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DMSA_ECOLI
ID   DMSA_ECOLI              Reviewed;         814 AA.
AC   P18775;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Dimethyl sulfoxide reductase DmsA;
DE            Short=DMSO reductase;
DE            Short=DMSOR;
DE            Short=Me2SO reductase;
DE            EC=1.8.5.3;
DE   Flags: Precursor;
GN   Name=dmsA; OrderedLocusNames=b0894, JW5118;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 46-51, AND FUNCTION
RP   AS A DIMETHYLSULPHOXIDE REDUCTASE.
RC   STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX   PubMed=3062312; DOI=10.1111/j.1365-2958.1988.tb00090.x;
RA   Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H.;
RT   "Nucleotide sequence of the dmsABC operon encoding the anaerobic
RT   dimethylsulphoxide reductase of Escherichia coli.";
RL   Mol. Microbiol. 2:785-795(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
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   [4]
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   [5]
RP   SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP   SUBUNIT, AND COFACTOR.
RX   PubMed=3280546; DOI=10.1128/jb.170.4.1505-1510.1988;
RA   Weiner J.H., MacIsaac D.P., Bishop R.E., Bilous P.T.;
RT   "Purification and properties of Escherichia coli dimethyl sulfoxide
RT   reductase, an iron-sulfur molybdoenzyme with broad substrate specificity.";
RL   J. Bacteriol. 170:1505-1510(1988).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=2170332; DOI=10.1128/jb.172.10.5938-5948.1990;
RA   Sambasivarao D., Scraba D.G., Trieber C., Weiner J.H.;
RT   "Organization of dimethyl sulfoxide reductase in the plasma membrane of
RT   Escherichia coli.";
RL   J. Bacteriol. 172:5938-5948(1990).
RN   [7]
RP   MUTAGENESIS OF LYS-57; CYS-67; CYS-71; CYS-104 AND ARG-106.
RX   PubMed=8125918; DOI=10.1016/s0021-9258(17)37253-8;
RA   Trieber C.A., Rothery R.A., Weiner J.H.;
RT   "Multiple pathways of electron transfer in dimethyl sulfoxide reductase of
RT   Escherichia coli.";
RL   J. Biol. Chem. 269:7103-7109(1994).
RN   [8]
RP   COFACTOR, AND ACTIVITY REGULATION.
RX   PubMed=7721698; DOI=10.1128/jb.177.8.2057-2063.1995;
RA   Rothery R.A., Grant J.L., Johnson J.L., Rajagopalan K.V., Weiner J.H.;
RT   "Association of molybdopterin guanine dinucleotide with Escherichia coli
RT   dimethyl sulfoxide reductase: effect of tungstate and a mob mutation.";
RL   J. Bacteriol. 177:2057-2063(1995).
RN   [9]
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBSTRATE
RP   SPECIFICITY.
RX   PubMed=8969520; DOI=10.1099/13500872-142-11-3231;
RA   Simala-Grant J.L., Weiner J.H.;
RT   "Kinetic analysis and substrate specificity of Escherichia coli dimethyl
RT   sulfoxide reductase.";
RL   Microbiology 142:3231-3239(1996).
RN   [10]
RP   MUTAGENESIS OF CYS-67 AND ARG-106, AND COFACTOR.
RX   PubMed=10224050; DOI=10.1074/jbc.274.19.13002;
RA   Rothery R.A., Trieber C.A., Weiner J.H.;
RT   "Interactions between the molybdenum cofactor and iron-sulfur clusters of
RT   Escherichia coli dimethylsulfoxide reductase.";
RL   J. Biol. Chem. 274:13002-13009(1999).
RN   [11]
RP   EXPORT VIA THE TAT-SYSTEM, AND MUTAGENESIS OF ARG-17.
RX   PubMed=10801884; DOI=10.1074/jbc.m909289199;
RA   Sambasivarao D., Turner R.J., Simala-Grant J.L., Shaw G., Hu J.,
RA   Weiner J.H.;
RT   "Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide
RT   reductase of Escherichia coli.";
RL   J. Biol. Chem. 275:22526-22531(2000).
RN   [12]
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).
RN   [13]
RP   INTERACTION OF SIGNAL PEPTIDE WITH DMSD; TATB AND TATC, AND MUTAGENESIS OF
RP   17-ARG-ARG-18.
