Full text data of OGDH
OGDH
[Confidence: low (only semi-automatic identification from reviews)]
2-oxoglutarate dehydrogenase, mitochondrial; 1.2.4.2 (2-oxoglutarate dehydrogenase complex component E1; OGDC-E1; Alpha-ketoglutarate dehydrogenase; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
2-oxoglutarate dehydrogenase, mitochondrial; 1.2.4.2 (2-oxoglutarate dehydrogenase complex component E1; OGDC-E1; Alpha-ketoglutarate dehydrogenase; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q02218
ID ODO1_HUMAN Reviewed; 1023 AA.
AC Q02218; B4E2U9; D3DVL0; E9PBM1; Q96DD3; Q9UDX0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-NOV-2007, sequence version 3.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial;
DE EC=1.2.4.2;
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE Short=OGDC-E1;
DE AltName: Full=Alpha-ketoglutarate dehydrogenase;
DE Flags: Precursor;
GN Name=OGDH;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1542694; DOI=10.1073/pnas.89.5.1963;
RA Koike K., Urata Y., Goto S.;
RT "Cloning and nucleotide sequence of the cDNA encoding human 2-
RT oxoglutarate dehydrogenase (lipoamide).";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1963-1967(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=7622061; DOI=10.1016/0378-1119(95)00086-L;
RA Koike K.;
RT "The gene encoding human 2-oxoglutarate dehydrogenase: structural
RT organization and mapping to chromosome 7p13-p14.";
RL Gene 159:261-266(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Bone marrow, and Muscle;
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 [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-534, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-970, AND MASS 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 [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 932-940 IN COMPLEX WITH H-2
RP CLASS I HISTOCOMPATIBILITY COMPLEX.
RX PubMed=18973345; DOI=10.1021/bi801349g;
RA Jones L.L., Colf L.A., Bankovich A.J., Stone J.D., Gao Y.G.,
RA Chan C.M., Huang R.H., Garcia K.C., Kranz D.M.;
RT "Different thermodynamic binding mechanisms and peptide fine
RT specificities associated with a panel of structurally similar high-
RT affinity T cell receptors.";
RL Biochemistry 47:12398-12408(2008).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: 2-
CC oxoglutarate dehydrogenase (E1), dihydrolipoamide
CC succinyltransferase (E2) and lipoamide dehydrogenase (E3).
CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC -!- COFACTOR: Thiamine pyrophosphate.
CC -!- ENZYME REGULATION: Catabolite repressed.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q02218-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02218-2; Sequence=VSP_042313;
CC Name=3;
CC IsoId=Q02218-3; Sequence=VSP_043628, VSP_043629;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01393.1; Type=Frameshift; Positions=1003;
CC Sequence=BAA06836.1; Type=Frameshift; Positions=1003;
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-ketoglutarate
CC dehydrogenase entry;
CC URL="http://en.wikipedia.org/wiki/Alpha-ketoglutarate_dehydrogenase";
CC -----------------------------------------------------------------------
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DR EMBL; D10523; BAA01393.1; ALT_FRAME; mRNA.
DR EMBL; D32064; BAA06836.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AK304439; BAG65261.1; -; mRNA.
DR EMBL; AC004859; AAQ96884.1; -; Genomic_DNA.
DR EMBL; AC004859; AAQ96885.1; -; Genomic_DNA.
DR EMBL; AC011894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471128; EAW61086.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61087.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61089.1; -; Genomic_DNA.
DR EMBL; BC004964; AAH04964.1; -; mRNA.
DR EMBL; BC009580; AAH09580.1; -; mRNA.
DR EMBL; BC014617; AAH14617.1; -; mRNA.
DR PIR; A38234; A38234.
DR RefSeq; NP_001003941.1; NM_001003941.2.
DR RefSeq; NP_001158508.1; NM_001165036.1.
DR RefSeq; NP_002532.2; NM_002541.3.
DR UniGene; Hs.488181; -.
