAND 122 130
FT HELIX 131 137
FT STRAND 140 145
FT HELIX 147 149
FT HELIX 150 160
FT TURN 165 167
FT STRAND 169 171
FT HELIX 179 207
FT HELIX 213 223
FT TURN 224 228
FT HELIX 231 241
FT STRAND 247 250
FT HELIX 251 253
FT HELIX 265 274
FT HELIX 279 292
FT HELIX 294 301
FT HELIX 316 349
FT HELIX 355 361
FT HELIX 371 382
FT HELIX 389 391
FT HELIX 393 416
FT HELIX 421 433
FT HELIX 440 451
FT STRAND 455 457
FT STRAND 460 465
SQ SEQUENCE 483 AA; 53140 MW; 6CEFC0077D1283E3 CRC64;
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE
MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG
ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG
HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL
KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA
SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL
MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM
PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS
YNA
//
ID 6PGD_HUMAN Reviewed; 483 AA.
AC P52209; A8K2Y9; Q9BWD8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 139.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=PGD; Synonyms=PGDH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8978909; DOI=10.1007/BF00554412;
RA Tsui S.K.W., Chan J.Y., Waye M.M.Y., Fung K.-P., Lee C.-Y.;
RT "Identification of a cDNA encoding 6-phosphogluconate dehydrogenase
RT from a human heart cDNA library.";
RL Biochem. Genet. 34:367-373(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59 AND LYS-309, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH NADP, AND
RP SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Structure of human phosphogluconate dehydrogenase in complex with
RT NADPH at 2.53 A.";
RL Submitted (SEP-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-
CC phosphogluconate to ribulose 5-phosphate and CO(2), with
CC concomitant reduction of NADP to NADPH (By similarity).
CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC 5-phosphate + CO(2) + NADPH.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC step 3/3.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC O95777:NAA38; NbExp=1; IntAct=EBI-372761, EBI-347779;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U30255; AAA75302.1; -; mRNA.
DR EMBL; AK290404; BAF83093.1; -; mRNA.
DR EMBL; AL139424; CAI95751.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71648.1; -; Genomic_DNA.
DR EMBL; BC000368; AAH00368.1; -; mRNA.
DR PIR; G01922; G01922.
DR RefSeq; NP_002622.2; NM_002631.2.
DR UniGene; Hs.464071; -.
DR PDB; 2JKV; X-ray; 2.53 A; A/B/C/D/E/F=1-483.
DR PDB; 4GWG; X-ray; 1.39 A; A=2-483.
DR PDB; 4GWK; X-ray; 1.53 A; A=2-483.
DR PDBsum; 2JKV; -.
DR PDBsum; 4GWG; -.
DR PDBsum; 4GWK; -.
DR ProteinModelPortal; P52209; -.
DR SMR; P52209; 2-470.
DR IntAct; P52209; 6.
DR MINT; MINT-1415782; -.
DR STRING; 9606.ENSP00000270776; -.
DR BindingDB; P52209; -.
DR ChEMBL; CHEMBL3404; -.
DR PhosphoSite; P52209; -.
DR DMDM; 20981679; -.
DR PaxDb; P52209; -.
DR PeptideAtlas; P52209; -.
DR PRIDE; P52209; -.
DR DNASU; 5226; -.
DR Ensembl; ENST00000270776; ENSP00000270776; ENSG00000142657.
DR GeneID; 5226; -.
DR KEGG; hsa:5226; -.
DR UCSC; uc001arc.3; human.
DR CTD; 5226; -.
DR GeneCards; GC01P010458; -.
DR HGNC; HGNC:8891; PGD.
DR HPA; HPA031314; -.
DR MIM; 172200; gene.
DR neXtProt; NX_P52209; -.
DR PharmGKB; PA33229; -.
DR eggNOG; COG0362; -.
DR HOGENOM; HOG000255147; -.
DR HOVERGEN; HBG000029; -.
