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Database: UniProt
Entry: Q9HR73
LinkDB: Q9HR73
Original site: Q9HR73 
ID   DMSB_HALSA              Reviewed;         262 AA.
AC   Q9HR73;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   10-APR-2019, entry version 112.
DE   RecName: Full=Putative dimethyl sulfoxide reductase iron-sulfur subunit B;
DE            Short=DMSO reductase subunit B;
GN   Name=dmsB; Synonyms=hmoA; OrderedLocusNames=VNG_0830G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Halobacteriales; 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.,
RA   Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J.,
RA   Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A.,
RA   Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W.,
RA   Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H.,
RA   Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H.,
RA   Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D.,
RA   Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., 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   PUTATIVE FUNCTION, AND INDUCTION.
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
RT   Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine
RT   N-oxide as terminal electron acceptors.";
RL   J. Bacteriol. 187:1659-1667(2005).
CC   -!- FUNCTION: Dimethyl sulfoxide (DMSO) reductase catalyzes the
CC       reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS)
CC       during anaerobic respiration; it can also use trimethylamine N-
CC       oxide (TMAO) as terminal electron acceptor. Subunit B is proposed
CC       to be involved in electron transfer.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC   -!- SUBUNIT: Probable multiprotein complex that likely consists of
CC       DmsA, DmsB and DmsC.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By anaerobic conditions. Its expression is under the
CC       control of DmsR. {ECO:0000269|PubMed:15716436}.
DR   EMBL; AE004437; AAG19285.1; -; Genomic_DNA.
DR   PIR; A84240; A84240.
DR   RefSeq; WP_010902581.1; NC_002607.1.
DR   ProteinModelPortal; Q9HR73; -.
DR   SMR; Q9HR73; -.
DR   TCDB; 5.A.3.3.3; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   PaxDb; Q9HR73; -.
DR   EnsemblBacteria; AAG19285; AAG19285; VNG_0830G.
DR   GeneID; 5953698; -.
DR   KEGG; hal:VNG_0830G; -.
DR   PATRIC; fig|64091.14.peg.638; -.
DR   eggNOG; arCOG01500; Archaea.
DR   eggNOG; COG0437; LUCA.
DR   InParanoid; Q9HR73; -.
DR   KO; K00184; -.
DR   OMA; CMHCENT; -.
DR   OrthoDB; 105930at2157; -.
DR   PhylomeDB; Q9HR73; -.
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:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF13247; Fer4_11; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Cell membrane; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN         1    262       Putative dimethyl sulfoxide reductase
FT                                iron-sulfur subunit B.
FT                                /FTId=PRO_0000428977.
FT   DOMAIN        4     34       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       62     93       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       94    123       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        13     13       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        16     16       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        19     19       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        23     23       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        71     71       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        74     74       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        79     79       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        83     83       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       103    103       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       106    106       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       109    109       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       113    113       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       147    147       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       150    150       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       162    162       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       166    166       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   262 AA;  28824 MW;  B0F6C9C959FBC1BC CRC64;
     MTNYGLVIDQ ERCIGCQSCS LTCKQENNVP MGQFWNRVLT QGGDHVDTPS GDYPEGGDGG
     TLEMTYQPTA CQHCENAPCV KVCPVNATYT RDDGIVEIDY DKCMGCRYCM AACPYNARVF
     NWDEPEHRPE DGTGDVAERP QGVVEKCTFC SHRVEDGLDP ACVVNCPADA RIFGDLDDDD
     STVSKYIAEY DTHQLLDEKG TDPSTYYING EMSPGRPWKS KKLESELDDD EAAKAARRRS
     GSVENGYDVT PHVPAETAGG DD
//
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