DR PDB; 3ERY; X-ray; 1.95 A; P/Q=932-940.
DR PDBsum; 3ERY; -.
DR ProteinModelPortal; Q02218; -.
DR SMR; Q02218; 130-1014.
DR IntAct; Q02218; 7.
DR MINT; MINT-1437057; -.
DR STRING; 9606.ENSP00000222673; -.
DR ChEMBL; CHEMBL2816; -.
DR DrugBank; DB00157; NADH.
DR PhosphoSite; Q02218; -.
DR DMDM; 160332299; -.
DR REPRODUCTION-2DPAGE; IPI00098902; -.
DR PaxDb; Q02218; -.
DR PRIDE; Q02218; -.
DR DNASU; 4967; -.
DR Ensembl; ENST00000222673; ENSP00000222673; ENSG00000105953.
DR Ensembl; ENST00000443864; ENSP00000388084; ENSG00000105953.
DR Ensembl; ENST00000449767; ENSP00000392878; ENSG00000105953.
DR GeneID; 4967; -.
DR KEGG; hsa:4967; -.
DR UCSC; uc003tln.3; human.
DR CTD; 4967; -.
DR GeneCards; GC07P044646; -.
DR HGNC; HGNC:8124; OGDH.
DR HPA; HPA019514; -.
DR HPA; HPA020347; -.
DR MIM; 613022; gene.
DR neXtProt; NX_Q02218; -.
DR Orphanet; 31; Oxoglutaricaciduria.
DR PharmGKB; PA31910; -.
DR eggNOG; COG0567; -.
DR HOGENOM; HOG000259586; -.
DR HOVERGEN; HBG001892; -.
DR InParanoid; Q02218; -.
DR KO; K00164; -.
DR PhylomeDB; Q02218; -.
DR BioCyc; MetaCyc:HS02832-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; OGDH; human.
DR EvolutionaryTrace; Q02218; -.
DR GeneWiki; OGDH; -.
DR GenomeRNAi; 4967; -.
DR NextBio; 19110; -.
DR PMAP-CutDB; Q02218; -.
DR PRO; PR:Q02218; -.
DR ArrayExpress; Q02218; -.
DR Bgee; Q02218; -.
DR CleanEx; HS_OGDH; -.
DR Genevestigator; Q02218; -.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
DR GO; GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; IEA:Ensembl.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0021695; P:cerebellar cortex development; IEA:Ensembl.
DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; IEA:Ensembl.
DR GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:Ensembl.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
DR GO; GO:0021794; P:thalamus development; IEA:Ensembl.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152; PTHR23152; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Glycolysis; Isopeptide bond; Mitochondrion; Oxidoreductase;
KW Polymorphism; Reference proteome; Thiamine pyrophosphate;
KW Transit peptide; Ubl conjugation.
FT TRANSIT 1 40 Mitochondrion.
FT CHAIN 41 1023 2-oxoglutarate dehydrogenase,
FT mitochondrial.
FT /FTId=PRO_0000020432.
FT MOD_RES 401 401 N6-acetyllysine (By similarity).
FT MOD_RES 970 970 N6-acetyllysine.
FT CROSSLNK 534 534 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 139 172 IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRG
FT HHIAKLDPLGISCVNFDDAPVTVSSNV (in isoform
FT 2).
FT /FTId=VSP_042313.
FT VAR_SEQ 404 427 MSILLHGDAAFAGQGIVYETFHLS -> RPRERRARQIVKA
FT PCSSMEFRSPT (in isoform 3).
FT /FTId=VSP_043628.
FT VAR_SEQ 428 1023 Missing (in isoform 3).
FT /FTId=VSP_043629.
FT VARIANT 1018 1018 V -> I (in dbSNP:rs2070607).
FT /FTId=VAR_050435.
FT CONFLICT 730 733 LGFA -> AGLR (in Ref. 1; BAA01393 and 2;
FT BAA06836).
FT CONFLICT 755 755 Q -> L (in Ref. 3; BAG65261).