DR InParanoid; P52209; -.
DR KO; K00033; -.
DR OMA; KQQIGVI; -.
DR PhylomeDB; P52209; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P52209; -.
DR UniPathway; UPA00115; UER00410.
DR ChiTaRS; PGD; human.
DR EvolutionaryTrace; P52209; -.
DR GenomeRNAi; 5226; -.
DR NextBio; 20204; -.
DR PRO; PR:P52209; -.
DR ArrayExpress; P52209; -.
DR Bgee; P52209; -.
DR CleanEx; HS_PGD; -.
DR Genevestigator; P52209; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019322; P:pentose biosynthetic process; IEA:Ensembl.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IDA:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR Gene3D; 1.20.5.320; -; 1.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_decarbox.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR006184; 6PGdom_BS.
DR InterPro; IPR013328; DH_multihelical.
DR InterPro; IPR012284; Fibritin/6PGD_C-extension.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 483 6-phosphogluconate dehydrogenase,
FT decarboxylating.
FT /FTId=PRO_0000090063.
FT NP_BIND 10 15 NADP.
FT NP_BIND 33 35 NADP.
FT NP_BIND 75 77 NADP.
FT NP_BIND 478 481 NADP; shared with dimeric partner.
FT REGION 129 131 Substrate binding (By similarity).
FT REGION 187 188 Substrate binding (By similarity).
FT ACT_SITE 184 184 Proton acceptor (By similarity).
FT ACT_SITE 191 191 Proton donor (By similarity).
FT BINDING 103 103 NADP.
FT BINDING 103 103 Substrate (By similarity).
FT BINDING 192 192 Substrate (By similarity).
FT BINDING 261 261 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 288 288 Substrate (By similarity).
FT BINDING 447 447 Substrate; shared with dimeric partner
FT (By similarity).
FT BINDING 453 453 Substrate; shared with dimeric partner
FT (By similarity).
FT MOD_RES 59 59 N6-acetyllysine.
FT MOD_RES 257 257 Phosphoserine (By similarity).
FT MOD_RES 263 263 Phosphothreonine (By similarity).
FT MOD_RES 267 267 Phosphothreonine (By similarity).
FT MOD_RES 270 270 Phosphoserine (By similarity).
FT MOD_RES 309 309 N6-acetyllysine.
FT VARIANT 268 268 A -> S (in dbSNP:rs11547610).
FT /FTId=VAR_048104.
FT CONFLICT 118 118 A -> G (in Ref. 1; AAA75302).
FT CONFLICT 135 135 A -> P (in Ref. 1; AAA75302).
FT STRAND 4 9
FT HELIX 13 24
FT STRAND 29 32
FT HELIX 37 44
FT TURN 45 49
FT HELIX 58 63
FT STRAND 70 73
FT HELIX 79 88
FT HELIX 89 91
FT STRAND 97 100
FT HELIX 106 118
FT STRAND 122 130
FT HELIX 131 137
FT STRAND 140 145
FT HELIX 147 149
FT HELIX 150 160
FT TURN 165 167
FT STRAND 169 171
FT HELIX 179 207
FT HELIX 213 223
FT TURN 224 228
FT HELIX 231 241
FT STRAND 247 250
FT HELIX 251 253
FT HELIX 265 274
FT HELIX 279 292
FT HELIX 294 301
FT HELIX 316 349
FT HELIX 355 361
FT HELIX 371 382
FT HELIX 389 391
FT HELIX 393 416
FT HELIX 421 433
FT HELIX 440 451
FT STRAND 455 457
FT STRAND 460 465
SQ SEQUENCE 483 AA; 53140 MW; 6CEFC0077D1283E3 CRC64;
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE
MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG
ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG
HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL
KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA
SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL
MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM
PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS
YNA
//
MIM
172200
*RECORD*
*FIELD* NO
172200
*FIELD* TI
*172200 6-@PHOSPHOGLUCONATE DEHYDROGENASE, ERYTHROCYTE; PGD
;;PGD, ERYTHROCYTE; 6PGD
read more*FIELD* TX
Brewer and Dern (1964) reported deficiency of 6-phosphogluconate
