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Database: UniProt
Entry: P45575
LinkDB: P45575
Original site: P45575 
ID   DSVB_DESVH              Reviewed;         381 AA.
AC   P45575;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   10-APR-2019, entry version 126.
DE   RecName: Full=Sulfite reductase, dissimilatory-type subunit beta;
DE            EC=1.8.99.5 {ECO:0000269|PubMed:4725615, ECO:0000269|PubMed:8033912};
DE   AltName: Full=Desulfoviridin subunit beta {ECO:0000303|PubMed:4725615};
DE   AltName: Full=Dissimilatory sulfite reductase subunit beta {ECO:0000303|PubMed:18829451};
DE            Short=dSiR beta {ECO:0000303|PubMed:18829451};
DE   AltName: Full=Hydrogensulfite reductase subunit beta;
GN   Name=dsvB; Synonyms=dsrB {ECO:0000303|PubMed:18829451};
GN   OrderedLocusNames=DVU_0403;
OS   Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 /
OS   NCIMB 8303).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7887608;
RA   Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G.;
RT   "Conservation of the genes for dissimilatory sulfite reductase from
RT   Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their
RT   detection by PCR.";
RL   Appl. Environ. Microbiol. 61:290-296(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D.,
RA   Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R.,
RA   Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-16, AND SUBUNIT.
RX   PubMed=1555572; DOI=10.1111/j.1432-1033.1992.tb16757.x;
RA   Pierik A.J., Duyvis M.G., van Helvoort J.M.L.M., Wolbert R.B.G.,
RA   Hagen W.R.;
RT   "The third subunit of desulfoviridin-type dissimilatory sulfite
RT   reductases.";
RL   Eur. J. Biochem. 205:111-115(1992).
RN   [4]
RP   CATALYTIC ACTIVITY.
RX   PubMed=4725615;
RA   Lee J.-P., LeGall J., Peck H.D. Jr.;
RT   "Isolation of assimilatroy- and dissimilatory-type sulfite reductases
RT   from Desulfovibrio vulgaris.";
RL   J. Bacteriol. 115:529-542(1973).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, EPR SPECTROSCOPY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=8033912; DOI=10.1111/j.1432-1033.1994.tb18968.x;
RA   Wolfe B.M., Lui S.M., Cowan J.A.;
RT   "Desulfoviridin, a multimeric-dissimilatory sulfite reductase from
RT   Desulfovibrio vulgaris (Hildenborough). Purification,
RT   characterization, kinetics and EPR studies.";
RL   Eur. J. Biochem. 223:79-89(1994).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH DSVA; DSVC;
RP   IRON-SULFUR (4FE-4S) AND SIROHEME, SUBUNIT, COFACTOR, AND REACTION
RP   MECHANISM.
RX   PubMed=18829451; DOI=10.1074/jbc.M805643200;
RA   Oliveira T.F., Vonrhein C., Matias P.M., Venceslau S.S.,
RA   Pereira I.A.C., Archer M.;
RT   "The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite
RT   reductase bound to DsrC provides novel insights into the mechanism of
RT   sulfate respiration.";
RL   J. Biol. Chem. 283:34141-34149(2008).
CC   -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is
CC       the terminal oxidation reaction in sulfate respiration, a process
CC       catalyzed by the sulfate-reducing bacteria.
CC       {ECO:0000269|PubMed:1555572, ECO:0000269|PubMed:8033912}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DsrC protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide
CC         = [DsrC protein]-dithiol + 2 AH2 + H(+) + sulfite;
CC         Xref=Rhea:RHEA:47008, Rhea:RHEA-COMP:11722, Rhea:RHEA-
CC         COMP:11723, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058;
CC         EC=1.8.99.5; Evidence={ECO:0000269|PubMed:4725615,
CC         ECO:0000269|PubMed:8033912};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3
CC         H2O = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite;
CC         Xref=Rhea:RHEA:47020, Rhea:RHEA-COMP:11722, Rhea:RHEA-
CC         COMP:11724, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:61963;
CC         EC=1.8.99.5; Evidence={ECO:0000269|PubMed:4725615,
CC         ECO:0000269|PubMed:8033912};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:18829451};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit.
CC       {ECO:0000269|PubMed:18829451};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000269|PubMed:18829451};
CC       Note=Binds 1 siroheme per subunit. {ECO:0000269|PubMed:18829451};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.06 mM for sulfite {ECO:0000269|PubMed:8033912};
CC         KM=0.028 mM for nitrite {ECO:0000269|PubMed:8033912};
CC         Note=kcat is 0.31 (sec-1) for sulfite. kcat is 0.038 (sec-1) for
CC         nitrite. {ECO:0000269|PubMed:8033912};
CC   -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma
CC       subunits. {ECO:0000269|PubMed:1555572,
CC       ECO:0000269|PubMed:18829451}.
CC   -!- INTERACTION:
CC       P45574:dsvA; NbExp=5; IntAct=EBI-9016987, EBI-9016991;
DR   EMBL; U16723; AAA70108.1; -; Genomic_DNA.
DR   EMBL; AE017285; AAS94886.1; -; Genomic_DNA.
DR   PIR; S21238; S21238.
DR   RefSeq; WP_010937710.1; NC_002937.3.
DR   RefSeq; YP_009627.1; NC_002937.3.
DR   PDB; 2V4J; X-ray; 2.10 A; B/E=1-381.
DR   PDBsum; 2V4J; -.
DR   ProteinModelPortal; P45575; -.
DR   SMR; P45575; -.
DR   IntAct; P45575; 4.
DR   STRING; 882.DVU_0403; -.
DR   PaxDb; P45575; -.
DR   EnsemblBacteria; AAS94886; AAS94886; DVU_0403.
DR   GeneID; 2796153; -.