RX   PubMed=20169075; DOI=10.1371/journal.pone.0009225;
RA   Kostecki J.S., Li H., Turner R.J., DeLisa M.P.;
RT   "Visualizing interactions along the Escherichia coli twin-arginine
RT   translocation pathway using protein fragment complementation.";
RL   PLoS ONE 5:E9225-E9225(2010).
CC   -!- FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) to
CC       dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase
CC       under anaerobic conditions, with DMSO being the terminal electron
CC       acceptor. Terminal reductase during anaerobic growth on various
CC       sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically
CC       on DMSO as respiratory oxidant. {ECO:0000269|PubMed:3062312}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a menaquinone + dimethyl sulfide + H2O = a menaquinol +
CC         dimethyl sulfoxide; Xref=Rhea:RHEA:28494, Rhea:RHEA-COMP:9537,
CC         Rhea:RHEA-COMP:9539, ChEBI:CHEBI:15377, ChEBI:CHEBI:16374,
CC         ChEBI:CHEBI:17437, ChEBI:CHEBI:18151, ChEBI:CHEBI:28262; EC=1.8.5.3;
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;
CC         Evidence={ECO:0000269|PubMed:10224050, ECO:0000269|PubMed:3280546,
CC         ECO:0000269|PubMed:7721698};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:10224050,
CC       ECO:0000269|PubMed:3280546, ECO:0000269|PubMed:7721698};
CC   -!- ACTIVITY REGULATION: Inhibited by dithionite, sodium hydrogensulfite
CC       and tungstate. {ECO:0000269|PubMed:7721698,
CC       ECO:0000269|PubMed:8969520}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.043 mM for 2-chloropyridine N-oxide (at pH 5 and at 30 degrees
CC         Celsius) {ECO:0000269|PubMed:8969520};
CC         KM=0.045 mM for 3-amidopyridine N-oxide (at pH 5 and at 30 degrees
CC         Celsius) {ECO:0000269|PubMed:8969520};
CC         KM=0.06 mM for tertramethylene sulfoxide (at pH 5 and at 30 degrees
CC         Celsius) {ECO:0000269|PubMed:8969520};
CC         KM=0.09 mM for methionine sulfoxide (at pH 5 and at 30 degrees
CC         Celsius) {ECO:0000269|PubMed:8969520};
CC         KM=0.246 mM for 4-phenylpyridine N-oxide (at pH 5 and at 30 degrees
CC         Celsius) {ECO:0000269|PubMed:8969520};
CC         KM=0.830 mM for dimethyldodecylamin N-oxide (at pH 5 and at 30
CC         degrees Celsius) {ECO:0000269|PubMed:8969520};
CC         KM=0.18 mM for DMSO (at pH 6.8 and at 23 degrees Celsius)
CC         {ECO:0000269|PubMed:3280546};
CC         KM=0.47 mM for L-methionine sulfoxide (at pH 6.8 and at 23 degrees
CC         Celsius) {ECO:0000269|PubMed:3280546};
CC         KM=0.5 mM for nicotinamide N-oxide (at pH 6.8 and at 23 degrees
CC         Celsius) {ECO:0000269|PubMed:3280546};
CC         KM=0.6 mM for TMAO (at pH 6.8 and at 23 degrees Celsius)
CC         {ECO:0000269|PubMed:3280546};
CC         KM=1.0 mM for 4-picoline N-oxide (at pH 6.8 and at 23 degrees
CC         Celsius) {ECO:0000269|PubMed:3280546};
CC         KM=20.2 mM for TMAO (at pH 5 and at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:8969520};
CC   -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
CC       (DmsAB) and a membrane anchor protein (DmsC).
CC       {ECO:0000269|PubMed:3280546}.
CC   -!- INTERACTION:
CC       P18775; P18776: dmsB; NbExp=2; IntAct=EBI-4411104, EBI-1120825;
CC       P18775; P69853: dmsD; NbExp=8; IntAct=EBI-4411104, EBI-4406374;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2170332,
CC       ECO:0000269|PubMed:3280546}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:2170332, ECO:0000269|PubMed:3280546}; Cytoplasmic
CC       side {ECO:0000269|PubMed:2170332, ECO:0000269|PubMed:3280546}.
CC   -!- PTM: Exported by the Tat system. The position of the signal peptide
CC       cleavage has been experimentally proven. Can also be exported by the
CC       Sec system.
