ID A0A167GW89_9FLAO Unreviewed; 668 AA.
AC A0A167GW89;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:OAB77967.1};
GN ORFNames=ULVI_10790 {ECO:0000313|EMBL:OAB77967.1};
OS Cochleicola gelatinilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cochleicola.
OX NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB77967.1, ECO:0000313|Proteomes:UP000077013};
RN [1] {ECO:0000313|EMBL:OAB77967.1, ECO:0000313|Proteomes:UP000077013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0005 {ECO:0000313|EMBL:OAB77967.1,
RC ECO:0000313|Proteomes:UP000077013};
RA Shin S.-K., Yi H.;
RT "Ulvibacter sp. LPB0005, isolated from Thais luteostoma.";
RL Submitted (FEB-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:OAB77967.1}.
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DR EMBL; LRXL01000045; OAB77967.1; -; Genomic_DNA.
DR RefSeq; WP_068592691.1; NZ_LRXL01000045.1.
DR AlphaFoldDB; A0A167GW89; -.
DR STRING; 1763537.ULVI_10790; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000077013; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077013}.
FT DOMAIN 351..524
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 668 AA; 74721 MW; 32474AD71CBBBB72 CRC64;
MKSQIVPKIH FDYDRTNINS DTLVSLYRAM LKPRLIEEKM MILLRQGKIS KWFSGIGQEA
ISVGVASVLN SNEYILPMHR NLGVFTTREI PLYRLFSQWQ GKANGFTNGR DRSFHFGTQE
FNIVGMISHL GPQFGVADGI ALANQLKKND HVCAVFTGEG GTSEGDIHEA LNVASVWQLP
VLFCIENNGY GLSTPTSEQY NCEHLADRGK GYGMESHIIE GNNILEVYSK LKELVSDMRK
NPRPVLLEFK TFRMRGHEEA SGTKYVPTEL IDFWGEKDPL INFEKYLISE ELLSEEMIEA
FTNAIKQEID ENLEKAFEEP TIEADLTKEL NDVYSSFKYQ EVAHTNDVEN IRLIDAISEG
LKLSMRKHDN LVIMGQDVAE YGGVFKITEG FVEEFGKERV RNTPICESAI VSAAMGLSIN
GFKAVMEMQF ADFVTSGFNP IINYLAKSHY RWNQKADVVI RMPCGAGVGA GPFHSQTNEA
WFTHTPGLKV VYPAFPYDAK GLLATAIEDP NPVLFFEHKA LYRSIRQDVP KEYYTLPIGK
AATLREGDAI TIISYGAGIH WAIETLDTLP DVKADLIDLR TLSPLDTETI FASVSKTGKA
IILQEDSLFG GIASDISALI SEHCFEKLDA PVMRVASIET PIPFAAALES QYLPKNKFKE
ALINLLAY
//