DR   KEGG; dvu:DVU0403; -.
DR   PATRIC; fig|882.5.peg.380; -.
DR   eggNOG; ENOG4105PJW; Bacteria.
DR   eggNOG; COG2221; LUCA.
DR   KO; K11181; -.
DR   OMA; HTQGWLH; -.
DR   BioCyc; DVUL882:G1GT1-424-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-12512; -.
DR   BRENDA; 1.8.99.3; 1914.
DR   EvolutionaryTrace; P45575; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0018551; F:hydrogensulfite reductase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011808; DsrB.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer_like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   TIGRFAMs; TIGR02066; dsrB; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:1555572}.
FT   CHAIN         2    381       Sulfite reductase, dissimilatory-type
FT                                subunit beta.
FT                                /FTId=PRO_0000080032.
FT   DOMAIN      249    276       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       151    151       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000244|PDB:2V4J,
FT                                ECO:0000269|PubMed:18829451}.
FT   METAL       188    188       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000244|PDB:2V4J,
FT                                ECO:0000269|PubMed:18829451}.
FT   METAL       189    189       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000244|PDB:2V4J,
FT                                ECO:0000269|PubMed:18829451}.
FT   METAL       193    193       Iron (siroheme axial ligand).
FT                                {ECO:0000305|PubMed:18829451}.
FT   METAL       193    193       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000244|PDB:2V4J,
FT                                ECO:0000269|PubMed:18829451}.
FT   METAL       231    231       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000244|PDB:2V4J,
FT                                ECO:0000269|PubMed:18829451}.
FT   METAL       258    258       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000244|PDB:2V4J,
FT                                ECO:0000269|PubMed:18829451}.
FT   METAL       261    261       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000244|PDB:2V4J,
FT                                ECO:0000269|PubMed:18829451}.
FT   METAL       264    264       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000244|PDB:2V4J,
FT                                ECO:0000269|PubMed:18829451}.
FT   TURN         13     16       {ECO:0000244|PDB:2V4J}.
FT   TURN         26     29       {ECO:0000244|PDB:2V4J}.
FT   HELIX        32     37       {ECO:0000244|PDB:2V4J}.
FT   STRAND       41     48       {ECO:0000244|PDB:2V4J}.
FT   STRAND       51     56       {ECO:0000244|PDB:2V4J}.
FT   STRAND       61     67       {ECO:0000244|PDB:2V4J}.
FT   STRAND       71     74       {ECO:0000244|PDB:2V4J}.
FT   HELIX        75     88       {ECO:0000244|PDB:2V4J}.
FT   STRAND       92     95       {ECO:0000244|PDB:2V4J}.
FT   STRAND      101    107       {ECO:0000244|PDB:2V4J}.
FT   HELIX       108    120       {ECO:0000244|PDB:2V4J}.
FT   STRAND      128    130       {ECO:0000244|PDB:2V4J}.
FT   STRAND      136    139       {ECO:0000244|PDB:2V4J}.
FT   HELIX       147    149       {ECO:0000244|PDB:2V4J}.
FT   HELIX       159    173       {ECO:0000244|PDB:2V4J}.
FT   STRAND      178    180       {ECO:0000244|PDB:2V4J}.
FT   STRAND      184    189       {ECO:0000244|PDB:2V4J}.
FT   HELIX       196    198       {ECO:0000244|PDB:2V4J}.
FT   STRAND      199    206       {ECO:0000244|PDB:2V4J}.
FT   HELIX       215    221       {ECO:0000244|PDB:2V4J}.
FT   HELIX       224    229       {ECO:0000244|PDB:2V4J}.
FT   STRAND      236    243       {ECO:0000244|PDB:2V4J}.
FT   STRAND      246    253       {ECO:0000244|PDB:2V4J}.
FT   HELIX       255    257       {ECO:0000244|PDB:2V4J}.
FT   HELIX       263    267       {ECO:0000244|PDB:2V4J}.
FT   TURN        276    278       {ECO:0000244|PDB:2V4J}.
FT   STRAND      280    285       {ECO:0000244|PDB:2V4J}.
FT   STRAND      292    294       {ECO:0000244|PDB:2V4J}.
FT   STRAND      300    307       {ECO:0000244|PDB:2V4J}.
FT   TURN        310    312       {ECO:0000244|PDB:2V4J}.
FT   HELIX       314    330       {ECO:0000244|PDB:2V4J}.
FT   HELIX       337    344       {ECO:0000244|PDB:2V4J}.
FT   HELIX       346    353       {ECO:0000244|PDB:2V4J}.
FT   HELIX       359    361       {ECO:0000244|PDB:2V4J}.
FT   HELIX       367    372       {ECO:0000244|PDB:2V4J}.
SQ   SEQUENCE   381 AA;  42519 MW;  678A04F716050D63 CRC64;
     MAFISSGYNP EKPMANRITD IGPRKFDEFF PPVIAKNFGS WLYHEILEPG VLMHVAESGD
     KVYTVRVGAA RLMSITHIRE MCDIADKYCG GHLRFTTRNN VEFMVADEAS LKALKEDLAS
     RKFDGGSLKF PIGGTGAGVS NIVHTQGWVH CHTPATDASG PVKAIMDEVF EDFQSMRLPA
     PVRISLACCI NMCGAVHCSD IGVVGIHRKP PMIDHEWTDQ LCEIPLAVAS CPTAAVRPTK
     LEIGDKKVNT IAIKNERCMY CGNCYTMCPA LPISDGEGDG VVIMVGGKVS NRISMPKFSK
     VVVAYIPNEP PRWPSLTKTI KHIIEVYSAN AYKYERLGEW AERIGWERFF SLTGLEFSHH
     LIDDFRDPAY YTWRQSTQFK F
//
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