ID A0A0J8VRF3_9ENTR Unreviewed; 935 AA.
AC A0A0J8VRF3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=ACH50_01215 {ECO:0000313|EMBL:KMV36068.1};
OS Franconibacter pulveris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Franconibacter.
OX NCBI_TaxID=435910 {ECO:0000313|EMBL:KMV36068.1, ECO:0000313|Proteomes:UP000037315};
RN [1] {ECO:0000313|EMBL:KMV36068.1, ECO:0000313|Proteomes:UP000037315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ34 {ECO:0000313|EMBL:KMV36068.1,
RC ECO:0000313|Proteomes:UP000037315};
RA Pal S., Banerjee T.D., Roy A., Sar P., Kazy S.K.;
RT "Genome sequencing of Cronobacter sp. strain DJ34 isolated from petroleum
RT contaminated sludge of Duliajan Oil Fields, Assam, India.";
RL Submitted (JUN-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};
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006936}.
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:KMV36068.1}.
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DR EMBL; LFEJ01000003; KMV36068.1; -; Genomic_DNA.
DR RefSeq; WP_024557137.1; NZ_LFEJ01000003.1.
DR AlphaFoldDB; A0A0J8VRF3; -.
DR STRING; 1121863.GCA_000621185_00385; -.
DR PATRIC; fig|1656095.3.peg.16; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000037315; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 593..786
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 935 AA; 105308 MW; 4BAF17BFFA329D69 CRC64;
MQNGAMQAWL DSSYLSGSNQ SWIEQLYEDF LTDPDSVDAH WRSMFQQLPG TGARPDQFHS
KTRDYFRRLA KDASRYTSSI TDPDADVKQV KVLQLINAYR FRGHQQANLD PLGLWKQDRV
ADLDPAFHNL TEADFQETFN VGSFAGGKEA MQLGELIEAL KQTYCGSIGA EYMHITSTEE
KRWIQQRIES VVGHASFSVE EKKRFLGELT AAEGLERYLG AKFPGAKRFS LEGGDALIPM
LKEMIRHAGK SGTREVVLGM AHRGRLNVLI NVLGKKPQDL FDEFAGKHKE HLGTGDVKYH
MGFSSDIETE GGLVHLALAF NPSHLEIVSP VVMGSVRARL DRLDEPSSNK VLPITIHGDA
AVTGQGVVQE TLNMSKARGY EVGGTVRIVI NNQVGFTTSN PLDARSTPYC TDIGKMVQAP
IFHVNADDPE AVAFVTRLAL EFRNNFKRDV FIDLVCYRRH GHNEADEPSA TQPLMYQKIK
KHPTPRKLYA DQLEQEKVAT LEDATEMVNL YRDALDAGEC VVKEWRPMNM HSFTWSPYLN
HEWDESYPNK VEMKRLQELA KRISTVPESI EMQSRVAKIY ADRQLMANGE KPFDWGGAET
LAYATLVDEG IPVRLSGEDS GRGTFFHRHA VVHNQTNGST YTPLQHVHNG QGQFKVWDSV
LSEEAVLAFE YGYATAEPRT LTIWEAQFGD FANGAQVVID QFISSGEQKW GRMCGLVMLL
PHGYEGQGPE HSSARLERYL QLCAEQNMQV CVPSTPAQVY HMLRRQALRG MRRPLVVMSP
KSLLRHPLAI SSLDELANGT FMPAIGEIDE LDPKEVKRVV LCSGKVYYDL LEQRRKNDQK
DVAIVRIEQL YPFPHQAVQE ALKPFAHVHD FVWCQEEPLN QGAWYCSQHH FREVIPFGSA
LRYAGRPASA SPAVGYMSVH QKQQQDLVND ALNVD
//