dehydrogenase (6PGD), the second dehydrogenase in the pentose phosphate
shunt, in 10 members of 4 generations of an American black family. They
concluded that the inheritance is autosomal dominant, all 6PGD-deficient
persons observed being heterozygotes. However, no male-to-male
transmission was observed; indeed, no offspring of affected males were
tested. Against X-linkage is the fact that the average enzyme level in 3
6PGD-deficient males was somewhat higher than that in seven
6PGD-deficient females. The opposite would be expected of an X-linked
trait. The authors commented on the autosomal control of an enzyme that
is closely related metabolically to G6PD, an enzyme determined by an
X-linked gene. In a survey of unrelated persons, Dern et al. (1966)
found in 3 of 873 American blacks and 2 of 275 Caucasians a reduction in
erythrocyte 6-phosphogluconate dehydrogenase to the range of 42 to 65%
of normal. Leukocyte enzyme was also reduced. No correlation was found
between electrophoretic phenotype and the quantitative variation. The
inheritance was clearly autosomal dominant. Using starch-gel
electrophoresis, Fildes and Parr (1963) detected 2 distinct types of
human red cell 6-phosphogluconate dehydrogenase. Ten of 150 random blood
samples showed 2 broad, less distinct bands in contrast to the single
narrow, sharp band in the remainder. Inheritance appears to be
autosomal, a point of particular note. Since the G6PD locus is X-linked,
these 2 functionally related genes do not show clustering. Heterozygotes
and homozygotes showed no quantitative difference in red blood cell 6PGD
activity. Deficiency of this enzyme, with or without electrophoretic
abnormality, has been observed (Parr, 1966). Nevo (1989) identified a
rare PGD variant called PGD Mediterranean. Severe deficiency of 6PGD,
although well-documented (Brewer and Dern, 1964; Dern et al., 1966; Parr
and Fitch, 1967), has never been incriminated as the cause of hemolytic
anemia. In fact, persons with less than 5% of normal activity in red
cell enzymes, who were found in population surveys by Parr and Fitch
(1967), were entirely asymptomatic. Beutler et al. (1985) found
hemolysis in a subject in whom partial deficiency of 6PGD coexisted with
G6PD deficiency, whereas no hemolysis was found in persons with the G6PD
variant alone. A synergism of the 2 enzymopathies is possible.
A possibility of linkage between the Rhesus and 6PGD loci was found by
Weitkamp et al. (1970). This has since been fully confirmed (Weitkamp et
al., 1971). Weitkamp (1972) gave valid criticism of the conclusions of
linkage studies of 2 groups. It is clear, however, that the Rhesus and
6PGD loci are on chromosome 1. Douglas et al. (1973) demonstrated that
the PGM1 and 6PGD loci are on the distal end of the short arm of
chromosome 1. Assuming that each arm of chromosome 1 is 140 male cM
long, Cook et al. (1974) concluded that, measured from the centromere,
map positions are as follows: PGD, 1p124; RH, 1p109; PGM1, 1p079; FY,
1p010; PEPC, 1q030. At HGM8, Povey et al. (1985) concluded that the
smallest region of overlap for PGD is 1p36.2-p36.13.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* SA
Benkmann et al. (1986); Blake and Kirk (1969); Bowman et al. (1966);
Burgerhout et al. (1973); Davidson (1967); Nelson (1982); Ritter
et al. (1971); Tariverdian et al. (1970); Westerveld and Meera Khan
(1972)
*FIELD* RF
1. Benkmann, H.-G.; Paik, Y. K.; Chen, L. Z.; Goedde, H. W.: Polymorphism
of 6-PGD in South Korea: a new genetic variant 6-PGD Korea. Hum.
