ID A0A1S1JDH7_9FLAO Unreviewed; 924 AA.
AC A0A1S1JDH7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=BHE19_02105 {ECO:0000313|EMBL:OHT46323.1};
OS Flavobacterium tructae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1114873 {ECO:0000313|EMBL:OHT46323.1, ECO:0000313|Proteomes:UP000180252};
RN [1] {ECO:0000313|Proteomes:UP000180252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSU {ECO:0000313|Proteomes:UP000180252};
RA Chen S., Walker E.;
RL Submitted (SEP-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:OHT46323.1}.
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DR EMBL; MIKE01000011; OHT46323.1; -; Genomic_DNA.
DR RefSeq; WP_070906106.1; NZ_MUHG01000002.1.
DR AlphaFoldDB; A0A1S1JDH7; -.
DR STRING; 1278819.BHE19_02105; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000180252; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 585..778
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 924 AA; 104600 MW; 88D9A5B865C625EC CRC64;
MDRFSFLNAA HTEFFAQLYD QYLVNPDSVE PSWRSFFQGF DFGQTTYNDE NPVQRIVEYV
TNDNVDCSLV SDKLQKEFNV LKLIDAYRTR GHLFTKTNPV RDRRTSSPTL DIENFGLTTA
DLSTVFDAAQ AIGVAPSTLQ DIVTRLQTIY CQHIGIEYMY IRNPGVVKWI QDKLAVNVNQ
PNFSSDEKKT ILNKLNQAVS FENFLHTKYV GQKRFSLEGG ESIIPALDAL IEQAAEKGVE
QFVMGMAHRG RLNVLANIFG KSTQDIFGEF DGKDYDQEYF DGDVKYHLGL TADKKTRTGK
NININLAPNP SHLETVGAVI EGITRAKQDK YYPNDFSKVL PIAVHGDAAI AGQGILYEII
QMSLLDGYKT GGTIHIVINN QVGFTTNYLD ARSSTYCTDV AKVTLSPVLH VNADDAEAVV
HAVSFALDYR MQFGRDVFID LLGYRKYGHN EGDEPRFTQP VLYKIIAKHK NPRDIYAEKL
LSDGIIDASY VNALEKEYKS ALEENLEASR KKDLTIITPF MQNEWNGFVQ VTDTQMLEKT
DTTFEKKELD SIINTISTLP ADKKFINKIT KIVTDRKVGY DNNTLDWGTA EALAYGSLLT
EGFDVRISGQ DVERGTFSHR HAVVKVEDSE EEVILLDTIA NKKGKFGVFN SLLSEYGVLG
FDYGYALANP NALTIWEAQF GDFSNGAQIM IDQYISCGED KWNNQNGIVL LLPHGYEGQG
AEHSSARMER YLQLCARHNM YVADCTTPAN FFHLIRRQMK TKFRKPLVVF SPKSLLRDPR
CVSTVEELAN GSFQETIDDT TVNKKDVKSL VFCTGKFYYD IVAERENNGR NDVAVVRIEQ
LFPFPVEQIK EIIAQYPNAD DYVWAQEEPK NMGAYSFMLM NFDLVKWRLA SLKAYSAPAS
GSYTRSKRRH ADAIRMVFDK NLFR
//