Full text data of PPCS
PPCS
(COAB)
[Confidence: low (only semi-automatic identification from reviews)]
Phosphopantothenate--cysteine ligase; 6.3.2.5 (Phosphopantothenoylcysteine synthetase; PPC synthetase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphopantothenate--cysteine ligase; 6.3.2.5 (Phosphopantothenoylcysteine synthetase; PPC synthetase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9HAB8
ID PPCS_HUMAN Reviewed; 311 AA.
AC Q9HAB8; Q3KQT2; Q5VVM0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2004, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Phosphopantothenate--cysteine ligase;
DE EC=6.3.2.5;
DE AltName: Full=Phosphopantothenoylcysteine synthetase;
DE Short=PPC synthetase;
GN Name=PPCS; Synonyms=COAB;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Ovary tumor, and Uterus;
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 [4]
RP FUNCTION.
RX PubMed=11923312; DOI=10.1074/jbc.M201708200;
RA Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A.,
RA de Crecy-Lagard V., Osterman A.;
RT "Complete reconstitution of the human coenzyme A biosynthetic pathway
RT via comparative genomics.";
RL J. Biol. Chem. 277:21431-21439(2002).
RN [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, AND HOMODIMERIZATION.
RX PubMed=12906824; DOI=10.1016/S0969-2126(03)00146-1;
RA Manoj N., Strauss E., Begley T.P., Ealick S.E.;
RT "Structure of human phosphopantothenoylcysteine synthetase at 2.3 A
RT resolution.";
RL Structure 11:927-936(2003).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of coenzyme
CC A from vitamin B5, where cysteine is conjugated to 4'-
CC phosphopantothenate to form 4-phosphopantothenoylcysteine.
CC -!- CATALYTIC ACTIVITY: CTP + (R)-4'-phosphopantothenate + L-cysteine
CC = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 2/5.
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HAB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAB8-2; Sequence=VSP_045796;
CC Note=No experimental confirmation available;
CC -!- MISCELLANEOUS: The mammalian enzyme has a preference for ATP over
CC CTP, in contrast to the E.coli ortholog.
CC -!- SIMILARITY: Belongs to the PPC synthetase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13931.1; Type=Frameshift; Positions=282;
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; AK021900; BAB13931.1; ALT_FRAME; mRNA.
DR EMBL; AL445669; CAH70748.1; -; Genomic_DNA.
DR EMBL; AL445669; CAH70749.1; -; Genomic_DNA.
DR EMBL; BC012383; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC104938; AAI04939.1; -; mRNA.
DR EMBL; BC106064; AAI06065.1; -; mRNA.
DR EMBL; BC112015; AAI12016.1; -; mRNA.
DR RefSeq; NP_001070915.1; NM_001077447.1.
DR RefSeq; NP_078940.2; NM_024664.2.
DR RefSeq; XP_005271259.1; XM_005271202.1.
DR RefSeq; XP_005271260.1; XM_005271203.1.
DR UniGene; Hs.706662; -.
DR PDB; 1P9O; X-ray; 2.30 A; A/B=1-311.
DR PDBsum; 1P9O; -.
DR ProteinModelPortal; Q9HAB8; -.
DR SMR; Q9HAB8; 7-307.
DR IntAct; Q9HAB8; 1.
DR STRING; 9606.ENSP00000361642; -.
DR PhosphoSite; Q9HAB8; -.
DR DMDM; 47117318; -.
DR PaxDb; Q9HAB8; -.
DR PRIDE; Q9HAB8; -.
DR Ensembl; ENST00000372561; ENSP00000361642; ENSG00000127125.
DR Ensembl; ENST00000372562; ENSP00000361643; ENSG00000127125.
DR Ensembl; ENST00000455780; ENSP00000389893; ENSG00000127125.
DR GeneID; 79717; -.
DR KEGG; hsa:79717; -.
DR UCSC; uc001chk.3; human.
DR CTD; 79717; -.
DR GeneCards; GC01P042921; -.
DR HGNC; HGNC:25686; PPCS.
DR HPA; HPA031361; -.
DR MIM; 609853; gene.
DR neXtProt; NX_Q9HAB8; -.
DR PharmGKB; PA142671158; -.
DR eggNOG; COG0452; -.
DR HOGENOM; HOG000194726; -.
