ID   I3XDY6_SINF2            Unreviewed;       998 AA.
AC   I3XDY6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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:AFL54092.1};
GN   ORFNames=USDA257_c55770 {ECO:0000313|EMBL:AFL54092.1};
OS   Sinorhizobium fredii (strain USDA 257).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1185652 {ECO:0000313|EMBL:AFL54092.1, ECO:0000313|Proteomes:UP000006180};
RN   [1] {ECO:0000313|EMBL:AFL54092.1, ECO:0000313|Proteomes:UP000006180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA 257 {ECO:0000313|EMBL:AFL54092.1,
RC   ECO:0000313|Proteomes:UP000006180};
RX   PubMed=22843606; DOI=10.1128/JB.00966-12;
RA   Schuldes J., Rodriguez Orbegoso M., Schmeisser C., Krishnan H.B.,
RA   Daniel R., Streit W.R.;
RT   "Complete genome sequence of the broad-host-range strain Sinorhizobium
RT   fredii USDA257.";
RL   J. Bacteriol. 194:4483-4483(2012).
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; CP003563; AFL54092.1; -; Genomic_DNA.
DR   RefSeq; WP_014766203.1; NC_018000.1.
DR   AlphaFoldDB; I3XDY6; -.
DR   STRING; 1185652.USDA257_c55770; -.
DR   KEGG; sfd:USDA257_c55770; -.
DR   PATRIC; fig|1185652.3.peg.5781; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   Proteomes; UP000006180; 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:AFL54092.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          644..837
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   998 AA;  112368 MW;  C195F95E357B9004 CRC64;
     MTRQEANEQF QLTSFLDGAN AAYIEQLYAR YEADPSSVSA EWQSFFKALA DRPEDVVKAA
     KGASWKKKNW PIAANGELVS ALDGDWGTVE KVVEKKVKAK AEEAAAATGV PVSEAEVHQS
     TRDSVRAIMM IRAYRMRGHL HAKLDPLGLA DPVEDYDELA PKTYGFEEKD YDRKIFIDNV
     LGLEYATVRE MVEILERTYC STMGVEFMHM SNPEEKAWIQ ERIEGPDKGV EFTPEGKRAI
     LQKLIEAEGF EQFIDVKYKG TKRFGLDGGE SLIPALEQLI KRGGQLGLKE IVLGMAHRGR
     LNVLSQVMAK PHRAIFHEFK GGSYAPDDVE GSGDVKYHLG ASSDREFDGN KVHLSLTANP
     SHLEIVNPVV MGKARAKQDQ MATVFEGDII PLRERVKVMP LLLHGDAAFA GQGVIAEILG
     LSGLRGHRVA GTVHFIINNQ IGFTTNPAFS RSSPYPSDVA KMIEAPIFHV NGDDPEAVVY
     AAKVATEFRM KFHKPVVVDM FCYRRFGHNE GDEPAFTQPK MYKAIRAHKT VVQVYSERLV
     AEGLMNDGEV EKMKADWRAR LEQEFEAGQS YKPNKADWLD GAWSGLRTAD NQDEQRRGRT
     SVPMKQLKEV GRKISEIPAG FSAHRTIQRF MENRANMVQT GEGIDWAMAE ALAFGTLVTE
     GTKIRLSGQD CERGTFSQRH SVLYDQETEE RYIPLANLSP TQARYEVINS MLSEEAVLGF
     EYGYSLARPN ALTLWEAQFG DFANGAQVVF DQFISSGERK WLRMSGLVCL LPHGYEGQGP
     EHSSARLERF LQLCAEDNMQ VANVTTPANY FHILRRQVKR DFRKPLILMT PKSLLRHKRA
     VSSLSEMAGE SSFHRLLWDD AEVIKDGPIK LQKDSKIRRV VMCSGKVYYD LLEEREKRGI
     DDIYLLRVEQ LYPFPAKALI NELSRFRHAE MVWCQEEPKN MGAWSFIDPY LEWVLAHIDA
     KYQRVRYTGR PAAASPATGL MSKHMAQLNA FLEDALGG
//