Genet. 74: 204-205, 1986.
2. Beutler, E.; Kuhl, W.; Gelbart, T.: 6-Phosphogluconolactonase
deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction
with glucose-6-phosphate dehydrogenase deficiency. Proc. Nat. Acad.
Sci. 82: 3876-3878, 1985.
3. Blake, N. M.; Kirk, R. L.: New genetic variant of 6-phosphogluconate
dehydrogenase in Australian aborigines. Nature 221: 278 only, 1969.
4. Bowman, J. E.; Carson, P. E.; Frischer, H.; De Garay, A. L.: Genetics
of starch-gel electrophoretic variants of human 6-phosphogluconic
dehydrogenase: population and family studies in the United States
and in Mexico. Nature 210: 811-812, 1966.
5. Brewer, G. J.; Dern, R. J.: A new inherited enzymatic deficiency
of human erythrocytes: 6-phosphogluconate dehydrogenase deficiency. Am.
J. Hum. Genet. 16: 472-476, 1964.
6. Burgerhout, W.; Van Someren, H.; Bootsma, D.: Cytological mapping
of the genes assigned to the human A1 chromosome by use of radiation-induced
chromosome breakage in a human-Chinese hamster hybrid cell line. Humangenetik 20:
159-162, 1973.
7. Cook, P. J. L.; Robson, E. B.; Buckton, K. E.; Jacobs, P. A.; Polani,
P. E.: Segregation of genetic markers in families with chromosome
polymorphisms and structural rearrangements involving chromosome 1. Ann.
Hum. Genet. 37: 261-274, 1974.
8. Davidson, R. G.: Electrophoretic variants of human 6-phosphogluconate
dehydrogenase: population and family studies and description of a
new variant. Ann. Hum. Genet. 30: 355-362, 1967.
9. Dern, R. J.; Brewer, G. J.; Tashian, R. E.; Shows, T. B.: Hereditary
variation of erythrocytic 6-phosphogluconate dehydrogenase. J. Lab.
Clin. Med. 67: 255-264, 1966.
10. Douglas, G. R.; McAlpine, P. J.; Hamerton, J. L.: Regional localization
of loci for human PGM-1 and 6PGD on human chromosome 1 by use of hybrids
of Chinese hamster-human somatic cells. Proc. Nat. Acad. Sci. 70:
2737-2740, 1973.
11. Fildes, R. A.; Parr, C. W.: Human red-cell phosphogluconate dehydrogenases. Nature 200:
890-891, 1963.
12. Nelson, M. S.: Biochemical and genetic characterization of the
Lowell variant: a new phenotype of 6-phosphogluconate dehydrogenase. Hum.
Genet. 62: 333-336, 1982.
13. Nevo, S.: A new rare PGD variant, PGD Mediterranean. Hum. Genet. 81:
199 only, 1989.
14. Parr, C. W.: Erythrocyte phosphogluconate dehydrogenase polymorphism. Nature 210:
487-489, 1966.
15. Parr, C. W.; Fitch, L. I.: Inherited quantitative variations
of human phosphogluconate dehydrogenase. Ann. Hum. Genet. 30: 339-353,
1967.
16. Povey, S.; Morton, N. E.; Sherman, S. L.: Report of the committee
on the genetic constitution of chromosomes 1 and 2. Cytogenet. Cell
Genet. 40: 67-106, 1985.
17. Ritter, H.; Toriverdiau, G.; Wendt, G. G.; Zilch, I.: Genetic
and linkage analysis on 6-PGD. Humangenetik 14: 73-75, 1971.
18. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World
Distribution. New York: Oxford Univ. Press (pub.) 1988.
19. Tariverdian, G.; Ropers, H.-H.; Op't Hof, J.; Ritter, H.: Zur
Genetik der 6-Phosphogluconatdehydrogenase (EC: 1.1.1.44): Eine neue
Variante F (Freiburg). Humangenetik 10: 355-357, 1970.
