ID   Q2K3F2_RHIEC            Unreviewed;       994 AA.
AC   Q2K3F2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
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   Name=sucA {ECO:0000313|EMBL:ABC92634.1};
GN   OrderedLocusNames=RHE_CH03888 {ECO:0000313|EMBL:ABC92634.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC92634.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|EMBL:ABC92634.1, ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC92634.1; -; Genomic_DNA.
DR   RefSeq; WP_011427083.1; NC_007761.1.
DR   AlphaFoldDB; Q2K3F2; -.
DR   KEGG; ret:RHE_CH03888; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000001936; 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   Reference proteome {ECO:0000313|Proteomes:UP000001936};
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;  111397 MW;  63BA434851067435 CRC64;
     MARQEANEQF QITSFLDGAN AAYIEQLYAR YEEDPASVDD QWRAFFKALE DDPADVKKAA
     KGASWRRKNW PLAAGGDLVS ALDGNWGIVE KAIETKVKAK AAAEGKPADS TDVLQATRDS
     VRAIMMIRAY RMRGHLHAKL DPLGIAAAVD DYRELSPENY GFTSADYDRK IFIDNVLGLE
     YATIREMIDI LERTYCSTLG VEFMHISNPE EKAWIQERIE GPDKGVAFTP EGKKAILSKL
     VEAEGYEQFL DVKFKGTKRF GLDGGESLIP ALEQILKRGG HLGLKEAVFG MAHRGRLNVL
     SQVMGKPHRA IFHEFKGGSY APDEVEGSGD VKYHLGASSD REFDGNKVHV SLTANPSHLE
     IVDPVVMGKA RAKQDMSATV WEGDIIPLSE RAKVLPLLIH GDAAFAGQGV IAEILGLSGL
     RGHRVAGTMH VIINNQIGFT TNPAFSRSSP YPSDVAKMIE APILHVNGDD PEAVVYAAKI
     ATEFRMKFHK PVVLDMFCYR RYGHNEGDEP SFTQPKMYKV IRGHKTVLQL YAARLVAEGL
     LTEGEVEKMK ADWRAHLEQE FDAGQHYKPN KADWLDGEWS GLRTADNADE QRRGKTAVPM
     KTLKEIGRKL AEIPAGFNAH RTIQRFMENR ANMIATGEGL DWAMAEALAF GALCLEGHKI
     RLSGQDCERG TFSQRHSVLY DQETEERYIP LANLSPTQAR YEVINSMLSE EAVLGFEYGY
     SLARPNALTL WEAQFGDFAN GAQVVFDQFI SSGERKWLRM SGLVCLLPHG YEGQGPEHSS
     ARLERFLQLC AEDNMQVANV TTPANYFHIL RRQLKRDFRK PLILMTPKSL LRHKRAVSTL
     AELAGESAFH RLLWDDAEVI KDGPIKLQKD NKIRRVVMCS GKVYYDLLEE REKRGIDDIY
     LLRVEQLYPF PAKALINELS RFRNAEMVWC QEEPKNMGAW SFIDPFLEWV LAHIDAKYQR
     VRYTGRPAAA SPATGLMSKH LSQLAAFLED ALGG
//