DR HOVERGEN; HBG049438; -.
DR InParanoid; Q9HAB8; -.
DR KO; K01922; -.
DR OMA; GPSAMFY; -.
DR OrthoDB; EOG7TTQ82; -.
DR PhylomeDB; Q9HAB8; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR UniPathway; UPA00241; UER00353.
DR EvolutionaryTrace; Q9HAB8; -.
DR GeneWiki; Phosphopantothenate%E2%80%94cysteine_ligase; -.
DR GenomeRNAi; 79717; -.
DR NextBio; 69059; -.
DR PRO; PR:Q9HAB8; -.
DR ArrayExpress; Q9HAB8; -.
DR Bgee; Q9HAB8; -.
DR CleanEx; HS_PPCS; -.
DR Genevestigator; Q9HAB8; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015939; P:pantothenate metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.10300; -; 1.
DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
DR Pfam; PF04127; DFP; 2.
DR SUPFAM; SSF102645; SSF102645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Ligase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 311 Phosphopantothenate--cysteine ligase.
FT /FTId=PRO_0000182040.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 173 Missing (in isoform 2).
FT /FTId=VSP_045796.
FT HELIX 19 32
FT STRAND 37 44
FT STRAND 46 52
FT STRAND 54 59
FT HELIX 64 75
FT STRAND 79 85
FT HELIX 93 95
FT HELIX 98 104
FT STRAND 114 121
FT TURN 122 124
FT HELIX 128 141
FT STRAND 144 149
FT HELIX 152 166
FT HELIX 167 172
FT STRAND 173 177
FT STRAND 183 185
FT STRAND 203 206
FT HELIX 211 214
FT HELIX 218 220
FT STRAND 225 231
FT HELIX 236 250
FT STRAND 253 258
FT STRAND 267 271
FT STRAND 274 278
FT HELIX 282 286
FT HELIX 291 306
SQ SEQUENCE 311 AA; 34005 MW; D3B337D3250D7170 CRC64;
MAEMDPVAEF PQPPGAARWA EVMARFAARL GAQGRRVVLV TSGGTKVPLE ARPVRFLDNF
SSGRRGATSA EAFLAAGYGV LFLYRARSAF PYAHRFPPQT WLSALRPSGP ALSGLLSLEA
EENALPGFAE ALRSYQEAAA AGTFLAVEFT TLADYLHLLQ AAAQALNPLG PSAMFYLAAA
VSDFYVPVSE MPEHKIQSSG GPLQITMKMV PKLLSPLVKD WAPKAFIISF KLETDPAIVI
NRARKALEIY QHQVVVANIL ESRQSFVFIV TKDSETKLLL SEEEIEKGVE IEEKIVDNLQ
SRHTAFIGDR N
//
ID PPCS_HUMAN Reviewed; 311 AA.
AC Q9HAB8; Q3KQT2; Q5VVM0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2004, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Phosphopantothenate--cysteine ligase;
DE EC=6.3.2.5;
DE AltName: Full=Phosphopantothenoylcysteine synthetase;
DE Short=PPC synthetase;
GN Name=PPCS; Synonyms=COAB;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Ovary tumor, and Uterus;
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 [4]
RP FUNCTION.
RX PubMed=11923312; DOI=10.1074/jbc.M201708200;
RA Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A.,
RA de Crecy-Lagard V., Osterman A.;
RT "Complete reconstitution of the human coenzyme A biosynthetic pathway
RT via comparative genomics.";
RL J. Biol. Chem. 277:21431-21439(2002).
RN [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, AND HOMODIMERIZATION.
RX PubMed=12906824; DOI=10.1016/S0969-2126(03)00146-1;
RA Manoj N., Strauss E., Begley T.P., Ealick S.E.;
RT "Structure of human phosphopantothenoylcysteine synthetase at 2.3 A
RT resolution.";
RL Structure 11:927-936(2003).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of coenzyme
CC A from vitamin B5, where cysteine is conjugated to 4'-
CC phosphopantothenate to form 4-phosphopantothenoylcysteine.
CC -!- CATALYTIC ACTIVITY: CTP + (R)-4'-phosphopantothenate + L-cysteine
CC = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 2/5.
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HAB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAB8-2; Sequence=VSP_045796;
CC Note=No experimental confirmation available;
CC -!- MISCELLANEOUS: The mammalian enzyme has a preference for ATP over
CC CTP, in contrast to the E.coli ortholog.
