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Putative dimethyl sulfoxide reductase catalytic subunit A (DMSO reductase subunit A) (EC 1.8.5.3)

 DMSA_HALSA              Reviewed;         837 AA.
Q9HR74;
14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
28-FEB-2018, entry version 91.
RecName: Full=Putative dimethyl sulfoxide reductase catalytic subunit A;
Short=DMSO reductase subunit A;
EC=1.8.5.3;
Flags: Precursor;
Name=dmsA; OrderedLocusNames=VNG_0829G;
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
(Halobacterium halobium).
Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
Halobacteriaceae; Halobacterium.
NCBI_TaxID=64091;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
PubMed=11016950; DOI=10.1073/pnas.190337797;
Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M.,
Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J.,
Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A.,
Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W.,
Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H.,
Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H.,
Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D.,
Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.;
"Genome sequence of Halobacterium species NRC-1.";
Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
[2]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
PubMed=15716436; DOI=10.1128/JB.187.5.1659-1667.2005;
Muller J.A., DasSarma S.;
"Genomic analysis of anaerobic respiration in the archaeon
Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine
N-oxide as terminal electron acceptors.";
J. Bacteriol. 187:1659-1667(2005).
-!- FUNCTION: Dimethyl sulfoxide (DMSO) reductase catalyzes the
reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS)
during anaerobic respiration; it can also use trimethylamine N-
oxide (TMAO) as terminal electron acceptor. Required for anaerobic
respiration on DMSO and TMAO; subunit A is proposed to be
catalytically active. {ECO:0000269|PubMed:15716436}.
-!- CATALYTIC ACTIVITY: Dimethylsulfide + menaquinone + H(2)O =
dimethylsulfoxide + menaquinol.
-!- 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};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000305};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
-!- SUBUNIT: Probable multiprotein complex that likely consists of
DmsA, DmsB and DmsC.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral
membrane protein {ECO:0000305}.
-!- INDUCTION: By anaerobic conditions. Its expression is under the
control of DmsR. {ECO:0000269|PubMed:15716436}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has not been experimentally proven.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow under
anaerobic conditions using either DMSO or TMAO as terminal
electron acceptors. {ECO:0000269|PubMed:15716436}.
-!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE004437; AAG19284.1; -; Genomic_DNA.
PIR; H84239; H84239.
RefSeq; WP_010902580.1; NC_002607.1.
ProteinModelPortal; Q9HR74; -.
SMR; Q9HR74; -.
STRING; 64091.VNG0829G; -.
TCDB; 5.A.3.3.3; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
PaxDb; Q9HR74; -.
EnsemblBacteria; AAG19284; AAG19284; VNG_0829G.
GeneID; 5952709; -.
KEGG; hal:VNG_0829G; -.
PATRIC; fig|64091.14.peg.637; -.
eggNOG; ENOG4102T1R; Archaea.
eggNOG; COG0243; LUCA.
InParanoid; Q9HR74; -.
KO; K00183; -.
OMA; HYGDYST; -.
OrthoDB; POG093Z00ML; -.
PhylomeDB; Q9HR74; -.
Proteomes; UP000000554; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS51318; TAT; 1.
2: Evidence at transcript level;
4Fe-4S; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane;
Metal-binding; Molybdenum; Oxidoreductase; Reference proteome; Signal.
SIGNAL 1 36 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648}.
CHAIN 37 837 Putative dimethyl sulfoxide reductase
catalytic subunit A.
/FTId=PRO_0000428975.
DOMAIN 53 110 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 60 60 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 64 64 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 68 68 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 96 96 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 200 200 Molybdenum. {ECO:0000250}.
SEQUENCE 837 AA; 92367 MW; B87E8623D4C63E9C CRC64;
MSDTDLNATR RDVLKSGAVA AVGLSGGGLL STLQEADDSD TAGDAVTSFL GEDQVVKTAC
SPNCRGKCPL DVFVRDGQIK KVEQQVPAAK TFKRGCTLGM THLQRVYNAD RLKYPMKRTS
WSPDDPQPDQ RGADAQFERI AWDDALDLVA DGIQRAKREY GPRSLLWHSG SGDGGITGYR
RLKELVGGLQ DDFTYGIDTN VGQGFNRVTG EGGVFMPPTN TADDWVNAET IIIWGSDIFA
SQFQMDAEWI LDAKRNGAKL VVVDPVYTNT AEKADLWLPI KPGKDTHLAL AMMQYIFEHD
HYDEAFLRSR TNAPALVRAD DGTLLDPASV TATPPEDGIV VFNTETGSPE VVPAETNGPF
ALFGEWTIDG TTVHTGLTAL REQASSYPPQ AVADTAGLAA ADIETAADWL ATRGPGGIMP
SYGVGRYLYG HVFGQTYATL LALTGDYGRH GNIHAQHPSY DGSYLETGDW NDPDGAAGVD
TYGYNRVLDL LANGDPVQTK FMYGMNSNML GNQFPERDRW LDAMSNLDTV VWADIYHTPT
TRQADIILPA AHWFETEDLL TTYTHPNLSY RTKAHDPLWE ARDDYYIMAG LAQRLGHGDK
FPDDKHDVLD RFVKNDDRLS WDALRETGTV ATDETPTVAY TDEFGTESGR ITVYDDDAPV
EEGPALPDDG VSLEVPKPLE ARTADDWAHA DEYPLLFMQK HSKWRIHSQW ANVPWLREIN
TEPQLDIHPK DATRRGIDDG EYVRVHNDRG SVVVRAKYND GIQPGLVNTD QGWWARDFVD
GHLQDLISAE TAKVGRTFAF YDCRVEVTRA ADEHQSNEYT QHNPRGSSGT ATDGDSS


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