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Dimethyl sulfoxide reductase DmsA (DMSO reductase) (DMSOR) (Me2SO reductase) (EC 1.8.5.3)

 DMSA_ECOLI              Reviewed;         814 AA.
P18775;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
12-SEP-2018, entry version 168.
RecName: Full=Dimethyl sulfoxide reductase DmsA;
Short=DMSO reductase;
Short=DMSOR;
Short=Me2SO reductase;
EC=1.8.5.3;
Flags: Precursor;
Name=dmsA; OrderedLocusNames=b0894, JW5118;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 46-51, AND
FUNCTION AS A DIMETHYLSULPHOXIDE REDUCTASE.
STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
PubMed=3062312; DOI=10.1111/j.1365-2958.1988.tb00090.x;
Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H.;
"Nucleotide sequence of the dmsABC operon encoding the anaerobic
dimethylsulphoxide reductase of Escherichia coli.";
Mol. Microbiol. 2:785-795(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
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).
[4]
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).
[5]
SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
LOCATION, SUBUNIT, AND COFACTOR.
PubMed=3280546; DOI=10.1128/jb.170.4.1505-1510.1988;
Weiner J.H., MacIsaac D.P., Bishop R.E., Bilous P.T.;
"Purification and properties of Escherichia coli dimethyl sulfoxide
reductase, an iron-sulfur molybdoenzyme with broad substrate
specificity.";
J. Bacteriol. 170:1505-1510(1988).
[6]
SUBCELLULAR LOCATION.
PubMed=2170332; DOI=10.1128/jb.172.10.5938-5948.1990;
Sambasivarao D., Scraba D.G., Trieber C., Weiner J.H.;
"Organization of dimethyl sulfoxide reductase in the plasma membrane
of Escherichia coli.";
J. Bacteriol. 172:5938-5948(1990).
[7]
MUTAGENESIS OF LYS-57; CYS-67; CYS-71; CYS-104 AND ARG-106.
PubMed=8125918;
Trieber C.A., Rothery R.A., Weiner J.H.;
"Multiple pathways of electron transfer in dimethyl sulfoxide
reductase of Escherichia coli.";
J. Biol. Chem. 269:7103-7109(1994).
[8]
COFACTOR, AND ACTIVITY REGULATION.
PubMed=7721698; DOI=10.1128/jb.177.8.2057-2063.1995;
Rothery R.A., Grant J.L., Johnson J.L., Rajagopalan K.V., Weiner J.H.;
"Association of molybdopterin guanine dinucleotide with Escherichia
coli dimethyl sulfoxide reductase: effect of tungstate and a mob
mutation.";
J. Bacteriol. 177:2057-2063(1995).
[9]
BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBSTRATE
SPECIFICITY.
PubMed=8969520; DOI=10.1099/13500872-142-11-3231;
Simala-Grant J.L., Weiner J.H.;
"Kinetic analysis and substrate specificity of Escherichia coli
dimethyl sulfoxide reductase.";
Microbiology 142:3231-3239(1996).
[10]
MUTAGENESIS OF CYS-67 AND ARG-106, AND COFACTOR.
PubMed=10224050; DOI=10.1074/jbc.274.19.13002;
Rothery R.A., Trieber C.A., Weiner J.H.;
"Interactions between the molybdenum cofactor and iron-sulfur clusters
of Escherichia coli dimethylsulfoxide reductase.";
J. Biol. Chem. 274:13002-13009(1999).
[11]
EXPORT VIA THE TAT-SYSTEM, AND MUTAGENESIS OF ARG-17.
PubMed=10801884; DOI=10.1074/jbc.M909289199;
Sambasivarao D., Turner R.J., Simala-Grant J.L., Shaw G., Hu J.,
Weiner J.H.;
"Multiple roles for the twin arginine leader sequence of dimethyl
sulfoxide reductase of Escherichia coli.";
J. Biol. Chem. 275:22526-22531(2000).
[12]
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).
[13]
INTERACTION OF SIGNAL PEPTIDE WITH DMSD; TATB AND TATC, AND
MUTAGENESIS OF 17-ARG-ARG-18.
PubMed=20169075; DOI=10.1371/journal.pone.0009225;
Kostecki J.S., Li H., Turner R.J., DeLisa M.P.;
"Visualizing interactions along the Escherichia coli twin-arginine
translocation pathway using protein fragment complementation.";
PLoS ONE 5:E9225-E9225(2010).
-!- FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) to
dimethyl sulfide (DMS). DMSO reductase serves as the terminal
reductase under anaerobic conditions, with DMSO being the terminal
electron acceptor. Terminal reductase during anaerobic growth on
various sulfoxides and N-oxide compounds. Allows E.coli to grow
anaerobically on DMSO as respiratory oxidant.
{ECO:0000269|PubMed:3062312}.
-!- CATALYTIC ACTIVITY: Dimethylsulfide + menaquinone + H(2)O =
dimethylsulfoxide + menaquinol.
