ID   A0A1I4G5W5_9RHOB        Unreviewed;       986 AA.
AC   A0A1I4G5W5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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   ORFNames=SAMN04488004_11177 {ECO:0000313|EMBL:SFL24476.1};
OS   Loktanella salsilacus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Loktanella.
OX   NCBI_TaxID=195913 {ECO:0000313|EMBL:SFL24476.1, ECO:0000313|Proteomes:UP000199550};
RN   [1] {ECO:0000313|EMBL:SFL24476.1, ECO:0000313|Proteomes:UP000199550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16199 {ECO:0000313|EMBL:SFL24476.1,
RC   ECO:0000313|Proteomes:UP000199550};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOTF01000011; SFL24476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4G5W5; -.
DR   STRING; 195913.SAMN04488004_11177; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000199550; Unassembled WGS sequence.
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:UP000199550};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          628..821
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   986 AA;  109981 MW;  A4509701DEC38FE7 CRC64;
     MNDQSPNDVL HASSFLQGHN ADYVEQLYAR YADNPQAVDE SWRDFFAALG DAPADAKAEA
     AGASWGRMDW PPVPNDDLTQ ALDGQWAQEP AAAGKKIAAK AEEKGVNLTE NQVRAAVLDS
     IRALMIIRAY RIRGHLIADL DPLGMREVTA HPELDPASYG FTKADMDRPI FIDNVLGLEV
     ATMAEIMAIV KRTYCGTFAL QYMHISNPDE AAWLKERIEG YGKEISFTQN GRKAILNKLV
     EAEGFEKFLH VKYMGTKRFG LDGGESLIPA MEQIIKRGGQ LGMEEVVIGM PHRGRLSVLA
     NVMQKPYRAI FNEFQGGSFK PEDVEGSGDV KYHLGASSDR EFDGNTVHLS LTANPSHLEA
     VNPVVLGKVR AKQDQKNDKD RIKVMAILLH GDAAFAGQGV VAEGFQLSGI RGHRTGGTMH
     IVVNNQIGFT TAPHFSRSSP YPTDIALMVE APIFHVNGDD PEAVVHAARV ATEFRQKFHK
     DVVLDIICYR RFGHNEGDEP MFTNPVMYTK IKKQKTTLTL YTDRLVKDGL IPEGEIEDMK
     ASFQSMLNAE FEAGKTYKPN KADWLDGRWS HLDRDKDNYQ RGETAISTEA MADIGKALTT
     PPEHFATHKT IDRLLDAKKQ MFEGGTGFDW ATGEALAFGS LVLEGYPVRL AGQDSTRGTF
     SQRHSALINQ NTEERYYPLN HVREGQAQYE VIDSMLSEYA VLGFEYGYSL AEPNALTLWE
     AQFGDFANGA QIMFDQFISS GEAKWLRMSG LVCLLPHGYE GQGPEHSSAR LERFLTMCGN
     DNWIVANCTT PANYFHILRR QLHRSYRKPL ILMTPKSLLR HKMAVSDAAD FTTGSSFHRV
     LWDDAQKGHS DTQLVADDKI KRVVMCSGKV YYDLLEERDA RGITDTYILR FEQFYPFPAQ
     SAVNELERFK NAEMVWCQEE PKNQGGWSFM EPNLEWCLTR IKAKHTRPVY AGRAAAASPA
     TGLASQHKAQ QAALVAEALN IEGITK
//