ID   A0A1M7FTB1_9GAMM        Unreviewed;       754 AA.
AC   A0A1M7FTB1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:SHM07362.1};
GN   ORFNames=SAMN05428972_2178 {ECO:0000313|EMBL:SHM07362.1};
OS   Rhodanobacter sp. OK091.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1881037 {ECO:0000313|EMBL:SHM07362.1, ECO:0000313|Proteomes:UP000184078};
RN   [1] {ECO:0000313|EMBL:SHM07362.1, ECO:0000313|Proteomes:UP000184078}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK091 {ECO:0000313|EMBL:SHM07362.1,
RC   ECO:0000313|Proteomes:UP000184078};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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};
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DR   EMBL; FRCH01000002; SHM07362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7FTB1; -.
DR   STRING; 1881037.SAMN05428972_2178; -.
DR   Proteomes; UP000184078; 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:UP000184078};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          417..598
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   754 AA;  82287 MW;  8E608198220EA129 CRC64;
     MPFAISARHK GFNRAEIVDQ NFIEFVQLWQ GEVRAAPRDS EAVLPGSALD ARGFRELLES
     QLISRHLDLM ARVLRVQNKV FYTIGSSGHE GNAMVARLTR HTDPAFLHYR SGGFMAERFR
     KLPGMDPVTD SALSFAASKD DPASGGRHKV WGSKPLWVLP QTSTIASHLP KALGTAVAIE
     QARRIGHQLP IPDDSITICS FGDASSNHAT AQTAFNAAAW TAYQKLPAPV LFVCEDNGIG
     ISVKTPAGWV ASNFQHRSNL DYFFADGLDL AEGYAQVQRA VEHCRSTRRP TFLHLKTTRV
     MGHAGTDFEI EWRSVEELFA VEAADPLLRS AGIALESGLY SKDALLNLYE ATRRRCFAAA
     EDADSRHRLT SLADVMKPLA PYTPAAVQAE ATRSDYAEKR LAVFGGEEKL PEKLPPRHLA
     IQIGQALHDL LAKYPQALLF GEDVAQKGGV YTVTKGLNKI FKGSRVFNTL LDETMILGLA
     QGYANMGMLP MPEIQYLAYF HNACDQIRGE AASLQFFSND QYRNPMVMRV ASLGYQKGFG
     GHFHNDNSIT ALRDIPGLVV GCASRGDDAA MMLRTMMALA KVDGRVCAFL EPIALYMTKD
     LYEAGDGLWQ YDYPAPDQAM TLGEGRIYNA AANDLVIFTF GNGVPMALRA ARTIEQELDW
     QVRVVDLRWL APLNDAFIAA QAKSAKRILV LDEGRKSAGV GEGVVTAIVE GGCGATPMRR
     VVGADTFTPL AGAALLVLPG EADVVAAARE LAKR
//