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Database: UniProt
Entry: F3L4S3_9GAMM
LinkDB: F3L4S3_9GAMM
Original site: F3L4S3_9GAMM 
ID   F3L4S3_9GAMM            Unreviewed;       948 AA.
AC   F3L4S3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   13-SEP-2023, entry version 36.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=IMCC3088_2674 {ECO:0000313|EMBL:EGG28657.1};
OS   Aequoribacter fuscus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Aequoribacter.
OX   NCBI_TaxID=2518989 {ECO:0000313|EMBL:EGG28657.1, ECO:0000313|Proteomes:UP000005615};
RN   [1] {ECO:0000313|EMBL:EGG28657.1, ECO:0000313|Proteomes:UP000005615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG28657.1,
RC   ECO:0000313|Proteomes:UP000005615};
RX   PubMed=21551310; DOI=10.1128/JB.05111-11;
RA   Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.;
RT   "Genome sequence of strain IMCC3088, a proteorhodopsin-containing marine
RT   bacterium belonging to the OM60/NOR5 clade.";
RL   J. Bacteriol. 193:3415-3416(2011).
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:EGG28657.1}.
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DR   EMBL; AEIG01000087; EGG28657.1; -; Genomic_DNA.
DR   RefSeq; WP_009576832.1; NZ_CP036423.1.
DR   AlphaFoldDB; F3L4S3; -.
DR   STRING; 2518989.IMCC3088_2674; -.
DR   eggNOG; COG0567; Bacteria.
DR   Proteomes; UP000005615; 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   Reference proteome {ECO:0000313|Proteomes:UP000005615};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          602..795
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   948 AA;  106131 MW;  7FA1F25C10160087 CRC64;
     MRDHSMEQFW LSSHIAGGNA AYVEDLYESF LLNPENVSEQ WRLYFEQLPQ VQTKHISVLD
     TPHSAVRDQF AKISKMRVRT EATVAHDAQA TEFERKQVRV VQLISAYRQR GHQHAKLDPL
     GLAKREIVPD LALQFHQLST ADLDTVFQTG SLYIGSDSAT LGEILHSLES TYCGTIGAEF
     MHIVDTDERH WVMQRMESVR SRPDYSAAVR RQLLSELTKA EGLEKSLGSK YPGTKRFGLE
     GGESLIPALT EMIQRCGAYR AKEIVIGMAH RGRLNVLINI LGKKPSELFA EFEGRASYQS
     SGDVKYHQGF SSNIMTPGGE LHLALAFNPS HLEIVSPVVE GSVRARQDRR DDKTGSMVVP
     IVIHGDAAFA GQGVVMETFQ MSQTRAYKTG GTIHIVLNNQ VGFTTSLRED ARSTEYCTDI
     AKMVQAPIFH VNGDDPEAVL FVTQMAVDYR NEFGKDVVID LVCYRRRGHN EADEPSVTQP
     VMYAQIKNQE TTRDLYAKKL IAEGVLTQEQ DSDLVSAYRE SLERGEPLVS SLVSEPNTSL
     FVDWTPYLNH PWDLPSDTRI DLQTLQSLAH EINQTPEGLP LQRQVGKILE DRRKMAAGAL
     PLNWGAAETL AYATLLKAGY PVRLTGQDVG RGTFSHRHAV LHNQKDASLY VPLQHLGQDQ
     APFTIHDSLL SEEAVLAFEY GYATTAPTGL VIWEAQFGDF ANGAQVVIDQ FITSGEHKWS
     RLCGLTMLLP HGYEGQGPEH SSARLERFMQ LCAEKNIQVC IPTTPAQVFH MIRRQAIRPL
     RKPLIVMSPK SLLRHKEAVS TLEELANGQF QLVIPEVDNV SPKAVRRVVL CAGKVYYELL
     AERRARGIKD IALVRIEQMY PFPERELLSA LKEYPNLSDV VWCQEEPMNQ GCWYASQHHM
     RRALDQLGSG LGVRYVGREA SAAPAAGYMA LHLKQQEALI NQALEPTQ
//
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