FT CONFLICT 831 831 N -> D (in Ref. 2; BAA06836).
FT CONFLICT 989 989 D -> N (in Ref. 1; BAA01393 and 2;
FT BAA06836).
SQ SEQUENCE 1023 AA; 115935 MW; F428DD342F232E7C CRC64;
MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES
DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH LGMYHRRINR
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
EAVMYVCKVA AEWRSTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
AELLVSQGVV NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR
SMSCPSTGLT EDILTHIGNV ASSVPVENFT IHGGLSRILK TRGEMVKNRT VDWALAEYMA
FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH
VLRRQILLPF RKPLIIFTPK SLLRHPEARS SFDEMLPGTH FQRVIPEDGP AAQNPENVKR
LLFCTGKVYY DLTRERKARD MVGQVAITRI EQLSPFPFDL LLKEVQKYPN AELAWCQEEH
KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK THLTELQRLL DTAFDLDVFK
NFS
//
ID ODO1_HUMAN Reviewed; 1023 AA.
AC Q02218; B4E2U9; D3DVL0; E9PBM1; Q96DD3; Q9UDX0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-NOV-2007, sequence version 3.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial;
DE EC=1.2.4.2;
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE Short=OGDC-E1;
DE AltName: Full=Alpha-ketoglutarate dehydrogenase;
DE Flags: Precursor;
GN Name=OGDH;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1542694; DOI=10.1073/pnas.89.5.1963;
RA Koike K., Urata Y., Goto S.;
RT "Cloning and nucleotide sequence of the cDNA encoding human 2-
RT oxoglutarate dehydrogenase (lipoamide).";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1963-1967(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=7622061; DOI=10.1016/0378-1119(95)00086-L;
RA Koike K.;
RT "The gene encoding human 2-oxoglutarate dehydrogenase: structural
RT organization and mapping to chromosome 7p13-p14.";
RL Gene 159:261-266(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Bone marrow, and Muscle;
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 [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-534, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-970, AND MASS 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 [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 932-940 IN COMPLEX WITH H-2
RP CLASS I HISTOCOMPATIBILITY COMPLEX.
RX PubMed=18973345; DOI=10.1021/bi801349g;
RA Jones L.L., Colf L.A., Bankovich A.J., Stone J.D., Gao Y.G.,
RA Chan C.M., Huang R.H., Garcia K.C., Kranz D.M.;
RT "Different thermodynamic binding mechanisms and peptide fine
RT specificities associated with a panel of structurally similar high-
RT affinity T cell receptors.";
RL Biochemistry 47:12398-12408(2008).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: 2-
CC oxoglutarate dehydrogenase (E1), dihydrolipoamide
CC succinyltransferase (E2) and lipoamide dehydrogenase (E3).
CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC -!- COFACTOR: Thiamine pyrophosphate.
CC -!- ENZYME REGULATION: Catabolite repressed.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q02218-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02218-2; Sequence=VSP_042313;
CC Name=3;
CC IsoId=Q02218-3; Sequence=VSP_043628, VSP_043629;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01393.1; Type=Frameshift; Positions=1003;
CC Sequence=BAA06836.1; Type=Frameshift; Positions=1003;
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-ketoglutarate
CC dehydrogenase entry;
CC URL="http://en.wikipedia.org/wiki/Alpha-ketoglutarate_dehydrogenase";
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; D10523; BAA01393.1; ALT_FRAME; mRNA.
DR EMBL; D32064; BAA06836.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AK304439; BAG65261.1; -; mRNA.
DR EMBL; AC004859; AAQ96884.1; -; Genomic_DNA.
DR EMBL; AC004859; AAQ96885.1; -; Genomic_DNA.
DR EMBL; AC011894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471128; EAW61086.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61087.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61089.1; -; Genomic_DNA.
DR EMBL; BC004964; AAH04964.1; -; mRNA.
DR EMBL; BC009580; AAH09580.1; -; mRNA.
