ID   Q11CV6_CHESB            Unreviewed;       994 AA.
AC   Q11CV6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   OrderedLocusNames=Meso_3398 {ECO:0000313|EMBL:ABG64769.1};
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG64769.1};
RN   [1] {ECO:0000313|EMBL:ABG64769.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BNC1 {ECO:0000313|EMBL:ABG64769.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR   EMBL; CP000390; ABG64769.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11CV6; -.
DR   STRING; 266779.Meso_3398; -.
DR   KEGG; mes:Meso_3398; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABG64769.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          641..834
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   994 AA;  111909 MW;  B869922109BE5894 CRC64;
     MARQNQANED FSITSFLYGG NAAYIEDLYA SYESDPSSVS DDWRTFFSQL KDNAADVKKS
     ARGASWKQKG WPLTANGELV SALDGDWGAL EGNIDLKLKK KAAEGGISLS EAELQRATRD
     SVRAIMMIRA YRMRGHLHAD LDPLGLAKPM EDYNELSPEA YGFTEADFDR PIFIDNVLGL
     ETATIREMLA ILRRTYCSTL GVEFMHISNP EEKAWIQERI EGPDKGVAFT ANGKKAILQK
     LIESEGFEQF LDVKYKGTKR FGLDGSESLI PALEQIIKRG GQLGLKEIVL GMAHRGRLNV
     LSQVMGKPHR AIFHEFKGGS FTPDEVEGSG DVKYHLGASS DREFDGNKVH LSLTANPSHL
     EIVNPVVMGK ARAKQDQLFG RTREEIIPLA ERSRVMPLLI HGDAAFAGQG VVAECLGLSG
     LRGHRVAGTV HVIINNQIGF TTNPRFSRSS PYPSDVAKMI EAPIFHVNGD DPEAVVYAAK
     VATEFRMAFQ KPVVIDMFCY RRFGHNEGDE PAFTQPIMYR TIRSHPTTVE VYSRKLIDEG
     LVTKDDIDQM RAEWRATLEA EFDAGQSYKP NKADWLDGAW SGLKKADDGD EQRRGKTAVP
     VKTLKEIGKK LTEVPADFEV HRTVRRFLEN RKQMIETGEG IDWATAEALA FGSILIEGNP
     VRLSGQDSER GTFSQRHSVL YDQRDENRYI PLNHLGPQQA YYDVINSMLS EEAVLGFEYG
     YSLAEPRALT LWEAQFGDFA NGAQVVFDQF ISSGERKWLR MSGLVCLLPH GYEGQGPEHS
     SARLERFLQL CAEDNMQVAN CTTPANYFHI LRRQLKRDFR KPLILMTPKS LLRHKRAVST
     LAEMSGESTF HRLLWDDAQS LQNQPIKLVK DSKIRRVVMC SGKVYYDLYE EREKRGINDV
     YLLRVEQLYP FPAKALITEL SRFRNAEMVW CQEEPKNMGA WSFIDPYLEW VLQHIEAKNK
     RVRYAGRPAS ASPATGLMSK HLEQLGQLLE DALG
//