ID A0A0R2QWA5_9FLAO Unreviewed; 658 AA.
AC A0A0R2QWA5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KRO54631.1};
GN ORFNames=ABR79_01325 {ECO:0000313|EMBL:KRO54631.1};
OS Cryomorphaceae bacterium BACL11 MAG-121001-bin54.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655587 {ECO:0000313|EMBL:KRO54631.1, ECO:0000313|Proteomes:UP000051874};
RN [1] {ECO:0000313|EMBL:KRO54631.1, ECO:0000313|Proteomes:UP000051874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL11 MAG-121001-bin54 {ECO:0000313|EMBL:KRO54631.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO54631.1}.
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DR EMBL; LIBL01000184; KRO54631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2QWA5; -.
DR Proteomes; UP000051874; 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}.
FT DOMAIN 341..514
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 658 AA; 73018 MW; 92DE56CA4ADE31E8 CRC64;
MQFNRKGIAD AELLGLYKAL IKPRLVEEKM LILLRQGKVS KWFSGIGQEA ISVGVAFALD
QDEYILPMHR NLGVFTVKNV PLNRLFSQFQ GKANGFTKGR DRSFHFGTKE HYIVGMISHL
GPQLGVADGI ALANKLQNNK KITAVFTGDG ATSEGDFHEA LNVAAVWDLP VIFVIENNGY
GLSTPSSEQF RCKQFADKGI GYGMDAYTID GNNILEVYKA VKDIKEQNLK KSKPVILECM
TFRMRGHEEA SGTKYVQDEL MEQWEKLDPI DNFETFLLNE KVITQSAIED FKKEIKSEIN
TAWEETESEP KIQSSAEKEL ADMYKEYTAQ IISPSENKSE KRLVDAVSDG LRQSMQKHDN
LIIMGQDIAE YGGVFKITDG FVNEFGKERV RNTPICESAI VSAALGLSIN GQKAVVEMQF
ADFVTSGFNP IVNNLAKTHY RWGENADVVV RMPTGAGVGA GPFHSQSNEA WFTHTPGLKV
VYPAFPEDAK GLLNASINDP NPVMFFEHKA LYRSFSEPVC DDYFTIEIGK AKLIAEGNDV
SIISYGMGVH WALEVLKNNP AISADLIDLR TLVPLDKDAI LNSVKKTGKA IVLHEDCMMG
GFGADIASII SDSCFEYLDA PVKRSASIDT PVPFARELED KFLAKSSFES QLKELLAY
//