ID A0A1L3JKK4_9FLAO Unreviewed; 908 AA.
AC A0A1L3JKK4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=LPB136_09870 {ECO:0000313|EMBL:APG65651.1};
OS Tenacibaculum todarodis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1850252 {ECO:0000313|EMBL:APG65651.1, ECO:0000313|Proteomes:UP000181898};
RN [1] {ECO:0000313|EMBL:APG65651.1, ECO:0000313|Proteomes:UP000181898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0136 {ECO:0000313|EMBL:APG65651.1,
RC ECO:0000313|Proteomes:UP000181898};
RA Kim E., Yi H.;
RT "Tenacibaculum sp. LPB0136, isolated from marine environment.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP018155; APG65651.1; -; Genomic_DNA.
DR RefSeq; WP_072556175.1; NZ_CP018155.1.
DR AlphaFoldDB; A0A1L3JKK4; -.
DR STRING; 1850252.LPB136_09870; -.
DR KEGG; ten:LPB136_09870; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000181898; Chromosome.
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:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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:UP000181898};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 574..767
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 908 AA; 103456 MW; B73BBCCD2BFC5FF4 CRC64;
MDKFSFLNAA HTGFIADLYE QYQKNPDAVE PSWRSFFQGY DLANEEYSDN EEVSSEIPEG
VRKEFLVIDL IDGYRSRGHL FTKTNPVRER RKYTPLLEVE NFGLTKNDLS TVFSAGEVLG
IGAKTLAQII DHLKAIYCDS IGVEYMYIRN PEELKWWQNR LNKNDNHPNY DLEGKKYILT
KLNQASTFES FLQTKYVGQK RFSVEGGETL IPGLSVALRD AAEKYGVKEC VLGMAHRGRL
NTLVNIFKKP VRDLFSEFEG KDFEDQTISG DVKYHLGLTL SKAYKGGQEM KMNLVPNPSH
LETVAAVAEG IVRAKIDKDY EGDNSKILPI IVHGDAAIAG QGIAYEIAQM MTLNGYKTGG
SIHIVVNNQV GFTTNYLDAR SSTYCTDVAK VTLSPVLHVN ADNAEAVCHA MEMAVEYRMK
FKKDIYIDLL GYRKYGHNEG DEPRFTQPEL YKAIAKHKNA KDIYAQQLIA NGSITAEYVT
QITNEFKEHL EEEFTQSKKK TTSKIQEFMP EVWDGFVRKQ LKDMLESTDT TYSADKLKEI
AKVISTTPEG HKFVRKAERI LQGREKMVFQ ENSLDWGIAE NLAYGSLLEE GFDVRISGED
VERGTFSHRH AIMRDENTLE RVNLLNTNTN NKGKLTIYNS HLSEYGVLGF DYGYAMATPK
TLTIWEAQFG DFANGAQIVF DQYITSAEDK WKLQNGLVVL LPHGYEGQGP EHSSGRIERF
LQQCAVDNIT VANCSNPANM YHLLRRQMKR DFRKPLVVFT PKSLLRHPKA VNTIEDLAEG
GFNEVIDDTI NPKNVTKMVF CMGKFYYDML AEREQLGRED VALVRIEQLF PLHEEKIKDV
IAKYPNVERY VWAQEEPKNM GAWGYMLERF DFVDRLEVAS RGYQAAPAAG SSTRYKKRHQ
EVLDKVFD
//
