YNFF_ECOLI
ID YNFF_ECOLI Reviewed; 807 AA.
AC P77783;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Probable dimethyl sulfoxide reductase chain YnfF;
DE Short=DMSO reductase;
DE EC=1.8.99.-;
DE Flags: Precursor;
GN Name=ynfF; OrderedLocusNames=b1588, JW5260;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
CC -!- FUNCTION: Terminal reductase during anaerobic growth on various
CC sulfoxide and N-oxide compounds. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- SUBUNIT: The complex consists of three subunits: YnfF, the reductase;
CC YnfG, an electron transfer protein, and YnfH, a membrane anchor
CC protein. {ECO:0000305}.
CC -!- INTERACTION:
CC P77783; P69853: dmsD; NbExp=3; IntAct=EBI-6406285, EBI-4406374;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven. Can also be exported by
CC the Sec system.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U00096; AAC74660.4; -; Genomic_DNA.
DR EMBL; AP009048; BAA15312.2; -; Genomic_DNA.
DR PIR; F64914; F64914.
DR RefSeq; NP_416105.4; NC_000913.3.
DR RefSeq; WP_001340362.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P77783; -.
DR SMR; P77783; -.
DR BioGRID; 4259130; 9.
DR ComplexPortal; CPX-6019; Putative dimethyl sulfoxide reductase.
DR DIP; DIP-12766N; -.
DR IntAct; P77783; 2.
DR STRING; 511145.b1588; -.
DR TCDB; 5.A.3.3.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P77783; -.
DR PaxDb; P77783; -.
DR PRIDE; P77783; -.
DR EnsemblBacteria; AAC74660; AAC74660; b1588.
DR EnsemblBacteria; BAA15312; BAA15312; BAA15312.
DR GeneID; 66674522; -.
DR GeneID; 945268; -.
DR KEGG; ecj:JW5260; -.
DR KEGG; eco:b1588; -.
DR PATRIC; fig|511145.12.peg.1659; -.
DR EchoBASE; EB3605; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR InParanoid; P77783; -.
DR OMA; NELMPYS; -.
DR PhylomeDB; P77783; -.
DR BioCyc; EcoCyc:G6846-MON; -.
DR BioCyc; MetaCyc:G6846-MON; -.
DR PRO; PR:P77783; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:1990204; C:oxidoreductase complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0033797; F:selenate reductase activity; IMP:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR InterPro; IPR011888; Anaer_DMSO_reductase.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR02166; dmsA_ynfE; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Molybdenum; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..45
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 46..807
FT /note="Probable dimethyl sulfoxide reductase chain YnfF"
FT /id="PRO_0000019148"
FT DOMAIN 52..113
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 195
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
SQ SEQUENCE 807 AA; 89987 MW; 8120594A8C5816C5 CRC64;
MKIHTTEALM KAEISRRSLM KTSALGSLAL ASSAFTLPFS QMVRAAEAPV EEKAVWSSCT
VNCGSRCLLR LHVKDDTVYW VESDTTGDDV YGNHQVRACL RGRSIRRRMN HPDRLKYPMK
RVGKRGEGKF ERISWDEALD TISDNLRRIL KDYGNEAVHV LYGTGVDGGN ITNSNVPYRL
MNSCGGFLSR YGSYSTAQIS AAMSYMFGAN DGNSPDDIAN TKLVVMFGNN PAETRMSGGG
VTYYVEQARE RSNARMIVID PRYNDTAAGR EDEWLPIRPG TDGALACAIA WVLITENMVD
QPFLDKYCVG YDEKTLPANA PRNAHYKAYI LGEGPDGIAK TPEWAAKITS IPAEKIIQLA
REIGSAKPAY ICQGWGPQRH SNGEQTSRAI AMLSVLTGNV GINGGNSGVR EGSWDLGVEW
FPMLENPVKT QISVFTWTDA IDHGTEMTAT RDGVRGKEKL DVPIKFLWCY ASNTLINQHG
DINHTHEVLQ DDSKCEMIVG IDHFMTASAK YCDILLPDLM PTEQEDLISH ESAGNMGYVI
LAQPATSAKF ERKPIYWMLS EVAKRLGPDV YQTFTEGRSQ HEWIKYLHAK TKERNPEMPD
YEEMKTTGIF KKKCPEEHYV AFRAFREDPQ ANPLKTPSGK IEIYSERLAK IADTWELKKD
EIIHPLPAYT PGFDGWDDPL RKTYPLQLTG FHYKARTHSS YGNIDVLQQA CPQEVWINPI
DAQARGIRHG DTVRVFNNNG EMLIAAKVTP RILPGVTAIG QGAWLKADMF GDRVDHGGSI
NILTSHRPSP LAKGNPSHSN LVQIEKV
