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Reviewed, UniProtKB/Swiss-Prot P45573 (DSVC_DESVH)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sulfite reductase, dissimilatory-type subunit gamma
    EC=1.8.99.3
Alternative name(s):
    Desulfoviridin subunit gamma
    Hydrogensulfite reductase subunit gamma
Gene names
Name: dsvC
Ordered Locus Names: DVU_2776
OrganismDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Complete proteome] [HAMAP]
Taxonomic identifier882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

(O3S.S.SO3)2- + acceptor + 2 H2O + OH- = 3 HSO3- + reduced acceptor.

Subunit structure

Heterohexamer of two alpha, two beta and two gamma subunits.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the dsrC/tusE family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydrogensulfite reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.3
Chain2 – 105104Sulfite reductase, dissimilatory-type subunit gamma
PRO_0000080033

Experimental info

Sequence conflict151E → D AA sequence Ref.3
Sequence conflict201L → LI AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P45573-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C1C68DFBA3801EC0

FASTA10511,873
        10         20         30         40         50         60 
MAEVTYKGKS FEVDEDGFLL RFDDWCPEWV EYVKESEGIS DISPDHQKII DFLQDYYKKN 

        70         80         90        100 
GIAPMVRILS KNTGFKLKEV YELFPSGPGK GACKMAGLPK PTGCV 

« Hide

References

« Hide 'large scale' references
[1]"Expression of the gamma-subunit gene of desulfoviridin-type dissimilatory sulfite reductase and of the alpha- and beta-subunit genes is not coordinately regulated."
Karkhoff-Schweizer R.R., Bruschi M., Voordouw G.
Eur. J. Biochem. 211:501-507(1993) [PubMed: 8436111] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-25.
[2]"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough."
Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. expand/collapse author list , Haft D.H., Selengut J., Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.
Nat. Biotechnol. 22:554-559(2004) [PubMed: 15077118] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The third subunit of desulfoviridin-type dissimilatory sulfite reductases."
Pierik A.J., Duyvis M.G., van Helvoort J.M.L.M., Wolbert R.B.G., Hagen W.R.
Eur. J. Biochem. 205:111-115(1992) [PubMed: 1555572] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-23.
+Additional computationally mapped references.

Cross-references

Sequence databases

L05610 Genomic DNA. Translation: AAA23366.1.
AE017285 Genomic DNA. Translation: AAS97248.1.
PIRS29376.
RefSeqYP_011988.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10C/F1-105[»]
ModBaseSearch...

Genome annotation databases

GeneID2796326.
GenomeReviewsGene locus DVU_2776 in contig AE017285_GR.
KEGGdvu:DVU2776.
TIGRDVU_2776.

Phylogenomic databases

HOGENOMP45573.
OMAP45573. YQIAPAV.

Enzyme and pathway databases

BioCycDVUL882:DVU_2776-MON.
MetaCyc:MON-12513.

Family and domain databases

InterProIPR007453. DsrC-like.
[Graphical view]
Gene3DG3DSA:1.10.10.370. DsrC. 1 hit.
PfamPF04358. DsrC. 1 hit.
[Graphical view]
ProDomPD012617. DsrC. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03342. dsrC_tusE_dsvC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDSVC_DESVH
AccessionPrimary (citable) accession number: P45573
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents