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Database: UniProt/SWISS-PROT
Entry: ODO1_GEOSW
LinkDB: ODO1_GEOSW
Original site: ODO1_GEOSW 
ID   ODO1_GEOSW              Reviewed;         952 AA.
AC   C5D802;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   10-OCT-2018, entry version 54.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE            EC=1.2.4.2 {ECO:0000255|HAMAP-Rule:MF_01169};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Name=odhA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   OrderedLocusNames=GWCH70_0919;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01169}.
DR   EMBL; CP001638; ACS23783.1; -; Genomic_DNA.
DR   RefSeq; WP_015863262.1; NC_012793.1.
DR   ProteinModelPortal; C5D802; -.
DR   SMR; C5D802; -.
DR   STRING; 471223.GWCH70_0919; -.
DR   EnsemblBacteria; ACS23783; ACS23783; GWCH70_0919.
DR   KEGG; gwc:GWCH70_0919; -.
DR   eggNOG; ENOG4105C7P; Bacteria.
DR   eggNOG; COG0567; LUCA.
DR   HOGENOM; HOG000259588; -.
DR   KO; K00164; -.
DR   OMA; IDMVCYR; -.
DR   OrthoDB; POG091H03SK; -.
DR   Proteomes; UP000002386; Chromosome.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    952       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_1000213736.
SQ   SEQUENCE   952 AA;  108481 MW;  D00671DCFA511D3B CRC64;
     MTKQTMNYAE PWSQFYGPNL GYVMEMYEQY LEDPDSVDPE LKQLFKEWGA PTTEAERFDH
     SESAAKTYQT FRLPENPTIF SKLVAAVKLA DKIRHYGHLA ADINPLNTQN KDTRRIELSE
     FDLTEDDLKQ IPVAFICPHA PAHVKNGLDA INHLRKIYTD KIAFEFSQVH NLEERNWLIS
     QIESGAYYPS LTNEEKVALL RRLTEVEGFE KFLHRTFVGQ KRFSIEGLDS MVPLLDELIR
     HSIEEEVKAV NIGMAHRGRL NVLAHVLGKP YEMIFAEFQH AESKDFMPSE GSVAITYGWT
     GDVKYHLGAA RRLRNKNEHT MRITLANNPS HLEVVNPVVL GFTRAAQEDR SNAGVPSQDT
     DSAFAIMIHG DAAFPGQGIV AETLNLSRLQ GYQTGGSIHI IANNMIGFTT ESYDSRSTKY
     ASDIAKGFEI PIVHVNADDP EACLAAANLA FAYRKRFKKD FVIDLIGYRR FGHNEMDEPM
     ATNPTMYSII QQHPTVRQLY AQKLIEKGII TKEAVEEMER EVAERLKIAY EKVPKDESKL
     DFIMDPPKPV ASKLPFVKTS VEKDVLRRLN KELLQFPSDF HVFNKLERIL KRREGVFDGK
     GKIDWAHAEI LAFATILRDG VPIRLTGQDS QRGTFAQRHL VLHDMKTGEE FVPLHHISDA
     NASFVVYNSP LTEAAVLGYE YGYNVFAPET LVLWEAQFGD FANMAQVMFD QFISSGRAKW
     GQKSGLVMLL PHGYEGQGPE HSSGRLERFL QLAAENNWTV ANLSTAAQYF HILRRQAGIL
     QREEVRPLVL MTPKSLLRHP LAASDVEEFT NGQFHPVIEQ KGLGENREKV ERIILCTGKF
     AIDLAEQINK MEGLDWLHIV RVEELYPFPK EELQAIFARY PNVKEIIWAQ EEPKNMGSWC
     YVEPKLREIA PDEVDVSYIG RRRRASPAEG DPVVHRKEQE RIIQCALTKK EQ
//
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