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Protein

Sulfite reductase, dissimilatory-type subunit gamma

Gene

dsvC

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BioCyciDVUL882:GJIL-2844-MONOMER.
MetaCyc:MONOMER-12513.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase, dissimilatory-type subunit gamma (EC:1.8.99.3)
Alternative name(s):
Desulfoviridin subunit gamma
Hydrogensulfite reductase subunit gamma
Gene namesi
Name:dsvC
Ordered Locus Names:DVU_2776
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 105104Sulfite reductase, dissimilatory-type subunit gammaPRO_0000080033Add
BLAST

Proteomic databases

PaxDbiP45573.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi882.DVU2776.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi9 – 113Combined sources
Helixi22 – 243Combined sources
Helixi27 – 337Combined sources
Helixi34 – 374Combined sources
Helixi44 – 6017Combined sources
Helixi66 – 738Combined sources
Helixi77 – 837Combined sources
Helixi87 – 904Combined sources
Helixi92 – 965Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10C/F1-105[»]
ProteinModelPortaliP45573.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45573.

Family & Domainsi

Sequence similaritiesi

Belongs to the DsrC/TusE family.Curated

Phylogenomic databases

eggNOGiENOG4108Z0T. Bacteria.
COG2920. LUCA.
KOiK11179.
OMAiEYNTSPA.
OrthoDBiEOG60390T.
PhylomeDBiP45573.

Family and domain databases

InterProiIPR025526. DsrC-like_dom.
IPR007453. DsrC/TusE.
[Graphical view]
PfamiPF04358. DsrC. 1 hit.
[Graphical view]
PIRSFiPIRSF006223. DsrC_TusE. 1 hit.
SUPFAMiSSF69721. SSF69721. 1 hit.
TIGRFAMsiTIGR03342. dsrC_tusE_dsvC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P45573-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVTYKGKS FEVDEDGFLL RFDDWCPEWV EYVKESEGIS DISPDHQKII
60 70 80 90 100
DFLQDYYKKN GIAPMVRILS KNTGFKLKEV YELFPSGPGK GACKMAGLPK

PTGCV
Length:105
Mass (Da):11,873
Last modified:January 23, 2007 - v2
Checksum:iC1C68DFBA3801EC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151E → D AA sequence (PubMed:1555572).Curated
Sequence conflicti20 – 201L → LI AA sequence (PubMed:1555572).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05610 Genomic DNA. Translation: AAA23366.1.
AE017285 Genomic DNA. Translation: AAS97248.1.
PIRiS29376.
RefSeqiWP_010940042.1. NC_002937.3.
YP_011988.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS97248; AAS97248; DVU_2776.
GeneIDi2796326.
KEGGidvu:DVU2776.
PATRICi32065124. VBIDesVul119526_2511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05610 Genomic DNA. Translation: AAA23366.1.
AE017285 Genomic DNA. Translation: AAS97248.1.
PIRiS29376.
RefSeqiWP_010940042.1. NC_002937.3.
YP_011988.1. NC_002937.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10C/F1-105[»]
ProteinModelPortaliP45573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi882.DVU2776.

Proteomic databases

PaxDbiP45573.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS97248; AAS97248; DVU_2776.
GeneIDi2796326.
KEGGidvu:DVU2776.
PATRICi32065124. VBIDesVul119526_2511.

Phylogenomic databases

eggNOGiENOG4108Z0T. Bacteria.
COG2920. LUCA.
KOiK11179.
OMAiEYNTSPA.
OrthoDBiEOG60390T.
PhylomeDBiP45573.

Enzyme and pathway databases

BioCyciDVUL882:GJIL-2844-MONOMER.
MetaCyc:MONOMER-12513.

Miscellaneous databases

EvolutionaryTraceiP45573.

Family and domain databases

InterProiIPR025526. DsrC-like_dom.
IPR007453. DsrC/TusE.
[Graphical view]
PfamiPF04358. DsrC. 1 hit.
[Graphical view]
PIRSFiPIRSF006223. DsrC_TusE. 1 hit.
SUPFAMiSSF69721. SSF69721. 1 hit.
TIGRFAMsiTIGR03342. dsrC_tusE_dsvC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDSVC_DESVH
AccessioniPrimary (citable) accession number: P45573
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 11, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.