ID A0A0B8NTE7_9VIBR Unreviewed; 448 AA.
AC A0A0B8NTE7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=4-oxoglutarate dehydrogenase {ECO:0000313|EMBL:GAM55582.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:GAM55582.1};
GN ORFNames=JCM19231_2934 {ECO:0000313|EMBL:GAM55582.1};
OS Vibrio ishigakensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM55582.1, ECO:0000313|Proteomes:UP000031671};
RN [1] {ECO:0000313|EMBL:GAM55582.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RT "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAM55582.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RG NBRP consortium;
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:GAM55582.1}.
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DR EMBL; BBRZ01000016; GAM55582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B8NTE7; -.
DR Proteomes; UP000031671; 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 Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR InterPro; IPR011603; 2oxoglutarate_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 PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:GAM55582.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031671};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 101..294
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 448 AA; 51194 MW; A23C199A9DAFF67F CRC64;
MMEREEIGID TATQLVNEYR DALDHGEVVV KEWRPMAMHS VDWSPYLGHE WDMKWDSEYE
IERLKELGQR ICQYPDSHKL QSRVNKLYND RMAMIEGEKA IDWGMAETLA YATLVDDGKR
IRISGQDSGR GTFFHRHAVL HNQGDASTYV PLAHVHDKQG PFQVFDSVLS EEAVLAFEYG
YATAEPGGLT LWEAQFGDFA NGAQVVIDQF ISSGEQKWGR LCGITMLLPH GYEGQGPEHS
SARLERYLQL CAEQNIQVVV PSTPAQVYHM LRRQVVRPMR RPLIVMSPKS LLRHPLCTST
LEELAEGTFQ PVINEIDELE PTKIRRVVFC SGKVYFDLLE ERRKREIDDV AIVRVEQLYP
FPLSDVREAI SIYPQVTDFV WCQEEPQNQG AWYSSQHNFR AATPFNTTLN YAGRPASASP
AVGYMSVHLK QQKALIDDAL TIDKELEE
//