CC -!- SIMILARITY: Belongs to the PPC synthetase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13931.1; Type=Frameshift; Positions=282;
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; AK021900; BAB13931.1; ALT_FRAME; mRNA.
DR EMBL; AL445669; CAH70748.1; -; Genomic_DNA.
DR EMBL; AL445669; CAH70749.1; -; Genomic_DNA.
DR EMBL; BC012383; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC104938; AAI04939.1; -; mRNA.
DR EMBL; BC106064; AAI06065.1; -; mRNA.
DR EMBL; BC112015; AAI12016.1; -; mRNA.
DR RefSeq; NP_001070915.1; NM_001077447.1.
DR RefSeq; NP_078940.2; NM_024664.2.
DR RefSeq; XP_005271259.1; XM_005271202.1.
DR RefSeq; XP_005271260.1; XM_005271203.1.
DR UniGene; Hs.706662; -.
DR PDB; 1P9O; X-ray; 2.30 A; A/B=1-311.
DR PDBsum; 1P9O; -.
DR ProteinModelPortal; Q9HAB8; -.
DR SMR; Q9HAB8; 7-307.
DR IntAct; Q9HAB8; 1.
DR STRING; 9606.ENSP00000361642; -.
DR PhosphoSite; Q9HAB8; -.
DR DMDM; 47117318; -.
DR PaxDb; Q9HAB8; -.
DR PRIDE; Q9HAB8; -.
DR Ensembl; ENST00000372561; ENSP00000361642; ENSG00000127125.
DR Ensembl; ENST00000372562; ENSP00000361643; ENSG00000127125.
DR Ensembl; ENST00000455780; ENSP00000389893; ENSG00000127125.
DR GeneID; 79717; -.
DR KEGG; hsa:79717; -.
DR UCSC; uc001chk.3; human.
DR CTD; 79717; -.
DR GeneCards; GC01P042921; -.
DR HGNC; HGNC:25686; PPCS.
DR HPA; HPA031361; -.
DR MIM; 609853; gene.
DR neXtProt; NX_Q9HAB8; -.
DR PharmGKB; PA142671158; -.
DR eggNOG; COG0452; -.
DR HOGENOM; HOG000194726; -.
DR HOVERGEN; HBG049438; -.
DR InParanoid; Q9HAB8; -.
DR KO; K01922; -.
DR OMA; GPSAMFY; -.
DR OrthoDB; EOG7TTQ82; -.
DR PhylomeDB; Q9HAB8; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR UniPathway; UPA00241; UER00353.
DR EvolutionaryTrace; Q9HAB8; -.
DR GeneWiki; Phosphopantothenate%E2%80%94cysteine_ligase; -.
DR GenomeRNAi; 79717; -.
DR NextBio; 69059; -.
DR PRO; PR:Q9HAB8; -.
DR ArrayExpress; Q9HAB8; -.
DR Bgee; Q9HAB8; -.
DR CleanEx; HS_PPCS; -.
DR Genevestigator; Q9HAB8; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015939; P:pantothenate metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.10300; -; 1.
DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
DR Pfam; PF04127; DFP; 2.
DR SUPFAM; SSF102645; SSF102645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Ligase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 311 Phosphopantothenate--cysteine ligase.
FT /FTId=PRO_0000182040.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 173 Missing (in isoform 2).
FT /FTId=VSP_045796.
