ID A0A3M7LAR1_9FLAO Unreviewed; 690 AA.
AC A0A3M7LAR1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Tungsten formylmethanofuran dehydrogenase {ECO:0000313|EMBL:RMZ58612.1};
GN ORFNames=D1632_13505 {ECO:0000313|EMBL:RMZ58612.1};
OS Chryseobacterium nematophagum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2305228 {ECO:0000313|EMBL:RMZ58612.1, ECO:0000313|Proteomes:UP000267524};
RN [1] {ECO:0000313|EMBL:RMZ58612.1, ECO:0000313|Proteomes:UP000267524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUb275 {ECO:0000313|EMBL:RMZ58612.1,
RC ECO:0000313|Proteomes:UP000267524};
RA Page A., Roberts M., Felix M.-A., Weir W.;
RT "Chryseobacterium nematophagum: a novel matrix digesting pathogen of
RT nematodes.";
RL Submitted (AUG-2018) 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:RMZ58612.1}.
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DR EMBL; QWIV01000014; RMZ58612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7LAR1; -.
DR Proteomes; UP000267524; 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 354..530
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 690 AA; 77233 MW; D306561A50540D79 CRC64;
MENTLHQQVS QDILLKAYNH MMLAKAMADI YEENRNVCKY VHSTSRGHEA IQLATAYQLR
KEDWVSPYYR DESLLLGIGF EPYQLMLQLL AKADDPFSGG RSYYSHPSSR NENIPKIIHQ
SSATGMQAIP TTGVAQGIKY ILEFKLQEFE NAPVVICSLG DNSVTEGEVS EALQFAALHQ
LPIIFLVQDN EWGISVTKEE ARTCDVYDFV SGFDGLSRMR VDGTDFAESF EIMKKAVDFV
RTERKPLVVC AKTVLIGHHT SGVRREFYRD EEDLAKHRAK DPGEILRKQL LDTGIDEELL
KQITKKSRLE AEEAFEKAKN AEDPKPETVM QHIFAPTPIT EEVGMREPEG GEKIVMVDAA
IHAIQELMWK HPEALLYGQD VGERIGGVFR ETVTLGKKFG NKRVFNTAIQ EAYIIGSTAG
MSAVGLKPIV EVQFADYIYP GINQLITEIS KSNYLSNGKF PVSNIIRVPI GAYGGGGPYH
SGSVESILAN IKGIKIAYPS NAADFKGLLK AAYYDPNPII MLEHKGLYWS KVPGTEDAKT
IEPAEDYILP FGKGNIVIEA DKKEVEKGRT LLIVTYGMGV YWAKEAVKNF NDRIEVIDLR
TLIPLDEKLV FERVKVHGKC IVLTEEQLNN SFAEAFAHRI SKNCFQYLDA PVETMGALDV
PAVPINLVLE KEMLPNAEKL TLKIEEMLTN
//