-!- 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:0000269|PubMed:10224050,
ECO:0000269|PubMed:3280546, ECO:0000269|PubMed:7721698};
Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
(Mo-bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:10224050,
ECO:0000269|PubMed:3280546, ECO:0000269|PubMed:7721698};
-!- ACTIVITY REGULATION: Inhibited by dithionite, sodium
hydrogensulfite and tungstate. {ECO:0000269|PubMed:7721698,
ECO:0000269|PubMed:8969520}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.043 mM for 2-chloropyridine N-oxide (at pH 5 and at 30
degrees Celsius) {ECO:0000269|PubMed:8969520};
KM=0.045 mM for 3-amidopyridine N-oxide (at pH 5 and at 30
degrees Celsius) {ECO:0000269|PubMed:8969520};
KM=0.06 mM for tertramethylene sulfoxide (at pH 5 and at 30
degrees Celsius) {ECO:0000269|PubMed:8969520};
KM=0.09 mM for methionine sulfoxide (at pH 5 and at 30 degrees
Celsius) {ECO:0000269|PubMed:8969520};
KM=0.246 mM for 4-phenylpyridine N-oxide (at pH 5 and at 30
degrees Celsius) {ECO:0000269|PubMed:8969520};
KM=0.830 mM for dimethyldodecylamin N-oxide (at pH 5 and at 30
degrees Celsius) {ECO:0000269|PubMed:8969520};
KM=0.18 mM for DMSO (at pH 6.8 and at 23 degrees Celsius)
{ECO:0000269|PubMed:3280546};
KM=0.47 mM for L-methionine sulfoxide (at pH 6.8 and at 23
degrees Celsius) {ECO:0000269|PubMed:3280546};
KM=0.5 mM for nicotinamide N-oxide (at pH 6.8 and at 23 degrees
Celsius) {ECO:0000269|PubMed:3280546};
KM=0.6 mM for TMAO (at pH 6.8 and at 23 degrees Celsius)
{ECO:0000269|PubMed:3280546};
KM=1.0 mM for 4-picoline N-oxide (at pH 6.8 and at 23 degrees
Celsius) {ECO:0000269|PubMed:3280546};
KM=20.2 mM for TMAO (at pH 5 and at 30 degrees Celsius)
{ECO:0000269|PubMed:8969520};
-!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
(DmsAB) and a membrane anchor protein (DmsC).
{ECO:0000269|PubMed:3280546}.
-!- INTERACTION:
P18776:dmsB; NbExp=2; IntAct=EBI-4411104, EBI-1120825;
P69853:dmsD; NbExp=8; IntAct=EBI-4411104, EBI-4406374;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2170332,
ECO:0000269|PubMed:3280546}; Peripheral membrane protein
{ECO:0000269|PubMed:2170332, ECO:0000269|PubMed:3280546};
Cytoplasmic side {ECO:0000269|PubMed:2170332,
ECO:0000269|PubMed:3280546}.
-!- PTM: Exported by the Tat system. The position of the signal
peptide cleavage has been experimentally proven. Can also be
exported by the Sec system.
-!- MISCELLANEOUS: The Tat signal sequence is essential for the
expression of dmsA, the stability of the DmsAB dimer and membrane
targeting. Despite the presence of a signal sequence, DmsA is not
exported to the periplasm.
-!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
oxidoreductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA83843.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; J03412; AAA83843.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73980.2; -; Genomic_DNA.
EMBL; AP009048; BAA35626.2; -; Genomic_DNA.
PIR; S03785; S03785.
RefSeq; NP_415414.4; NC_000913.3.
RefSeq; WP_000850303.1; NZ_LN832404.1.
ProteinModelPortal; P18775; -.
SMR; P18775; -.
BioGrid; 4261945; 69.
ComplexPortal; CPX-320; DMSO reductase complex.
DIP; DIP-9452N; -.
IntAct; P18775; 8.
MINT; P18775; -.
STRING; 316385.ECDH10B_0964; -.
TCDB; 5.A.3.3.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
PaxDb; P18775; -.
PRIDE; P18775; -.
EnsemblBacteria; AAC73980; AAC73980; b0894.
EnsemblBacteria; BAA35626; BAA35626; BAA35626.
GeneID; 945508; -.
KEGG; ecj:JW5118; -.
KEGG; eco:b0894; -.
PATRIC; fig|1411691.4.peg.1383; -.
EchoBASE; EB0228; -.
EcoGene; EG10232; dmsA.
eggNOG; ENOG4107QY8; Bacteria.
eggNOG; COG0243; LUCA.
HOGENOM; HOG000284390; -.
InParanoid; P18775; -.
KO; K07306; -.
OMA; HYGDYST; -.
PhylomeDB; P18775; -.
BioCyc; EcoCyc:DMSA-MONOMER; -.
BioCyc; MetaCyc:DMSA-MONOMER; -.
BRENDA; 1.8.5.3; 2026.
PRO; PR:P18775; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009390; C:dimethyl sulfoxide reductase complex; IDA:EcoCyc.
GO; GO:0031237; C:intrinsic component of periplasmic side of plasma membrane; IDA:EcoCyc.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP:EcoCyc.