CC   -!- MISCELLANEOUS: The Tat signal sequence is essential for the expression
CC       of dmsA, the stability of the DmsAB dimer and membrane targeting.
CC       Despite the presence of a signal sequence, DmsA is not exported to the
CC       periplasm.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA83843.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; J03412; AAA83843.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73980.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35626.2; -; Genomic_DNA.
DR   PIR; S03785; S03785.
DR   RefSeq; NP_415414.4; NC_000913.3.
DR   RefSeq; WP_000850303.1; NZ_SSZK01000002.1.
DR   AlphaFoldDB; P18775; -.
DR   SMR; P18775; -.
DR   BioGRID; 4261945; 69.
DR   BioGRID; 849882; 3.
DR   ComplexPortal; CPX-320; DmaABC DMSO reductase complex.
DR   DIP; DIP-9452N; -.
DR   IntAct; P18775; 8.
DR   MINT; P18775; -.
DR   STRING; 511145.b0894; -.
DR   TCDB; 5.A.3.3.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   jPOST; P18775; -.
DR   PaxDb; P18775; -.
DR   PRIDE; P18775; -.
DR   EnsemblBacteria; AAC73980; AAC73980; b0894.
DR   EnsemblBacteria; BAA35626; BAA35626; BAA35626.
DR   GeneID; 945508; -.
DR   KEGG; ecj:JW5118; -.
DR   KEGG; eco:b0894; -.
DR   PATRIC; fig|1411691.4.peg.1383; -.
DR   EchoBASE; EB0228; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   InParanoid; P18775; -.
DR   OMA; CPLDCPD; -.
DR   PhylomeDB; P18775; -.
DR   BioCyc; EcoCyc:DMSA-MON; -.
DR   BioCyc; MetaCyc:DMSA-MON; -.
DR   BRENDA; 1.8.5.3; 2026.
DR   PRO; PR:P18775; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009390; C:dimethyl sulfoxide reductase complex; IDA:EcoCyc.
DR   GO; GO:0031237; C:intrinsic component of periplasmic side of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP:EcoCyc.
DR   GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IMP:EcoCyc.
DR   GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR   GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR   GO; GO:0018907; P:dimethyl sulfoxide metabolic process; IDA:ComplexPortal.
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   InterPro; IPR019546; TAT_signal_bac_arc.
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   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cell membrane; Direct protein sequencing; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Molybdenum; Oxidoreductase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..45
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:3062312"
FT   CHAIN           46..814
FT                   /note="Dimethyl sulfoxide reductase DmsA"
FT                   /id="PRO_0000019143"
FT   DOMAIN          56..118
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
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         71
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         104
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         172..176
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
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"
FT   BINDING         244..245
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         270..271
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         291..293
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         386..387
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         512..513
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         701
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         707..709
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         788
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   BINDING         804..805
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         17
FT                   /note="R->S: Not targeted to the membrane, does not support
FT                   anaerobic growth."
FT                   /evidence="ECO:0000269|PubMed:10801884"
FT   MUTAGEN         57
FT                   /note="K->D: No alteration of the growth, expression, or
FT                   catalytic activities."
FT                   /evidence="ECO:0000269|PubMed:8125918"
FT   MUTAGEN         67
FT                   /note="C->S: Electron transfer from the 4Fe-4S clusters of
FT                   DmsB to the Mo-bisMGD of DmsA is blocked. Little effect on
FT                   the coordination sphere of the molybdenum and only minor
FT                   effects on its redox chemistry."
FT                   /evidence="ECO:0000269|PubMed:10224050,
FT                   ECO:0000269|PubMed:8125918"
FT   MUTAGEN         71
FT                   /note="C->S: Cannot support growth."
FT                   /evidence="ECO:0000269|PubMed:8125918"
FT   MUTAGEN         104
FT                   /note="C->S: No alteration of the growth, expression, or
FT                   catalytic activities."
FT                   /evidence="ECO:0000269|PubMed:8125918"
FT   MUTAGEN         106
FT                   /note="R->S: Electron transfer from the 4Fe-4S clusters of
FT                   DmsB to the Mo-bisMGD of DmsA is blocked. Little effect on
FT                   the coordination sphere of the molybdenum and only minor
FT                   effects on its redox chemistry."
FT                   /evidence="ECO:0000269|PubMed:10224050,
FT                   ECO:0000269|PubMed:8125918"
SQ   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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