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
//