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Database: UniProt
Entry: A0A0J8VRF3_9ENTR
LinkDB: A0A0J8VRF3_9ENTR
Original site: A0A0J8VRF3_9ENTR 
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
//
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