DR EMBL; BC014617; AAH14617.1; -; mRNA.
DR PIR; A38234; A38234.
DR RefSeq; NP_001003941.1; NM_001003941.2.
DR RefSeq; NP_001158508.1; NM_001165036.1.
DR RefSeq; NP_002532.2; NM_002541.3.
DR UniGene; Hs.488181; -.
DR PDB; 3ERY; X-ray; 1.95 A; P/Q=932-940.
DR PDBsum; 3ERY; -.
DR ProteinModelPortal; Q02218; -.
DR SMR; Q02218; 130-1014.
DR IntAct; Q02218; 7.
DR MINT; MINT-1437057; -.
DR STRING; 9606.ENSP00000222673; -.
DR ChEMBL; CHEMBL2816; -.
DR DrugBank; DB00157; NADH.
DR PhosphoSite; Q02218; -.
DR DMDM; 160332299; -.
DR REPRODUCTION-2DPAGE; IPI00098902; -.
DR PaxDb; Q02218; -.
DR PRIDE; Q02218; -.
DR DNASU; 4967; -.
DR Ensembl; ENST00000222673; ENSP00000222673; ENSG00000105953.
DR Ensembl; ENST00000443864; ENSP00000388084; ENSG00000105953.
DR Ensembl; ENST00000449767; ENSP00000392878; ENSG00000105953.
DR GeneID; 4967; -.
DR KEGG; hsa:4967; -.
DR UCSC; uc003tln.3; human.
DR CTD; 4967; -.
DR GeneCards; GC07P044646; -.
DR HGNC; HGNC:8124; OGDH.
DR HPA; HPA019514; -.
DR HPA; HPA020347; -.
DR MIM; 613022; gene.
DR neXtProt; NX_Q02218; -.
DR Orphanet; 31; Oxoglutaricaciduria.
DR PharmGKB; PA31910; -.
DR eggNOG; COG0567; -.
DR HOGENOM; HOG000259586; -.
DR HOVERGEN; HBG001892; -.
DR InParanoid; Q02218; -.
DR KO; K00164; -.
DR PhylomeDB; Q02218; -.
DR BioCyc; MetaCyc:HS02832-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; OGDH; human.
DR EvolutionaryTrace; Q02218; -.
DR GeneWiki; OGDH; -.
DR GenomeRNAi; 4967; -.
DR NextBio; 19110; -.
DR PMAP-CutDB; Q02218; -.
DR PRO; PR:Q02218; -.
DR ArrayExpress; Q02218; -.
DR Bgee; Q02218; -.
DR CleanEx; HS_OGDH; -.
DR Genevestigator; Q02218; -.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
DR GO; GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; IEA:Ensembl.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0021695; P:cerebellar cortex development; IEA:Ensembl.
DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; IEA:Ensembl.
DR GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:Ensembl.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
DR GO; GO:0021794; P:thalamus development; IEA:Ensembl.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152; PTHR23152; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Glycolysis; Isopeptide bond; Mitochondrion; Oxidoreductase;
KW Polymorphism; Reference proteome; Thiamine pyrophosphate;
KW Transit peptide; Ubl conjugation.
FT TRANSIT 1 40 Mitochondrion.
FT CHAIN 41 1023 2-oxoglutarate dehydrogenase,
FT mitochondrial.
FT /FTId=PRO_0000020432.
FT MOD_RES 401 401 N6-acetyllysine (By similarity).
FT MOD_RES 970 970 N6-acetyllysine.
FT CROSSLNK 534 534 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 139 172 IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRG
FT HHIAKLDPLGISCVNFDDAPVTVSSNV (in isoform
FT 2).
FT /FTId=VSP_042313.
FT VAR_SEQ 404 427 MSILLHGDAAFAGQGIVYETFHLS -> RPRERRARQIVKA
FT PCSSMEFRSPT (in isoform 3).
FT /FTId=VSP_043628.
FT VAR_SEQ 428 1023 Missing (in isoform 3).
