ID   DSVC_NITV2              Reviewed;         105 AA.
AC   P45573;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 143.
DE   RecName: Full=Sulfite reductase, dissimilatory-type subunit gamma;
DE            EC=1.8.1.22 {ECO:0000269|PubMed:1555572};
DE   AltName: Full=Desulfoviridin subunit gamma;
DE   AltName: Full=Hydrogensulfite reductase subunit gamma;
GN   Name=dsvC; OrderedLocusNames=DVU_2776;
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], 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 / 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 2-23, 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 IN COMPLEX WITH DSVA AND DSVB, SUBUNIT, 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   -!- 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: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; NC_002937.3.
DR   PDB; 2V4J; X-ray; 2.10 A; C/F=1-105.
DR   AlphaFoldDB; P45573; -.
DR   SMR; P45573; -.
DR   IntAct; P45573; 4.
DR   STRING; 882.DVU_2776; -.
DR   PaxDb; 882-DVU_2776; -.
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; ADWHPDM; -.
DR   OrthoDB; 9786347at2; -.
DR   PhylomeDB; P45573; -.
DR   BioCyc; MetaCyc:MONOMER-12513; -.
DR   EvolutionaryTrace; P45573; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0018551; F:dissimilatory sulfite reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0097163; F:sulfur carrier activity; IEA:TreeGrafter.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:TreeGrafter.
DR   Gene3D; 3.30.1420.10; -; 1.
DR   Gene3D; 1.10.10.370; DsrC-like protein, C-terminal domain; 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   NCBIfam; TIGR03342; dsrC_tusE_dsvC; 1.
DR   PANTHER; PTHR37010; SULFURTRANSFERASE TUSE; 1.
DR   PANTHER; PTHR37010:SF1; SULFURTRANSFERASE TUSE; 1.
DR   Pfam; PF04358; DsrC; 1.
DR   PIRSF; PIRSF006223; DsrC_TusE; 1.
DR   SUPFAM; SSF69721; DsrC, the gamma subunit of dissimilatory sulfite reductase; 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           88..93
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           98..101
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
//