DSVB_DESVH
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 03-AUG-2022, entry version 141.
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 ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
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 / NCIMB 8303 / VKM B-1760 / 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]-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-COMP:11723,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:17499, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058; EC=1.8.99.5;
CC Evidence={ECO:0000269|PubMed:4725615, ECO:0000269|PubMed:8033912};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3 H2O
CC = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite;
CC Xref=Rhea:RHEA:47020, Rhea:RHEA-COMP:11722, Rhea:RHEA-COMP:11724,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:61963; EC=1.8.99.5;
CC Evidence={ECO:0000269|PubMed:4725615, 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; NZ_CABHLV010000001.1.
DR RefSeq; YP_009627.1; NC_002937.3.
DR PDB; 2V4J; X-ray; 2.10 A; B/E=1-381.
DR PDBsum; 2V4J; -.
DR AlphaFoldDB; P45575; -.
DR SMR; P45575; -.
DR IntAct; P45575; 4.
DR STRING; 882.DVU_0403; -.
DR PaxDb; P45575; -.
DR PRIDE; P45575; -.
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 OMA; HTQGWLH; -.
DR PhylomeDB; P45575; -.
DR BioCyc; MetaCyc:MON-12512; -.
DR BRENDA; 1.8.99.5; 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 Gene3D; 3.30.413.10; -; 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 PANTHER; PTHR11493; PTHR11493; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR SUPFAM; SSF55124; SSF55124; 1.
DR SUPFAM; SSF56014; SSF56014; 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; 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 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