FT HELIX 19 32
FT STRAND 37 44
FT STRAND 46 52
FT STRAND 54 59
FT HELIX 64 75
FT STRAND 79 85
FT HELIX 93 95
FT HELIX 98 104
FT STRAND 114 121
FT TURN 122 124
FT HELIX 128 141
FT STRAND 144 149
FT HELIX 152 166
FT HELIX 167 172
FT STRAND 173 177
FT STRAND 183 185
FT STRAND 203 206
FT HELIX 211 214
FT HELIX 218 220
FT STRAND 225 231
FT HELIX 236 250
FT STRAND 253 258
FT STRAND 267 271
FT STRAND 274 278
FT HELIX 282 286
FT HELIX 291 306
SQ SEQUENCE 311 AA; 34005 MW; D3B337D3250D7170 CRC64;
MAEMDPVAEF PQPPGAARWA EVMARFAARL GAQGRRVVLV TSGGTKVPLE ARPVRFLDNF
SSGRRGATSA EAFLAAGYGV LFLYRARSAF PYAHRFPPQT WLSALRPSGP ALSGLLSLEA
EENALPGFAE ALRSYQEAAA AGTFLAVEFT TLADYLHLLQ AAAQALNPLG PSAMFYLAAA
VSDFYVPVSE MPEHKIQSSG GPLQITMKMV PKLLSPLVKD WAPKAFIISF KLETDPAIVI
NRARKALEIY QHQVVVANIL ESRQSFVFIV TKDSETKLLL SEEEIEKGVE IEEKIVDNLQ
SRHTAFIGDR N
//
MIM
609853
*RECORD*
*FIELD* NO
609853
*FIELD* TI
*609853 PHOSPHOPANTOTHENOYLCYSTEINE SYNTHETASE; PPCS
*FIELD* TX
DESCRIPTION
Biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5) is
read morean essential universal pathway in prokaryotes and eukaryotes. PPCS (EC
6.3.2.5), one of the last enzymes in this pathway, converts
phosphopantothenate to phosphopantothenoylcysteine (Daugherty et al.,
2002).
CLONING
By searching for sequences similar to PPCS from Streptococcus
pneumoniae, followed by PCR of a brain cDNA library, Daugherty et al.
(2002) cloned human PPCS.
GENE FUNCTION
Daugherty et al. (2002) showed that recombinant PPCS functioned within
the CoA synthetic pathway. PPCS used ATP for the activation of substrate
in the ligation reaction 4 times more efficiently than CTP. Daugherty et
al. (2002) verified the function of PPCS by complementation in E. coli.
Incubation of PPCS, PPCDC (609854), and the bifunctional enzyme COASY
(609855) with the necessary substrates and cofactors reconstituted the
4-step biochemical transformation of phosphopantothenate to CoA.
MAPPING
By genomic sequence analysis, Daugherty et al. (2002) mapped the PPCS
gene to chromosome 1.
*FIELD* RF
1. Daugherty, M.; Polanuyer, B.; Farrell, M.; Scholle, M.; Lykidis,
A.; de Crecy-Lagard, V.; Osterman, A.: Complete reconstitution of
the human coenzyme A biosynthetic pathway via comparative genomics. J.
Biol. Chem. 277: 21431-21439, 2002.
*FIELD* CD
Patricia A. Hartz: 1/27/2006
*FIELD* ED
mgross: 01/27/2006
*RECORD*
*FIELD* NO
609853
*FIELD* TI
*609853 PHOSPHOPANTOTHENOYLCYSTEINE SYNTHETASE; PPCS
*FIELD* TX
DESCRIPTION
Biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5) is
read morean essential universal pathway in prokaryotes and eukaryotes. PPCS (EC
6.3.2.5), one of the last enzymes in this pathway, converts
phosphopantothenate to phosphopantothenoylcysteine (Daugherty et al.,
2002).
CLONING
By searching for sequences similar to PPCS from Streptococcus
pneumoniae, followed by PCR of a brain cDNA library, Daugherty et al.
(2002) cloned human PPCS.
GENE FUNCTION
Daugherty et al. (2002) showed that recombinant PPCS functioned within
the CoA synthetic pathway. PPCS used ATP for the activation of substrate
in the ligation reaction 4 times more efficiently than CTP. Daugherty et
al. (2002) verified the function of PPCS by complementation in E. coli.
Incubation of PPCS, PPCDC (609854), and the bifunctional enzyme COASY
(609855) with the necessary substrates and cofactors reconstituted the
4-step biochemical transformation of phosphopantothenate to CoA.
MAPPING
By genomic sequence analysis, Daugherty et al. (2002) mapped the PPCS
gene to chromosome 1.
*FIELD* RF
1. Daugherty, M.; Polanuyer, B.; Farrell, M.; Scholle, M.; Lykidis,
A.; de Crecy-Lagard, V.; Osterman, A.: Complete reconstitution of
the human coenzyme A biosynthetic pathway via comparative genomics. J.
Biol. Chem. 277: 21431-21439, 2002.
*FIELD* CD
Patricia A. Hartz: 1/27/2006
*FIELD* ED
mgross: 01/27/2006