ID A0A0R2T937_9FLAO Unreviewed; 684 AA.
AC A0A0R2T937;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Tungsten formylmethanofuran dehydrogenase {ECO:0000313|EMBL:KRO81970.1};
GN ORFNames=ABR87_00005 {ECO:0000313|EMBL:KRO81970.1};
OS Cryomorphaceae bacterium BACL7 MAG-121220-bin83.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655595 {ECO:0000313|EMBL:KRO81970.1, ECO:0000313|Proteomes:UP000051535};
RN [1] {ECO:0000313|EMBL:KRO81970.1, ECO:0000313|Proteomes:UP000051535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL29 MAG-121220-bin83 {ECO:0000313|EMBL:KRO81970.1};
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:KRO81970.1}.
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DR EMBL; LICF01000045; KRO81970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2T937; -.
DR Proteomes; UP000051535; 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 350..526
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 684 AA; 75111 MW; A1D2786AB5FA8D13 CRC64;
MSKNIHPSLL KAYTLMATAK AMTDLFEANR DVTQTYVHAT SRGHEAIQLA CSLQLKSVDY
LYPYYRDDAM LLGIGMRPYD LMLQLLAKRD DPFSGGRTYY SHPSLRDDDK PKIPHQSSAT
GMQAIPAAGA AMGIQYREKQ GLTQEWGDEK PVVVCSIGDA AMTEGEISEA LQMAALKQFP
LLMLVQDNGW DISASAAETR SGSAVDYAKG FKGLNVVQVD GSDFNASFHA VREVLKNMRK
TRQPYLIHAK VPLLNHHTSG VRMEWYRDDL EEHGKRDPFP KLHAFLLDEG VALSELESLV
SQAEKTVAED YALALEAEDP RPEDLFTHRY APTPVTEEKG ERTPVNREKT VMVDSALFAI
REILAAHPEA LLYGQDVGRR LGGVFREAAT LAQQFGDDRV FNTPIQEAFI VGSTVGMSAV
GLKPIVEVQF ADYIWPGLNQ LFTELSRSYY LSNGKWAASA VIRVPIGAYG GGGPYHSSSV
ESVLTNIRGI KVAYPSTGAD LKGLMKAAYA DPNPVVILEH KGLYWSKIPG TEGAKTVEPD
ADYVIPFGKG RIALEARPHP DGSSLCVVTY GRGVYWAAEA AKHFEGRVEI IDLRTLLPWD
EALVMERVTA HHRALVVTEE PVVNTFAQAV AGKIQSECFR ALDAPVRVIG SEDTPAIPLN
KILEAALLPN ADKVRLAIEG LLAY
//