ID A0A1H5GIZ5_9FLAO Unreviewed; 908 AA.
AC A0A1H5GIZ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=SAMN04487765_1583 {ECO:0000313|EMBL:SEE15515.1};
OS Tenacibaculum sp. MAR_2010_89.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1250198 {ECO:0000313|EMBL:SEE15515.1, ECO:0000313|Proteomes:UP000198792};
RN [1] {ECO:0000313|EMBL:SEE15515.1, ECO:0000313|Proteomes:UP000198792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_89 {ECO:0000313|EMBL:SEE15515.1,
RC ECO:0000313|Proteomes:UP000198792};
RA de Groot N.N.;
RL Submitted (OCT-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; FNUB01000005; SEE15515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5GIZ5; -.
DR STRING; 1250198.SAMN04487765_1583; -.
DR Proteomes; UP000198792; 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:UP000198792};
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 908 AA; 103660 MW; 3D3C1BD38C4F6318 CRC64;
MDKFSFLNAV HTGFIGDLYE QYQKNPDAVE PSWRSFFQGY DLANEDYSLT DEENSIEIPE
EVRKEFLVID LINGYRTRGH LFTKTNPVRE RRKYEPSLDL ENFGLNKSDL STVFNAGDIL
GMGPSPLSQI ISHLKAIYCD SIGVEYMYLR NPEELKWWQS RLNKNDNHPM YDLEGKKYIL
TKLNQASTFE SFLQTKYVGQ KRFSVEGGET LIPGISVALR DAAEKYGVEE CVLGMAHRGR
LNTLVNIFKK PVRDLFSEFE GKDFEDQDID GDVKYHLGLT LSKEYKGGQK MKMNLVPNPS
HLETVDAVAE GIVRAKVDLD YKGDNGKILP ILVHGDAAIA GQGIVYEVGQ MMNLNGYKTG
GTIHVVVNNQ VGFTTNYLDA RSSTYCTDVA KVTLSPVLHV NADDAEAVCH AMEMAVEYRT
KFKKDIYIDL LGYRKYGHNE GDEPRFTQPK LYKAISKHKN AKEIYAAKLI EEGSISSDYV
KQITDEFKSH LEAEFTESKK KTTSKIQEFM PEVWDGFVRK QLQDMLQPVD TSYSVEALKG
IAKVISTTPT GHKFVRKAER ILKGREKMVF EDNSLDWGTA ENLAYGTLLE EGYNIRISGE
DVERGTFSHR HAIMRDEETL ERVNLLNTNP NNKGEMTIFN SHLSEYGVLG FDYGYAMAAP
NTLTIWEAQF GDFANGAQIV FDQYISSAED KWKLQNGLVM LLPHGYEGQG PEHSSARIER
FLQSSAIDNW TVANCSTPAN IYHILRRQMK RDFRKPLVVF TPKSLLRLPK AVNTIEELAN
GTFQEVIDDT VDTSKVRKMV FCSGKFYYDL LAEREELNRE DVALVRIEQL FPLHNDQIKK
VMDRYPNVER YVWAQEEPKN MGSWGYMLER FELAKLECAS RDYHSAPAAG SSARYKRRHQ
RVLDKVFD
//