20. Weitkamp, L. R.: Genetic linkage relationships of the ADA and
6-PGD loci in 'Humangenetik.' (Letter) Humangenetik 15: 359-360,
1972.
21. Weitkamp, L. R.; Guttormsen, S. A.; Greendyke, R. M.: Genetic
linkage between a locus for 6-PGD and the Rh locus: evaluation of
possible heterogeneity in the recombination fraction between sexes
and among families. Am. J. Hum. Genet. 23: 462-470, 1971.
22. Weitkamp, L. R.; Guttormsen, S. A.; Shreffler, D. C.; Sing, C.
F.; Napier, J. A.: Genetic linkage relations of the loci for 6-phosphogluconate
dehydrogenase and adenosine deaminase in man. Am. J. Hum. Genet. 22:
216-220, 1970.
23. Westerveld, A.; Meera Khan, P.: Evidence for linkage between
human loci for 6-phosphogluconate dehydrogenase and phosphoglucomutase(1)
in man-Chinese hamster somatic cell hybrids. Nature 236: 30-32,
1972.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 10/31/2003
carol: 9/29/1998
mimadm: 1/14/1995
warfield: 3/4/1994
supermim: 3/16/1992
carol: 3/4/1992
carol: 8/19/1991
carol: 4/30/1991
*RECORD*
*FIELD* NO
172200
*FIELD* TI
*172200 6-@PHOSPHOGLUCONATE DEHYDROGENASE, ERYTHROCYTE; PGD
;;PGD, ERYTHROCYTE; 6PGD
read more*FIELD* TX
Brewer and Dern (1964) reported deficiency of 6-phosphogluconate
dehydrogenase (6PGD), the second dehydrogenase in the pentose phosphate
shunt, in 10 members of 4 generations of an American black family. They
concluded that the inheritance is autosomal dominant, all 6PGD-deficient
persons observed being heterozygotes. However, no male-to-male
transmission was observed; indeed, no offspring of affected males were
tested. Against X-linkage is the fact that the average enzyme level in 3
6PGD-deficient males was somewhat higher than that in seven
6PGD-deficient females. The opposite would be expected of an X-linked
trait. The authors commented on the autosomal control of an enzyme that
is closely related metabolically to G6PD, an enzyme determined by an
X-linked gene. In a survey of unrelated persons, Dern et al. (1966)
found in 3 of 873 American blacks and 2 of 275 Caucasians a reduction in
erythrocyte 6-phosphogluconate dehydrogenase to the range of 42 to 65%
of normal. Leukocyte enzyme was also reduced. No correlation was found
between electrophoretic phenotype and the quantitative variation. The
inheritance was clearly autosomal dominant. Using starch-gel
electrophoresis, Fildes and Parr (1963) detected 2 distinct types of
human red cell 6-phosphogluconate dehydrogenase. Ten of 150 random blood
samples showed 2 broad, less distinct bands in contrast to the single
narrow, sharp band in the remainder. Inheritance appears to be
autosomal, a point of particular note. Since the G6PD locus is X-linked,
these 2 functionally related genes do not show clustering. Heterozygotes
and homozygotes showed no quantitative difference in red blood cell 6PGD
activity. Deficiency of this enzyme, with or without electrophoretic
abnormality, has been observed (Parr, 1966). Nevo (1989) identified a
rare PGD variant called PGD Mediterranean. Severe deficiency of 6PGD,
although well-documented (Brewer and Dern, 1964; Dern et al., 1966; Parr
and Fitch, 1967), has never been incriminated as the cause of hemolytic
anemia. In fact, persons with less than 5% of normal activity in red
cell enzymes, who were found in population surveys by Parr and Fitch
(1967), were entirely asymptomatic. Beutler et al. (1985) found
hemolysis in a subject in whom partial deficiency of 6PGD coexisted with
G6PD deficiency, whereas no hemolysis was found in persons with the G6PD
variant alone. A synergism of the 2 enzymopathies is possible.
