ID A0A2S7TK76_9FLAO Unreviewed; 909 AA.
AC A0A2S7TK76;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=BSU00_05830 {ECO:0000313|EMBL:PQJ21982.1};
OS Tenacibaculum sp. SG-28.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=754426 {ECO:0000313|EMBL:PQJ21982.1, ECO:0000313|Proteomes:UP000239112};
RN [1] {ECO:0000313|Proteomes:UP000239112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-28 {ECO:0000313|Proteomes:UP000239112};
RA Kumagai Y., Yoshizawa S., Kogure K.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
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};
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:PQJ21982.1}.
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DR EMBL; MQVY01000002; PQJ21982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7TK76; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000239112; 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: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:UP000239112};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 575..768
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 909 AA; 103535 MW; 07F61E0D9485F3E9 CRC64;
MDKFSFLNAV HAGFIGDLYE QYQNNPDAVE PSWRSFFQGY DLANEDYLLT DEEVSVEIPQ
EVRKEFLVID LINGYRTRGH LFTKTNPVRE RRKYTPTLDI ENFGLSQSDL STVFNAGEIL
GIGPKTLSQI IDHLKAIYCD SIGVEYMYLR NPEELKWWQN RLNENDNHPK YSADTKKYIL
SKLNQAVGFE SFLQTKYVGQ KRFSVEGGET LIPGISIALR DAAEKYGVKE CVLGMAHRGR
LNTLVNIFKK PVRDLFSEFE GKDFEDQAIA GDVKYHLGLT LSKQYKNGEE IKMNLVPNPS
HLETVDAVVE GIVRAKVDND YEGDASKILP ILVHGDAAIA GQGIVYEVVQ MAQLNGYKTG
GTIHVVVNNQ VGFTTNYLDA RSSTYCTDIA KVTLSPVLHV NADDAEAVCH AMQLAVEFRM
KFKRDIFIDL LGYRKYGHNE GDEPRFTQPK LYKAIAKHKN PKLIYADALI AQNVVDASYV
KQITDEFKEM LELEFQESKK QEVSRVNEFM PEVWTGFLRK KLETMLQPTD TTYSLSKLKN
IAKVVSTVPE GVKFLRKAER ILNDRSKRVF ETNALDWGVA ETLAYGTLLE EGFDVRISGE
DVERGTFSHR HAILRDEVSE ERINLLNTNK NNKGVMTIYN SHLSEYGVLG FDYGYAMAAP
NTLTIWEAQF GDFANGAQIM FDQYISSAED KWKLQNGLVV LLPHGYEGQG PEHSSGRMER
FLQSCAIDNM IVANCSTPAN MYHILRRQMK RDYRKPLIVF TPKSLLRLPK AVSTMEELAE
GTFQEVIDDV SVTKSKVKKM VFCMGKFYYD LLEARESLGR EDVALVRIEQ LFPLHNEKIK
EIMDLYPNVE RYVWAQEEPK NMGAWTHMLE RFENATLECA SRGYHSAPAA GSSARFKRRH
QAVIDKVFD
//