ID A0A368MIS4_9FLAO Unreviewed; 682 AA.
AC A0A368MIS4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Tungsten formylmethanofuran dehydrogenase {ECO:0000313|EMBL:RCT56054.1};
GN ORFNames=DUZ96_01300 {ECO:0000313|EMBL:RCT56054.1};
OS Winogradskyella sp. KYW1333.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=2282123 {ECO:0000313|EMBL:RCT56054.1, ECO:0000313|Proteomes:UP000253188};
RN [1] {ECO:0000313|EMBL:RCT56054.1, ECO:0000313|Proteomes:UP000253188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KYW1333 {ECO:0000313|EMBL:RCT56054.1,
RC ECO:0000313|Proteomes:UP000253188};
RA Yang H.G., Seong C.N.;
RT "Complete genome sequence of Winogradskyella aestuarii KYW1333 isolated
RT from seawater.";
RL Submitted (JUL-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:RCT56054.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QPHL01000010; RCT56054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368MIS4; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000253188; 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:UP000253188}.
FT DOMAIN 346..522
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 76002 MW; DC78CAD0A2D9D039 CRC64;
MKKEILKKGF IKLCTAKAMT ELYEANFKQV SKYVHATSRG HEAVQIALGL QLLPQDYAFP
YYRDDAMLLA FGMEPYDLML QLLAKKDDPF SGGRSYYSHP SLKDDDKPKI PHQSSATGMQ
AIPATGVAMG IKYKELQGLN EITMENPLVV CSLGDASVTE GEIAEAFQMA ALKQMPILYL
VQDNGWDISA NAEETRAQNA FEYAKGFHGL DAISIDGANF IESYNALEEV IATIRKERRP
ILVHAKVPLL NHHTSGVRME WYRDDLDEAK FRDPYPVIKK QLLDAGFSKQ EVKKLEESAY
RKVDSDFKKA LKAEDPKPED LFTHDFVPTP IIEESGVREP EGAERVVMVD CALFAVEELM
REHKECLLYG QDVGGRLGGV FRETATLAQK FGDDRVFNTP IQEAFIVGST VGMSAVGLKP
IVEVQFADYI WPGLNQLFTE VSRSCYLTNG KWPVSMILRV PIGAYGSGGP YHSSSVESVV
TNIRGIKIAY PSNGADLKGL MKAAYHDPNP VVILEHKGLY WSKVPGTKTA TSIEPAEDYI
LPFGKAWVLQ EIWKQEDVET LTIVSYGMGV HWAYNASGEL GLRDQIEIID LRTLFPLDED
TIMKSVKKTG KCLVVTEEPS NNSFARALAG KIQEECFKYL DGPVMVIGSE NMPAIPLNST
LEETMIPSTE KIKAKIEMIL DY
//