ID   DSVB_NITV2              Reviewed;         381 AA.
AC   P45575;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 158.
DE   RecName: Full=Sulfite reductase, dissimilatory-type subunit beta;
DE            EC=1.8.1.22 {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   Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 /
OS   NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7887608; DOI=10.1128/aem.61.1.290-296.1995;
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 detection by
RT   PCR.";
RL   Appl. Environ. Microbiol. 61:290-296(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 /
RC   Hildenborough;
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., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   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; DOI=10.1128/jb.115.2.529-542.1973;
RA   Lee J.-P., LeGall J., Peck H.D. Jr.;
RT   "Isolation of assimilatory- and dissimilatory-type sulfite reductases from
RT   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, characterization,
RT   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., Pereira I.A.C.,
RA   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 the
CC       terminal oxidation reaction in sulfate respiration, a process catalyzed
CC       by the sulfate-reducing bacteria. {ECO:0000269|PubMed:1555572,
CC       ECO:0000269|PubMed:8033912}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DsrC protein]-trisulfide + NAD(+) + 3 H2O = [DsrC protein]-
CC         dithiol + sulfite + NADH + 3 H(+); Xref=Rhea:RHEA:78943, Rhea:RHEA-
CC         COMP:11723, Rhea:RHEA-COMP:19152, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:229579;
CC         EC=1.8.1.22; 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 subunits.
CC       {ECO:0000269|PubMed:1555572, ECO:0000269|PubMed:18829451}.
CC   -!- INTERACTION:
CC       P45575; P45574: dsvA; NbExp=5; IntAct=EBI-9016987, EBI-9016991;
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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   PDB; 2V4J; X-ray; 2.10 A; B/E=1-381.
DR   AlphaFoldDB; P45575; -.
DR   SMR; P45575; -.
DR   IntAct; P45575; 4.
DR   STRING; 882.DVU_0403; -.
DR   PaxDb; 882-DVU_0403; -.
DR   EnsemblBacteria; AAS94886; AAS94886; DVU_0403.
DR   KEGG; dvu:DVU_0403; -.
DR   PATRIC; fig|882.5.peg.380; -.
DR   eggNOG; COG2221; Bacteria.
DR   HOGENOM; CLU_044442_0_0_7; -.
DR   OrthoDB; 9766142at2; -.
DR   PhylomeDB; P45575; -.
DR   BioCyc; MetaCyc:MONOMER-12512; -.
DR   BRENDA; 1.8.1.22; 1914.
DR   EvolutionaryTrace; P45575; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:TreeGrafter.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0018551; F:dissimilatory sulfite reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:TreeGrafter.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:TreeGrafter.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.30.70.3340; -; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
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   InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   NCBIfam; TIGR02066; dsrB; 1.
DR   PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR   PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PDBsum; 2V4J; -.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1555572"
FT   CHAIN           2..381
FT                   /note="Sulfite reductase, dissimilatory-type subunit beta"
FT                   /id="PRO_0000080032"
FT   DOMAIN          249..276
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         151
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         188
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         189
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         193
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         193
FT                   /ligand="siroheme"
FT                   /ligand_id="ChEBI:CHEBI:60052"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305|PubMed:18829451"
FT   BINDING         231
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         258
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         261
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         264
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   TURN            13..16
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   TURN            26..29
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           32..37
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           75..88
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          101..107
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           108..120
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          136..139
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           159..173
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          184..189
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           196..198
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          199..206
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           215..221
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           224..229
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          236..243
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          246..253
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           263..267
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   TURN            276..278
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          280..285
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          300..307
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   TURN            310..312
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           314..330
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           337..344
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           346..353
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           359..361
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           367..372
FT                   /evidence="ECO:0007829|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
//