DMSA_HALSA
ID DMSA_HALSA Reviewed; 837 AA.
AC Q9HR74;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative dimethyl sulfoxide reductase catalytic subunit A;
DE Short=DMSO reductase subunit A;
DE EC=1.8.5.3;
DE Flags: Precursor;
GN Name=dmsA; OrderedLocusNames=VNG_0829G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=15716436; DOI=10.1128/jb.187.5.1659-1667.2005;
RA Muller J.A., DasSarma S.;
RT "Genomic analysis of anaerobic respiration in the archaeon Halobacterium
RT sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal
RT electron acceptors.";
RL J. Bacteriol. 187:1659-1667(2005).
CC -!- FUNCTION: Dimethyl sulfoxide (DMSO) reductase catalyzes the reduction
CC of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) during anaerobic
CC respiration; it can also use trimethylamine N-oxide (TMAO) as terminal
CC electron acceptor. Required for anaerobic respiration on DMSO and TMAO;
CC subunit A is proposed to be catalytically active.
CC {ECO:0000269|PubMed:15716436}.
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=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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Probable multiprotein complex that likely consists of DmsA,
CC DmsB and DmsC.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By anaerobic conditions. Its expression is under the control
CC of DmsR. {ECO:0000269|PubMed:15716436}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow under
CC anaerobic conditions using either DMSO or TMAO as terminal electron
CC acceptors. {ECO:0000269|PubMed:15716436}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE004437; AAG19284.1; -; Genomic_DNA.
DR PIR; H84239; H84239.
DR RefSeq; WP_010902580.1; NC_002607.1.
DR AlphaFoldDB; Q9HR74; -.
DR SMR; Q9HR74; -.
DR STRING; 64091.VNG_0829G; -.
DR TCDB; 5.A.3.3.3; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; Q9HR74; -.
DR PRIDE; Q9HR74; -.
DR EnsemblBacteria; AAG19284; AAG19284; VNG_0829G.
DR GeneID; 5952709; -.
DR KEGG; hal:VNG_0829G; -.
DR PATRIC; fig|64091.14.peg.637; -.
DR HOGENOM; CLU_000422_13_3_2; -.
DR InParanoid; Q9HR74; -.
DR OMA; CPLDCPD; -.
DR OrthoDB; 1029at2157; -.
DR PhylomeDB; Q9HR74; -.
DR Proteomes; UP000000554; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02785; MopB_CT_4; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041945; DmsA_C.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
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 PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Molybdenum; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..36
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 37..837
FT /note="Putative dimethyl sulfoxide reductase catalytic
FT subunit A"
FT /id="PRO_0000428975"
FT DOMAIN 53..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT REGION 813..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 68
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 200
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 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
