ID   Q1MAW4_RHIJ3            Unreviewed;      1027 AA.
AC   Q1MAW4;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
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:CAK09921.1};
GN   Synonyms=odhA {ECO:0000313|EMBL:CAK09921.1};
GN   OrderedLocusNames=RL4435 {ECO:0000313|EMBL:CAK09921.1};
OS   Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium
OS   leguminosarum bv. viciae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium;
OC   Rhizobium johnstonii.
OX   NCBI_TaxID=216596 {ECO:0000313|EMBL:CAK09921.1, ECO:0000313|Proteomes:UP000006575};
RN   [1] {ECO:0000313|EMBL:CAK09921.1, ECO:0000313|Proteomes:UP000006575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841 {ECO:0000313|EMBL:CAK09921.1,
RC   ECO:0000313|Proteomes:UP000006575};
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach A.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(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; AM236080; CAK09921.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1MAW4; -.
DR   EnsemblBacteria; CAK09921; CAK09921; RL4435.
DR   KEGG; rle:RL4435; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   Proteomes; UP000006575; 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:CAK09921.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          673..866
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1027 AA;  114973 MW;  7A85EA6EACCB7B80 CRC64;
     MRRGQAAIGM RQPAIKPANS SKSGGGRKRP HNTMARQEAN EQFQITSFLD GANAAYIEQL
     YARYEEDPAS VDDQWRSFFK ALEEDPSDVK RAAKGASWRK KNWPLQASGD LVSALDGDWG
     IVEKVIETKV KAKAEAQGKP ADSTEVLQAT RDSVRAIMMI RAYRMRGHLH AKLDPLGIAA
     SVDDYHELSA ENYGFTAADY DRKIFIDNVL GLEYATIREM IEILERTYCS TLGVEFMHIS
     NPEEKAWIQE RIEGPDKGVA FTPEGKKAIL AKLVEAEGYE QFLDVKFKGT KRFGLDGGES
     LIPALEQILK RGGHLGLKEA VFGMAHRGRL NVLSQVMGKP HRAIFHEFKG GSAAPDEVEG
     SGDVKYHLGA SSDREFDGNK IHVSLTANPS HLEIVDPVVM GKARAKQDMN ATVWDGDIIP
     LSERAKVLPL LIHGDAAFAG QGVIAEILGL SGLRGHRVAG TMHVIINNQI GFTTNPAFSR
     SSPYPSDVAK MIEAPILHVN GDDPEAVVYG AKIATEFRMK FHKPVVLDLF CYRRYGHNEG
     DEPSFTQPKM YKVIRAHKTV LQLYAARLVA EGLLTDGEVE KMKADWRAHL EQEFDAGQHY
     KPNKADWLDG EWSGLRTADN ADEQRRGKTA VPMKTLKEIG RKLSEIPSGF NAHRTIQRFM
     ENRANMIATG EGIDWAMAEA LSFGALCVEG SKIRLSGQDC ERGTFSQRHS VLYDQETEER
     YIPLANLSPT QGRYEVINSM LSEEAVLGFE YGYSLARPNA LTLWEAQFGD FANGAQVVFD
     QFISSGERKW LRMSGLVCLL PHGYEGQGPE HSSARLERFL QLCAEDNMQV ANVTTPANYF
     HILRRQLKRD FRKPLILMTP KSLLRHKRAV STLAEMAGES AFHRLLWDDA EVIKDGPIKL
     QKDNKIRRVV MCSGKVYYDL LEEREKRGID DIYLLRVEQL YPFPAKALIN ELSRFRNAEM
     VWCQEEPKNM GAWSFIDPFL EWVLAHIDAK YQRVRYTGRP AAASPATGLM SKHLSQLAAF
     LEDALGG
//