LOCUS NP_001003941 427 aa linear PRI 22-OCT-2008
DEFINITION oxoglutarate (alpha-ketoglutarate) dehydrogenase (lipoamide)
isoform 2 precursor [Homo sapiens].
ACCESSION NP_001003941
VERSION NP_001003941.1 GI:51873038
DBSOURCE REFSEQ: accession NM_001003941.1
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 427)
AUTHORS van Bever,Y., Balemans,W., Duval,E.L., Jespers,A., Eyskens,F., van
Hul,W. and Courtens,W.
TITLE Exclusion of OGDH and BMP4 as candidate genes in two siblings with
autosomal recessive DOOR syndrome
JOURNAL Am. J. Med. Genet. A 143 (7), 763-767 (2007)
PUBMED 17343268
REMARK GeneRIF: Association with autosomal recessive DOOR syndrome not
found.
REFERENCE 2 (residues 1 to 427)
AUTHORS Shi,Q., Chen,H.L., Xu,H. and Gibson,G.E.
TITLE Reduction in the E2k subunit of the alpha-ketoglutarate
dehydrogenase complex has effects independent of complex activity
JOURNAL J. Biol. Chem. 280 (12), 10888-10896 (2005)
PUBMED 15649899
REMARK GeneRIF: Reduction in the E2k subunit of the alpha-ketoglutarate
dehydrogenase complex has effects independent of complex activity.
REFERENCE 3 (residues 1 to 427)
AUTHORS Habelhah,H., Laine,A., Erdjument-Bromage,H., Tempst,P.,
Gershwin,M.E., Bowtell,D.D. and Ronai,Z.
TITLE Regulation of 2-oxoglutarate (alpha-ketoglutarate) dehydrogenase
stability by the RING finger ubiquitin ligase Siah
JOURNAL J. Biol. Chem. 279 (51), 53782-53788 (2004)
PUBMED 15466852
REMARK GeneRIF: 2-oxoglutarate (alpha-ketoglutarate) dehydrogenase
stability is regulated by the RING finger ubiquitin ligase Siah
REFERENCE 4 (residues 1 to 427)
AUTHORS McCartney,R.G., Rice,J.E., Sanderson,S.J., Bunik,V., Lindsay,H. and
Lindsay,J.G.
TITLE Subunit interactions in the mammalian alpha-ketoglutarate
dehydrogenase complex. Evidence for direct association of the
alpha-ketoglutarate dehydrogenase and dihydrolipoamide
dehydrogenase components
JOURNAL J. Biol. Chem. 273 (37), 24158-24164 (1998)
PUBMED 9727038
REFERENCE 5 (residues 1 to 427)
AUTHORS Koike,K.
TITLE The gene encoding human 2-oxoglutarate dehydrogenase: structural
organization and mapping to chromosome 7p13-p14
JOURNAL Gene 159 (2), 261-266 (1995)
PUBMED 7622061
REFERENCE 6 (residues 1 to 427)
AUTHORS Szabo,P., Cai,X., Ali,G. and Blass,J.P.
TITLE Localization of the gene (OGDH) coding for the E1k component of the
alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2
JOURNAL Genomics 20 (2), 324-326 (1994)
PUBMED 8020988
REFERENCE 7 (residues 1 to 427)
AUTHORS Koike,K., Urata,Y. and Goto,S.
TITLE Cloning and nucleotide sequence of the cDNA encoding human
2-oxoglutarate dehydrogenase (lipoamide)
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 89 (5), 1963-1967 (1992)
PUBMED 1542694
REFERENCE 8 (residues 1 to 427)
AUTHORS Reed,L.J. and Hackert,M.L.
TITLE Structure-function relationships in dihydrolipoamide
acyltransferases
JOURNAL J. Biol. Chem. 265 (16), 8971-8974 (1990)
PUBMED 2188967
REMARK Review article
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AU140451.1, BC004964.1,
BC009580.1 and BM998792.1.
Summary: This gene encodes one subunit of the 2-oxoglutarate
dehydrogenase complex. This complex catalyzes the overall
conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA
and CO(2) during the Krebs cycle. The protein is located in the
mitocondrial matrix and uses thiamine pyrophosphate as a cofactor.
A congential deficiency in 2-oxoglutarate dehydrogenase activity is
believed to lead to hypotonia, metabolic acidosis, and
hyperlactatemia. [provided by RefSeq].
Transcript Variant: This variant (2) uses an alternate splice site
in the 3' end of coding region, compared to variant 1. Variant 2
encodes isoform 2 which has a shorter and distinct C-terminus,
compared to isoform 1. Variant 2 is supported by transcriptional
evidence although the protein product is predicted.
FEATURES Location/Qualifiers
source 1..427
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="7"
/map="7p14-p13"
Protein 1..427
/product="oxoglutarate (alpha-ketoglutarate) dehydrogenase
(lipoamide) isoform 2 precursor"
/EC_number="1.2.4.2"
/note="oxoglutarate dehydrogenase (lipoamide);
2-oxoglutarate dehydrogenase; oxoglutarate dehydrogenase
(succinyl-transferring); oxoglutarate decarboxylase';
H_DJ0691F11_gi16307008.sp_cds.1"
transit_peptide 1..40
/calculated_mol_wt=4613
mat_peptide 41..427
/product="oxoglutarate (alpha-ketoglutarate) dehydrogenase
isoform 2"
/calculated_mol_wt=43585
CDS 1..427
/gene="OGDH"
/gene_synonym="E1k"
/gene_synonym="OGDC"
/gene_synonym="AKGDH"
/coded_by="NM_001003941.1:110..1393"
/note="isoform 2 precursor is encoded by transcript
variant 2"
/db_xref="GeneID:4967"
/db_xref="HGNC:8124"
/db_xref="MIM:203740"
ORIGIN
1 mfhlrtcaak lrpltasqtv ktfsqnrpaa artfqqircy sapvaaepfl sgtssnyvee
61 mycawlenpk svhkswdiff rntnagappg tayqsplpls rgslaavaha qslveaqpnv
121 dklvedhlav qslirayqir ghhvaqldpl gildadldss vpadiisstd klgfygldes
181 dldkvfhlpt ttfiggqesa lplreiirrl emaycqhigv efmfindleq cqwirqkfet
241 pgimqftnee krtllarlvr strfeeflqr kwssekrfgl egcevlipal ktiidkssen
301 gvdyvimgmp hrgrlnvlan virkeleqif cqfdskleaa degsgdvkyh lgmyhrrinr
361 vtdrnitlsl vanpshleaa dpvvmgktka eqfycgdteg kkvrprerra rqivkapcss
421 mefrspt
//