Skip Header

Contribute Send feedback
Read comments (?) or add your own

P45573 (DSVC_DESVH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome] [HAMAP]
Taxonomic identifier882 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio ›

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
Reference proteome
Gene Ontology (GO)
   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

Secondary structure

1 .................... 105
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45573 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
[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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-23.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L05610 Genomic DNA. Translation: AAA23366.1.
AE017285 Genomic DNA. Translation: AAS97248.1.
PIRS29376.
RefSeqYP_011988.1. NC_002937.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10C/F1-105[»]
ProteinModelPortalP45573.
ModBaseSearch...

Protein-protein interaction databases

STRING882.DVU2776.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS97248; AAS97248; DVU_2776.
GeneID2796326.
KEGGdvu:DVU2776.
PATRIC32065124. VBIDesVul119526_2511.

Phylogenomic databases

eggNOGCOG2920.
KOK11179.
OMANSRYLQR.
ProtClustDBCLSK926783.

Enzyme and pathway databases

BioCycDVUL882:GJIL-2844-MONOMER.
MetaCyc:MONOMER-12513.

Family and domain databases

InterProIPR025526. DsrC-like_dom.
IPR007453. DsrC/TusE.
[Graphical view]
PfamPF04358. DsrC. 1 hit.
[Graphical view]
PIRSFPIRSF006223. DsrC_TusE. 1 hit.
SUPFAMSSF69721. DsrC. 1 hit.
TIGRFAMsTIGR03342. dsrC_tusE_dsvC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP45573.

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: May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents