ID   C6AY62_RHILS            Unreviewed;       994 AA.
AC   C6AY62;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=Rleg_3970 {ECO:0000313|EMBL:ACS58211.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS58211.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS58211.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS58211.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii strain
RT   WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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; CP001622; ACS58211.1; -; Genomic_DNA.
DR   RefSeq; WP_012759276.1; NC_012850.1.
DR   AlphaFoldDB; C6AY62; -.
DR   KEGG; rlg:Rleg_3970; -.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000002256; Chromosome.
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:ACS58211.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          640..833
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   994 AA;  111425 MW;  EF832E00A7D89BF9 CRC64;
     MARQEANEQF QITSFLDGAN AAYIEQLYAL YEEDPASVDD QWRSFFKALE EDPSDVKRAA
     KGASWRKKNW PLQASGDLVS ALDGDWGIVE KVIETKVKAK AEAQGKPADS TEVLQATRDS
     VRAIMMIRAY RMRGHLHAKL DPLGIAAPVD DYHELSAENY GFTAADYDRK IFIDNVLGLE
     YATIREMIEI LERTYCSTLG VEFMHISNPE EKAWIQERIE GPDKGVAFTP EGKKAILAKL
     VEAEGYEQFL DVKFKGTKRF GLDGGESLIP ALEQILKRGG HLGLKEAVFG MAHRGRLNVL
     SQVMGKPHRA IFHEFKGGSA APDEVEGSGD VKYHLGASSD REFDGNKIHV SLTANPSHLE
     IVDPVVMGKA RAKQDMNATV WDGDIIPLSE RAKVLPLLIH GDAAFAGQGV IAEILGLSGL
     RGHRVAGTMH VIINNQIGFT TNPAFSRSSP YPSDVAKMIE APILHVNGDD PEAVVYGAKI
     ATEFRMKFHK PVVLDLFCYR RYGHNEGDEP SFTQPKMYKV IRAHKTVLQL YAARLVAEGL
     LTDGEVEKMK ADWRAHLEQE FEAGQHYKPN KADWLDGEWS GLRTADNADE QRRGKTAVPM
     KTLKEIGRKL SEIPAGFNAH RTIQRFMENR ANMIATGEGI DWAMAEALSF GALCVEGSKI
     RLSGQDCERG TFSQRHSVLY DQETEERYIP LANLSPTQGR YEVINSMLSE EAVLGFEYGY
     SLARPNALTL WEAQFGDFAN GAQVVFDQFI SSGERKWLRM SGLVCLLPHG YEGQGPEHSS
     ARLERFLQLC AEDNMQVANV TTPANYFHIL RRQLKRDFRK PLVLMTPKSL LRHKRAVSTL
     AEMAGESAFH RLLWDDAEVI KDGPIKLQKD NKIRRVVMCS GKVYYDLLEE REKRGIDDIY
     LLRVEQLYPF PAKALINELS RFRNAEMVWC QEEPKNMGAW SFIDPFLEWV LAHIDAKYQR
     VRYTGRPAAA SPATGLMSKH LSQLAAFLED ALGG
//