FT /FTId=VSP_043629.
FT VARIANT 1018 1018 V -> I (in dbSNP:rs2070607).
FT /FTId=VAR_050435.
FT CONFLICT 730 733 LGFA -> AGLR (in Ref. 1; BAA01393 and 2;
FT BAA06836).
FT CONFLICT 755 755 Q -> L (in Ref. 3; BAG65261).
FT CONFLICT 831 831 N -> D (in Ref. 2; BAA06836).
FT CONFLICT 989 989 D -> N (in Ref. 1; BAA01393 and 2;
FT BAA06836).
SQ SEQUENCE 1023 AA; 115935 MW; F428DD342F232E7C CRC64;
MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES
DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH LGMYHRRINR
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
EAVMYVCKVA AEWRSTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
AELLVSQGVV NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR
SMSCPSTGLT EDILTHIGNV ASSVPVENFT IHGGLSRILK TRGEMVKNRT VDWALAEYMA
FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH
VLRRQILLPF RKPLIIFTPK SLLRHPEARS SFDEMLPGTH FQRVIPEDGP AAQNPENVKR
LLFCTGKVYY DLTRERKARD MVGQVAITRI EQLSPFPFDL LLKEVQKYPN AELAWCQEEH
KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK THLTELQRLL DTAFDLDVFK
NFS
//
MIM
613022
*RECORD*
*FIELD* NO
613022
*FIELD* TI
*613022 OXOGLUTARATE DEHYDROGENASE; OGDH
;;ALPHA-KETOGLUTARATE DEHYDROGENASE; AKGDH;;
read moreE1K
*FIELD* TX
DESCRIPTION
The alpha-ketoglutarate dehydrogenase complex is a multienzyme complex
consisting of 3 protein subunits, oxoglutarate dehydrogenase, also known
as alpha-ketoglutarate dehydrogenase or E1k (EC 1.2.4.2.), dihydrolipoyl
succinyltransferase (DLST, or E2k; 126063), and dihydrolipoyl
dehydrogenase (DLD, or E3; 238331). The complex catalyzes a key reaction
in the Krebs tricarboxylic acid cycle (summary by Szabo et al., 1994).
CLONING
Koike et al. (1992) cloned a human OGDH cDNA from a fetal liver cDNA
library. The ORF encodes a presequence of 40 amino acids and a mature
protein of 963 amino acids with a molecular mass of 108,642 daltons. It
is located in mitochondria within the inner membrane/matrix compartment.
GENE STRUCTURE
Koike (1995) found that the human OGDH gene contains 22 exons spanning
approximately 85 kb. All exon/intron splice junctions follow the GT/AG
rule. Primary extension analysis showed that the OGDH transcription
start point is a thymine residue 55 bp upstream from the ATG start
codon. The 5-prime-flanking region lacked canonical TATA or CAAT boxes.
MAPPING
Using 2 human/rodent somatic cell hybrid panels, Szabo et al. (1994)
mapped the OGDH gene to 7p13-p11.2. A second related sequence, possibly
a pseudogene, was identified and mapped to chromosome 10.
Using DNAs from human/rodent somatic cell hybrids in conjunction with
fluorescence in situ hybridization, Koike (1995) assigned the OGDH gene
to the boundary between bands 7p13 and 7p14.
GENE FUNCTION
Oxoglutarate dehydrogenase is a component of the enzyme complex that
catalyzes the conversion of 2-oxoglutarate to succinyl coenzyme A (Koike
et al., 1992).
Szabo et al. (1994) pointed to a possible significance to the finding of
a reduction in the activity of this complex in Alzheimer disease brain
and cultured skin fibroblasts from Alzheimer disease patients.
See 203740 for a discussion of alpha-ketoglutarate dehydrogenase
deficiency.
*FIELD* RF
1. Koike, K.: The gene encoding human 2-oxoglutarate dehydrogenase:
structural organization and mapping to chromosome 7p13-p14. Gene 159:
261-266, 1995.