GO; GO:0048037; F:cofactor binding; IMP:EcoCyc.
GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
GO; GO:0009055; F:electron transfer activity; IMP:EcoCyc.
GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
GO; GO:0009061; P:anaerobic respiration; IEP: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.
InterPro; IPR019546; TAT_signal_bac_arc.
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.
TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
4Fe-4S; Cell membrane; Complete proteome; Direct protein sequencing;
Iron; Iron-sulfur; Membrane; Metal-binding; Molybdenum;
Oxidoreductase; Reference proteome; Signal.
SIGNAL 1 45 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648,
ECO:0000269|PubMed:3062312}.
CHAIN 46 814 Dimethyl sulfoxide reductase DmsA.
/FTId=PRO_0000019143.
DOMAIN 56 118 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
REGION 172 176 MGD 1 binding. {ECO:0000250}.
REGION 244 245 MGD 2 binding. {ECO:0000250}.
REGION 270 271 MGD 2 binding. {ECO:0000250}.
REGION 291 293 MGD 2 binding. {ECO:0000250}.
REGION 386 387 MGD 2 binding. {ECO:0000250}.
REGION 512 513 MGD 1 binding. {ECO:0000250}.
REGION 701 701 MGD 1 binding. {ECO:0000250}.
REGION 707 709 MGD 1 binding. {ECO:0000250}.
REGION 804 805 MGD 1 binding. {ECO:0000250}.
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 71 71 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 104 104 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 205 205 Molybdenum. {ECO:0000250}.
BINDING 390 390 Molybdopterin guanine dinucleotide 1.
{ECO:0000250}.
BINDING 488 488 Molybdopterin guanine dinucleotide 1.
{ECO:0000250}.
BINDING 788 788 Molybdopterin guanine dinucleotide 1.
{ECO:0000250}.
MUTAGEN 17 17 R->S: Not targeted to the membrane, does
not support anaerobic growth.
{ECO:0000269|PubMed:10801884}.
MUTAGEN 57 57 K->D: No alteration of the growth,
expression, or catalytic activities.
{ECO:0000269|PubMed:8125918}.
MUTAGEN 67 67 C->S: Electron transfer from the 4Fe-4S
clusters of DmsB to the Mo-bisMGD of DmsA
is blocked. Little effect on the
coordination sphere of the molybdenum and
only minor effects on its redox
chemistry. {ECO:0000269|PubMed:10224050,
ECO:0000269|PubMed:8125918}.
MUTAGEN 71 71 C->S: Cannot support growth.
{ECO:0000269|PubMed:8125918}.
MUTAGEN 104 104 C->S: No alteration of the growth,
expression, or catalytic activities.
{ECO:0000269|PubMed:8125918}.
MUTAGEN 106 106 R->S: Electron transfer from the 4Fe-4S
clusters of DmsB to the Mo-bisMGD of DmsA
is blocked. Little effect on the
coordination sphere of the molybdenum and
only minor effects on its redox
chemistry. {ECO:0000269|PubMed:10224050,
ECO:0000269|PubMed:8125918}.
SEQUENCE 814 AA; 90399 MW; B97C830ABAC7C32C CRC64;
MKTKIPDAVL AAEVSRRGLV KTTAIGGLAM ASSALTLPFS RIAHAVDSAI PTKSDEKVIW
SACTVNCGSR CPLRMHVVDG EIKYVETDNT GDDNYDGLHQ VRACLRGRSM RRRVYNPDRL
KYPMKRVGAR GEGKFERISW EEAYDIIATN MQRLIKEYGN ESIYLNYGTG TLGGTMTRSW
PPGNTLVARL MNCCGGYLNH YGDYSSAQIA EGLNYTYGGW ADGNSPSDIE NSKLVVLFGN
NPGETRMSGG GVTYYLEQAR QKSNARMIII DPRYTDTGAG REDEWIPIRP GTDAALVNGL
AYVMITENLV DQAFLDKYCV GYDEKTLPAS APKNGHYKAY ILGEGPDGVA KTPEWASQIT
GVPADKIIKL AREIGSTKPA FISQGWGPQR HANGEIATRA ISMLAILTGN VGINGGNSGA
REGSYSLPFV RMPTLENPIQ TSISMFMWTD AIERGPEMTA LRDGVRGKDK LDVPIKMIWN
YAGNCLINQH SEINRTHEIL QDDKKCELIV VIDCHMTSSA KYADILLPDC TASEQMDFAL
DASCGNMSYV IFNDQVIKPR FECKTIYEMT SELAKRLGVE QQFTEGRTQE EWMRHLYAQS
REAIPELPTF EEFRKQGIFK KRDPQGHHVA YKAFREDPQA NPLTTPSGKI EIYSQALADI
AATWELPEGD VIDPLPIYTP GFESYQDPLN KQYPLQLTGF HYKSRVHSTY GNVDVLKAAC
RQEMWINPLD AQKRGIHNGD KVRIFNDRGE VHIEAKVTPR MMPGVVALGE GAWYDPDAKR
VDKGGCINVL TTQRPSPLAK GNPSHTNLVQ VEKV


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