ID A3J3R5_9FLAO Unreviewed; 924 AA.
AC A3J3R5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=FBBAL38_06370 {ECO:0000313|EMBL:EAZ95302.1};
OS Flavobacteria bacterium BAL38.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391598 {ECO:0000313|EMBL:EAZ95302.1, ECO:0000313|Proteomes:UP000003784};
RN [1] {ECO:0000313|EMBL:EAZ95302.1, ECO:0000313|Proteomes:UP000003784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL38 {ECO:0000313|EMBL:EAZ95302.1,
RC ECO:0000313|Proteomes:UP000003784};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) 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:EAZ95302.1}.
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DR EMBL; AAXX01000002; EAZ95302.1; -; Genomic_DNA.
DR AlphaFoldDB; A3J3R5; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000003784; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003784};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 584..777
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 924 AA; 105047 MW; E6F4B1982900E3DB CRC64;
MDRFSFLNAA HTAFFADLYD QYLQNPDSVE ASWRSFFQGF DFAQEGYTSE DFTDRVVRAA
SSNAGEGSEK MQKEFNVLKL IEGYRTRGHL FTKTNPVRDR RVHGPSLAIE NFGLSQADLS
LVFDAARMVN MQPSTLADII KHLENVYCQS IGVEFMYIRE PRIQEWIKNR LDVNDNQPNF
SSDQKKNILK KLNEAVSFET FLHAKYVGQK RFSLEGCEST IPALDALIEA AADRGVEQFV
MGMAHRGRLN VLANIFGKNT QNIFSEFDGK DYDDDMYFDG DVKYHLGLTS DRLTDSGKKI
NLNLAPNPSH LETVGAVIEG ITRAKQDVFY KEDVSKVLPI AVHGDAAVAG QGIVYEIIQM
AKLDGYKTGG TIHLVINNQV GFTTNYLDAR SSTYCTDIAK VTLSPVLHVN ADDAEAVVHA
MLFALDYRME FGTDVFIDLL GYRKYGHNEG DEPKFTQPIL YKAISKHKNP RDIYAEKLKQ
EGIIDANYVK ELEAKYKAKL DENLEESRKK DLTIITPFMQ NEWVGFEQVS DEGMLKKYDT
TFDQNQLTAI AKTICELPSD KKFISKITKI IKDRNDMYFE NNNLDWAMGE LLAYGSLIKE
GYNVRISGQD VERGTFSHRH AVVKVEDSEE EVILLDKIND KKGNFYIYNS HLSEYGVVGF
EYGYALASPN TLTIWEAQFG DFSNGAQIMI DQYISAGEDK WNNQNGLVML LPHGYENQGA
EHSSARMERY LQMCAKHNMY IADCTTPANF FHLLRRQMKT KFRKPLIVFT PKSLLRHPLA
VSSKEELATG HFQEIIDDPN VSDKKAIKTL VFCTGKVYYD IIAQREELNR NDVAVVRLEQ
LFPLAIDQIK AIIDSYPNAD DYVWAQEEPK NMGAYSFMLM NFDLVKLRLA SPKAYSAPAA
GSYERSKKRQ KNAIAMVFDK TLFQ
//