2. Koike, K.; Urata, Y.; Goto, S.: Cloning and nucleotide sequence
of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide). Proc.
Nat. Acad. Sci. 89: 1963-1967, 1992.
3. Szabo, P.; Cai, X.; Ali, G.; Blass, J. P.: Localization of the
gene (OGDH) coding for the E1k component of the alpha-ketoglutarate
dehydrogenase complex to chromosome 7p13-p11.2. Genomics 20: 324-326,
1994.
*FIELD* CD
Carol A. Bocchini: 9/18/2009
*FIELD* ED
carol: 12/21/2011
carol: 12/8/2011
carol: 9/18/2009
*RECORD*
*FIELD* NO
613022
*FIELD* TI
*613022 OXOGLUTARATE DEHYDROGENASE; OGDH
;;ALPHA-KETOGLUTARATE DEHYDROGENASE; AKGDH;;
read moreE1K
*FIELD* TX
DESCRIPTION
The alpha-ketoglutarate dehydrogenase complex is a multienzyme complex
consisting of 3 protein subunits, oxoglutarate dehydrogenase, also known
as alpha-ketoglutarate dehydrogenase or E1k (EC 1.2.4.2.), dihydrolipoyl
succinyltransferase (DLST, or E2k; 126063), and dihydrolipoyl
dehydrogenase (DLD, or E3; 238331). The complex catalyzes a key reaction
in the Krebs tricarboxylic acid cycle (summary by Szabo et al., 1994).
CLONING
Koike et al. (1992) cloned a human OGDH cDNA from a fetal liver cDNA
library. The ORF encodes a presequence of 40 amino acids and a mature
protein of 963 amino acids with a molecular mass of 108,642 daltons. It
is located in mitochondria within the inner membrane/matrix compartment.
GENE STRUCTURE
Koike (1995) found that the human OGDH gene contains 22 exons spanning
approximately 85 kb. All exon/intron splice junctions follow the GT/AG
rule. Primary extension analysis showed that the OGDH transcription
start point is a thymine residue 55 bp upstream from the ATG start
codon. The 5-prime-flanking region lacked canonical TATA or CAAT boxes.
MAPPING
Using 2 human/rodent somatic cell hybrid panels, Szabo et al. (1994)
mapped the OGDH gene to 7p13-p11.2. A second related sequence, possibly
a pseudogene, was identified and mapped to chromosome 10.
Using DNAs from human/rodent somatic cell hybrids in conjunction with
fluorescence in situ hybridization, Koike (1995) assigned the OGDH gene
to the boundary between bands 7p13 and 7p14.
GENE FUNCTION
Oxoglutarate dehydrogenase is a component of the enzyme complex that
catalyzes the conversion of 2-oxoglutarate to succinyl coenzyme A (Koike
et al., 1992).
Szabo et al. (1994) pointed to a possible significance to the finding of
a reduction in the activity of this complex in Alzheimer disease brain
and cultured skin fibroblasts from Alzheimer disease patients.
See 203740 for a discussion of alpha-ketoglutarate dehydrogenase
deficiency.
*FIELD* RF
1. Koike, K.: The gene encoding human 2-oxoglutarate dehydrogenase:
structural organization and mapping to chromosome 7p13-p14. Gene 159:
261-266, 1995.
2. Koike, K.; Urata, Y.; Goto, S.: Cloning and nucleotide sequence
of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide). Proc.
Nat. Acad. Sci. 89: 1963-1967, 1992.
3. Szabo, P.; Cai, X.; Ali, G.; Blass, J. P.: Localization of the
gene (OGDH) coding for the E1k component of the alpha-ketoglutarate
dehydrogenase complex to chromosome 7p13-p11.2. Genomics 20: 324-326,
1994.
*FIELD* CD
Carol A. Bocchini: 9/18/2009
*FIELD* ED
carol: 12/21/2011
carol: 12/8/2011
carol: 9/18/2009