ID   A0A0M3V905_9GAMM        Unreviewed;       953 AA.
AC   A0A0M3V905;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=AOC03_06965 {ECO:0000313|EMBL:ALF59807.1};
OS   Psychrobacter urativorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=45610 {ECO:0000313|EMBL:ALF59807.1, ECO:0000313|Proteomes:UP000059847};
RN   [1] {ECO:0000313|EMBL:ALF59807.1, ECO:0000313|Proteomes:UP000059847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R10.10B {ECO:0000313|EMBL:ALF59807.1,
RC   ECO:0000313|Proteomes:UP000059847};
RA   See-Too W.S., Chan K.G.;
RT   "Complete genome of Psychrobacter urativorans R10.10B.";
RL   Submitted (SEP-2015) 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; CP012678; ALF59807.1; -; Genomic_DNA.
DR   RefSeq; WP_062534525.1; NZ_CP012678.1.
DR   AlphaFoldDB; A0A0M3V905; -.
DR   STRING; 45610.AOC03_06965; -.
DR   KEGG; pur:AOC03_06965; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000059847; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          600..794
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   953 AA;  106587 MW;  F2BCBE575B30D759 CRC64;
     MNSITKKSAD TGQTELAADN AHYIESLYEQ FLSDPDSVDA DWQDYFKQYQ SPNDAKHNAI
     QDQFLLLARN QTANKGKPVA TGTVGSSNAA DPKQMGVQQL ISAYRRRGHR RAKLDPLELH
     PRAAVEDLTL AYHGLSDADL DTVYSTGDLS IGKSEAPLRE IIEIMERVYC RHIGIEYMHV
     TTSTEKRWME KYLETNHGHI IFDKEKRLSI LERLTAAEGL EKYLARKYTG VKRFGLEGGE
     SFIPAINEII QRAGGYGTKE VVIGMAHRGR LNLLVNVLGK NPADLFDEFD GKVQPEKGSG
     DVKYHNGYSS NVMTPGGEAH LALGFNPSHL EIVSPVIQGS VRARQVRRDD TTGNLVLPIV
     IHGDAAFAGQ GVVQETFQMS QTRAYTTGGT VRIVINNQVG FTTSRQEDAR STEYCTDVAK
     MVHAPILHVN GDDPESVIFA AQLALDYRHE FGKDIIIDLF CYRRNGHNEA DEPSATQPLM
     YAVIKKLPTT RTLYAQKLIA EGVITAADEA RYEDEYRESL DRGEYVANSL VLEPNTEMFV
     DWTPYLGHDL VDEWDTSVDI EKLKAYGRRM AEMPEGYKLQ RQVQKVVEQR LAMQTGEEPL
     NWGAAETLAY ATLVDHDEVL VRITGEDVGR GTFSHRHSEL FNMDDGSMYV PLAHMSETQA
     RFATYNSLLS EEAVLAFEYG YATTVPNALV IWEAQFGDFV NGAQVVIDQF IASGETKWQR
     VCGLTMLLPH GFEGQGPEHS SARLERFLQL CAEENMQVIT PTTPAQIYHA LRRQAVRPSR
     KPMIVMSPKS LLRHKLATSQ LEELANGKFE TVLPEIDQQN ADKVTRLVLC GGKVYYDLLE
     QRRALGLDHV AIVRIEQLYP LPEKRLIAEI EKYSNLAEIV WTQEEPLNQG AWYYLAPHMY
     RIVVPHPTRA KVMEPVARPA SAAPATGSAK IHLQQQQALI AGGLGISVDE LAK
//