A possibility of linkage between the Rhesus and 6PGD loci was found by
Weitkamp et al. (1970). This has since been fully confirmed (Weitkamp et
al., 1971). Weitkamp (1972) gave valid criticism of the conclusions of
linkage studies of 2 groups. It is clear, however, that the Rhesus and
6PGD loci are on chromosome 1. Douglas et al. (1973) demonstrated that
the PGM1 and 6PGD loci are on the distal end of the short arm of
chromosome 1. Assuming that each arm of chromosome 1 is 140 male cM
long, Cook et al. (1974) concluded that, measured from the centromere,
map positions are as follows: PGD, 1p124; RH, 1p109; PGM1, 1p079; FY,
1p010; PEPC, 1q030. At HGM8, Povey et al. (1985) concluded that the
smallest region of overlap for PGD is 1p36.2-p36.13.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* SA
Benkmann et al. (1986); Blake and Kirk (1969); Bowman et al. (1966);
Burgerhout et al. (1973); Davidson (1967); Nelson (1982); Ritter
et al. (1971); Tariverdian et al. (1970); Westerveld and Meera Khan
(1972)
*FIELD* RF
1. Benkmann, H.-G.; Paik, Y. K.; Chen, L. Z.; Goedde, H. W.: Polymorphism
of 6-PGD in South Korea: a new genetic variant 6-PGD Korea. Hum.
Genet. 74: 204-205, 1986.
2. Beutler, E.; Kuhl, W.; Gelbart, T.: 6-Phosphogluconolactonase
deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction
with glucose-6-phosphate dehydrogenase deficiency. Proc. Nat. Acad.
Sci. 82: 3876-3878, 1985.
3. Blake, N. M.; Kirk, R. L.: New genetic variant of 6-phosphogluconate
dehydrogenase in Australian aborigines. Nature 221: 278 only, 1969.
4. Bowman, J. E.; Carson, P. E.; Frischer, H.; De Garay, A. L.: Genetics
of starch-gel electrophoretic variants of human 6-phosphogluconic
dehydrogenase: population and family studies in the United States
and in Mexico. Nature 210: 811-812, 1966.
5. Brewer, G. J.; Dern, R. J.: A new inherited enzymatic deficiency
of human erythrocytes: 6-phosphogluconate dehydrogenase deficiency. Am.
J. Hum. Genet. 16: 472-476, 1964.
6. Burgerhout, W.; Van Someren, H.; Bootsma, D.: Cytological mapping
of the genes assigned to the human A1 chromosome by use of radiation-induced
chromosome breakage in a human-Chinese hamster hybrid cell line. Humangenetik 20:
159-162, 1973.
7. Cook, P. J. L.; Robson, E. B.; Buckton, K. E.; Jacobs, P. A.; Polani,
P. E.: Segregation of genetic markers in families with chromosome
polymorphisms and structural rearrangements involving chromosome 1. Ann.
Hum. Genet. 37: 261-274, 1974.
8. Davidson, R. G.: Electrophoretic variants of human 6-phosphogluconate
dehydrogenase: population and family studies and description of a
new variant. Ann. Hum. Genet. 30: 355-362, 1967.
9. Dern, R. J.; Brewer, G. J.; Tashian, R. E.; Shows, T. B.: Hereditary
variation of erythrocytic 6-phosphogluconate dehydrogenase. J. Lab.
Clin. Med. 67: 255-264, 1966.
10. Douglas, G. R.; McAlpine, P. J.; Hamerton, J. L.: Regional localization
of loci for human PGM-1 and 6PGD on human chromosome 1 by use of hybrids
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*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 10/31/2003
carol: 9/29/1998
mimadm: 1/14/1995
warfield: 3/4/1994
supermim: 3/16/1992
carol: 3/4/1992
carol: 8/19/1991
carol: 4/30/1991