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Probable dimethyl sulfoxide reductase chain YnfF (DMSO reductase) (EC 1.8.99.-)

 YNFF_ECOLI              Reviewed;         807 AA.
P77783;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 4.
28-MAR-2018, entry version 157.
RecName: Full=Probable dimethyl sulfoxide reductase chain YnfF;
Short=DMSO reductase;
EC=1.8.99.-;
Flags: Precursor;
Name=ynfF; OrderedLocusNames=b1588, JW5260;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
PubMed=17218314; DOI=10.1074/jbc.M610507200;
Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P.,
Ribnicky B., Palmer T., Georgiou G.;
"Export pathway selectivity of Escherichia coli twin arginine
translocation signal peptides.";
J. Biol. Chem. 282:8309-8316(2007).
-!- FUNCTION: Terminal reductase during anaerobic growth on various
sulfoxide and N-oxide compounds. {ECO:0000250}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000305};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
-!- COFACTOR:
Name=Mo-bis(molybdopterin guanine dinucleotide);
Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
(Mo-bis-MGD) cofactor per subunit. {ECO:0000250};
-!- SUBUNIT: The complex consists of three subunits: YnfF, the
reductase; YnfG, an electron transfer protein, and YnfH, a
membrane anchor protein. {ECO:0000305}.
-!- INTERACTION:
P69853:dmsD; NbExp=3; IntAct=EBI-6406285, EBI-4406374;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
-!- PTM: Exported by the Tat system. The position of the signal
peptide cleavage has not been experimentally proven. Can also be
exported by the Sec system.
-!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U00096; AAC74660.4; -; Genomic_DNA.
EMBL; AP009048; BAA15312.2; -; Genomic_DNA.
PIR; F64914; F64914.
RefSeq; NP_416105.4; NC_000913.3.
RefSeq; WP_001340362.1; NZ_LN832404.1.
ProteinModelPortal; P77783; -.
SMR; P77783; -.
BioGrid; 4259130; 9.
DIP; DIP-12766N; -.
IntAct; P77783; 2.
STRING; 316385.ECDH10B_1721; -.
TCDB; 5.A.3.3.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
PaxDb; P77783; -.
PRIDE; P77783; -.
EnsemblBacteria; AAC74660; AAC74660; b1588.
EnsemblBacteria; BAA15312; BAA15312; BAA15312.
GeneID; 945268; -.
KEGG; ecj:JW5260; -.
KEGG; eco:b1588; -.
PATRIC; fig|511145.12.peg.1659; -.
EchoBASE; EB3605; -.
EcoGene; EG13844; ynfF.
eggNOG; ENOG4105C3J; Bacteria.
eggNOG; COG1104; LUCA.
HOGENOM; HOG000284390; -.
InParanoid; P77783; -.
KO; K07310; -.
OMA; HTQGHTV; -.
PhylomeDB; P77783; -.
BioCyc; EcoCyc:G6846-MONOMER; -.
BioCyc; MetaCyc:G6846-MONOMER; -.
PRO; PR:P77783; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
GO; GO:0033797; F:selenate reductase activity; IMP:EcoCyc.
InterPro; IPR011888; Anaer_DMSO_reductase.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR006657; MoPterin_dinucl-bd_dom.
InterPro; IPR006656; Mopterin_OxRdtase.
InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
InterPro; IPR006311; TAT_signal.
Pfam; PF04879; Molybdop_Fe4S4; 1.
Pfam; PF00384; Molybdopterin; 1.
Pfam; PF01568; Molydop_binding; 1.
SMART; SM00926; Molybdop_Fe4S4; 1.
SUPFAM; SSF50692; SSF50692; 1.
TIGRFAMs; TIGR02166; dmsA_ynfE; 1.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
4Fe-4S; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane;
Metal-binding; Molybdenum; Oxidoreductase; Reference proteome; Signal.
SIGNAL 1 45 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648}.
CHAIN 46 807 Probable dimethyl sulfoxide reductase
chain YnfF.
/FTId=PRO_0000019148.
DOMAIN 52 113 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 59 59 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 63 63 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 67 67 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 99 99 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 195 195 Molybdenum. {ECO:0000250}.
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


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