DSVC_DESVH
ID DSVC_DESVH Reviewed; 105 AA.
AC P45573;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Sulfite reductase, dissimilatory-type subunit gamma;
DE EC=1.8.99.5 {ECO:0000269|PubMed:1555572};
DE AltName: Full=Desulfoviridin subunit gamma;
DE AltName: Full=Hydrogensulfite reductase subunit gamma;
GN Name=dsvC; OrderedLocusNames=DVU_2776;
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], AND PROTEIN SEQUENCE OF 2-25.
RX PubMed=8436111; DOI=10.1111/j.1432-1033.1993.tb17576.x;
RA Karkhoff-Schweizer R.R., Bruschi M., Voordouw G.;
RT "Expression of the gamma-subunit gene of desulfoviridin-type dissimilatory
RT sulfite reductase and of the alpha- and beta-subunit genes is not
RT coordinately regulated.";
RL Eur. J. Biochem. 211:501-507(1993).
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 2-23, FUNCTION, AND CATALYTIC ACTIVITY.
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 X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH DSVA AND DSVB,
RP SUBUNIT, AND REACTION 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 -!- 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:1555572};
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:1555572};
CC -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
CC {ECO:0000269|PubMed:18829451}.
CC -!- INTERACTION:
CC P45573; P45574: dsvA; NbExp=3; IntAct=EBI-9017020, EBI-9016991;
CC P45573; Q72CN2: DVU_1251; NbExp=3; IntAct=EBI-9017020, EBI-10064808;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the DsrC/TusE family. {ECO:0000305}.
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DR EMBL; L05610; AAA23366.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS97248.1; -; Genomic_DNA.
DR PIR; S29376; S29376.
DR RefSeq; WP_010940042.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_011988.1; NC_002937.3.
DR PDB; 2V4J; X-ray; 2.10 A; C/F=1-105.
DR PDBsum; 2V4J; -.
DR AlphaFoldDB; P45573; -.
DR SMR; P45573; -.
DR IntAct; P45573; 4.
DR STRING; 882.DVU_2776; -.
DR PaxDb; P45573; -.
DR PRIDE; P45573; -.
DR EnsemblBacteria; AAS97248; AAS97248; DVU_2776.
DR KEGG; dvu:DVU_2776; -.
DR PATRIC; fig|882.5.peg.2511; -.
DR eggNOG; COG2920; Bacteria.
DR HOGENOM; CLU_153199_1_0_7; -.
DR OMA; EYNTSPA; -.
DR PhylomeDB; P45573; -.
DR BioCyc; MetaCyc:MON-12513; -.
DR EvolutionaryTrace; P45573; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.370; -; 1.
DR Gene3D; 3.30.1420.10; -; 1.
DR InterPro; IPR042072; DsrC-like_C.
DR InterPro; IPR025526; DsrC-like_dom_sf.
DR InterPro; IPR043163; DsrC-like_N.
DR InterPro; IPR007453; DsrC/TusE.
DR PANTHER; PTHR37010; PTHR37010; 1.
DR Pfam; PF04358; DsrC; 1.
DR PIRSF; PIRSF006223; DsrC_TusE; 1.
DR SUPFAM; SSF69721; SSF69721; 1.
DR TIGRFAMs; TIGR03342; dsrC_tusE_dsvC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1555572,
FT ECO:0000269|PubMed:8436111"
FT CHAIN 2..105
FT /note="Sulfite reductase, dissimilatory-type subunit gamma"
FT /id="PRO_0000080033"
FT CONFLICT 15
FT /note="E -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="L -> LI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2V4J"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 44..60
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:2V4J"
SQ SEQUENCE 105 AA; 11873 MW; C1C68DFBA3801EC0 CRC64;
MAEVTYKGKS FEVDEDGFLL RFDDWCPEWV EYVKESEGIS DISPDHQKII DFLQDYYKKN
GIAPMVRILS KNTGFKLKEV YELFPSGPGK GACKMAGLPK PTGCV
