ID   N9WEU8_9SPHN            Unreviewed;       733 AA.
AC   N9WEU8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   ORFNames=EBMC1_05044 {ECO:0000313|EMBL:ENY82228.1};
OS   Sphingopyxis sp. MC1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY82228.1, ECO:0000313|Proteomes:UP000013072};
RN   [1] {ECO:0000313|EMBL:ENY82228.1, ECO:0000313|Proteomes:UP000013072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|EMBL:ENY82228.1,
RC   ECO:0000313|Proteomes:UP000013072};
RA   Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., Nielsen J.L.;
RT   "Differential expression analysis of membrane associated proteins from
RT   triclosan-degrading sphingopyxis.";
RL   Submitted (FEB-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENY82228.1}.
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DR   EMBL; AOUN01000003; ENY82228.1; -; Genomic_DNA.
DR   RefSeq; WP_003041588.1; NZ_AOUN01000003.1.
DR   AlphaFoldDB; N9WEU8; -.
DR   PATRIC; fig|1174684.3.peg.1013; -.
DR   eggNOG; COG0022; Bacteria.
DR   eggNOG; COG1071; Bacteria.
DR   Proteomes; UP000013072; Unassembled WGS sequence.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013072}.
FT   DOMAIN          398..579
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   733 AA;  78427 MW;  71ED43C2261965AA CRC64;
     MDAAQAVHEK FLGALASGTL ARRADAPDPA RAGLTRSDAT DIFLSQLTSR QMDRLSRTLQ
     ARGEGFYTIG SSGHEGNAAV AAALRVTDMA FLHYRSNAFQ LHRARQLPGQ TPDWDMLLSF
     AASAEDPISG GRHKVIGSKP LAIPPQTSTI ASHLPKAVGA AFSIGIARRL GMCGLPLPED
     AVVLASFGDA SANHSTAQGA FNTAGWSAFQ GTPLPLIFLC EDNGIGISTR TPTGWIEAQF
     RHRAGLHYIQ CDGTDLVAAY AGAKEAADFA RRTRKPVFLH MGTVRLYGHA GSDVQGAYLP
     KALIEADEAR DPLLAGAALM VEQGWMSAAE VADAYEEIGA TLARQAEAAI RRPKLTTAAA
     VMESLVPPKI DRPPANRPST DERAALFAGD ANQMDKPMHM ARLLSWALAD LMLAYPEIVV
     AGEDVGPKGG VYNVTAKLHQ RFGSARVINT LLDEQAILGL AIGMAHNGFV PMPEIQFLAY
     VHNAEDQIRG EAATLSFFSN GQYTNPMVIR IAGLGYQKGF GGHFHNDNSL AVFRDIPGVI
     LAVPSNGRDA VQMLRECVRL AREEQRVVVF VEPIALYMTR DLHEEGDGLW TSAYEAPGEG
     TPIRLGDVGV HGDGTDLAIV TYGNGTYLSR QAEKLLAADG VKARVIDLRW LGPVDADKLV
     AAVGEAKRVL IVDECRITGS QSEALMALFT ERTPEKKLAR IAAEDSFIPL GKAATVTLPS
     RDSIYAAAKE LLA
//