YNFE_ECOLI
ID YNFE_ECOLI Reviewed; 808 AA.
AC P77374; P77291;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Putative dimethyl sulfoxide reductase chain YnfE;
DE Short=DMSO reductase;
DE EC=1.8.99.-;
DE Flags: Precursor;
GN Name=ynfE; OrderedLocusNames=b1587, JW1579;
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.
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 -!- INTERACTION:
CC P77374; P69853: dmsD; NbExp=3; IntAct=EBI-556186, 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.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U00096; AAC74659.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15311.1; -; Genomic_DNA.
DR PIR; E64914; E64914.
DR RefSeq; NP_416104.1; NC_000913.3.
DR RefSeq; WP_000041675.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P77374; -.
DR SMR; P77374; -.
DR BioGRID; 4261571; 9.
DR DIP; DIP-12765N; -.
DR IntAct; P77374; 5.
DR STRING; 511145.b1587; -.
DR TCDB; 5.A.3.3.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P77374; -.
DR PaxDb; P77374; -.
DR PRIDE; P77374; -.
DR EnsemblBacteria; AAC74659; AAC74659; b1587.
DR EnsemblBacteria; BAA15311; BAA15311; BAA15311.
DR GeneID; 946135; -.
DR KEGG; ecj:JW1579; -.
DR KEGG; eco:b1587; -.
DR PATRIC; fig|1411691.4.peg.675; -.
DR EchoBASE; EB3604; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR InParanoid; P77374; -.
DR OMA; FGFHYKA; -.
DR PhylomeDB; P77374; -.
DR BioCyc; EcoCyc:G6845-MON; -.
DR BioCyc; MetaCyc:G6845-MON; -.
DR PRO; PR:P77374; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
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; 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; 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..43
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 44..808
FT /note="Putative dimethyl sulfoxide reductase chain YnfE"
FT /id="PRO_0000019147"
FT DOMAIN 49..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 96
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 196
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 808 AA; 89780 MW; E7A6A626C9E46449 CRC64;
MSKNERMVGI SRRTLVKSTA IGSLALAAGG FSLPFTLRNA AAAVQQAREK VVWGACSVNC
GSRCALRLHV KDNEVTWVET DNTGSDEYGN HQVRACLRGR SIRRRINHPD RLNYPMKRVG
KRGEGKFERI SWDEALDTIA SSLKKTVEQY GNEAVYIQYS SGIVGGNMTR SSPSASAVKR
LMNCYGGSLN QYGSYSTAQI SCAMPYTYGS NDGNSTTDIE NSKLVVMFGN NPAETRMSGG
GITYLLEKAR EKSNAKMIVI DPRYTDTAAG REDEWLPIRP GTDAALVAGI AWVLINENLV
DQPFLDKYCV GYDEKTLPAD APKNGHYKAY ILGEGDDKTA KTPQWASQIT GIPEDRIIKL
AREIGTAKPA YICQGWGPQR QANGELTARA IAMLPILTGN VGISGGNSGA RESTYTITIE
RLPVLDNPVK TSISCFSWTD AIDHGPQMTA IRDGVRGKDK LDVPIKFIWN YAGNTLVNQH
SDINKTHEIL QDESKCEMIV VIENFMTSSA KYADILLPDL MTVEQEDIIP NDYAGNMGYL
IFLQPVTSEK FERKPIYWIL SEVAKRLGPD VYQKFTEGRT QEQWLQHLYA KMLAKDPALP
SYDELKKMGI YKRKDPNGHF VAYKAFRDDP EANPLKTPSG KIEIYSSRLA EIARTWELEK
DEVISPLPVY ASTFEGWNSP ERRTFPLQLF GFHYKSRTHS TYGNIDLLKA ACRQEVWINP
IDAQKRGIAN GDMVRVFNHR GEVRLPAKVT PRILPGVSAM GQGAWHEANM SGDKIDHGGC
VNTLTTLRPS PLAKGNPQHT NLVEIEKI
