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Reviewed, UniProtKB/Swiss-Prot O33998 (DSRA_CHRVI)

Last modified February 9, 2010. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | 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

Names and origin

Protein namesRecommended name:
    Sulfite reductase, dissimilatory-type subunit alpha
    EC=1.8.99.3
Alternative name(s):
    Hydrogensulfite reductase subunit alpha
Gene names
Name: dsrA
OrganismChromatium vinosum (Allochromatium vinosum)
Taxonomic identifier1049 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existencePredicted.

General annotation (Comments)

Function

Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.

Catalytic activity

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

Cofactor

Binds 1 4Fe-4S cluster per subunit.

Binds 2 sirohemes per subunit.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Sulfite reductase, dissimilatory-type subunit alpha
PRO_0000080026

Sites

Metal binding1701Iron (heme axial ligand) Potential
Metal binding1761Iron (heme axial ligand) Potential
Metal binding2141Iron (heme axial ligand) Potential
Metal binding2181Iron (heme axial ligand) Potential
Metal binding2641Iron-sulfur (4Fe-4S) Potential
Metal binding2841Iron-sulfur (4Fe-4S) Potential
Metal binding2871Iron-sulfur (4Fe-4S) Potential
Metal binding2901Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
O33998-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 474680A622F37B40

FASTA41746,791
        10         20         30         40         50         60 
MAIDKHATPM LDQLETGPWP SFISGIKRLR DQHPDARINA VTNDLLGQLE HSYETRKGYW 

        70         80         90        100        110        120 
KGGTVSVFGY GGGIIPRFSE VGKVFPSSKE FHTVRVQPPA GNHYTTAMLR QLADTWEKYG 

       130        140        150        160        170        180 
SGLITFHGQT GNIMFIGVDT PNTQNFFDEI NDYGWDLGGA GPCVRTAMSC VGSARCEMSC 

       190        200        210        220        230        240 
TNELKAHRLL VNNFTDDVHR PALPYKFKFK VSGCPNDCQN AIERSDFAVL GTWRDDMKVD 

       250        260        270        280        290        300 
QAEVKHYIAD KGRQYYIDNV ITRCPTKALS LNDDDTLDVN NRDCVRCMHC LNVMPKALHP 

       310        320        330        340        350        360 
GDDKGVTILI GGKRTLKIGD LMGTVVVPFK KLETEEDYES LVELAETIID FWAENGLEHE 

       370        380        390        400        410 
RCGEMIERIG LANFLEGIGI EPDPNMLSHP RQSSYIRMDG WDEAAEEWFA RQAEAGR 

« Hide

References

[1]"Towards the phylogeny of APS reductases and sirohaem sulfite reductases in sulfate-reducing and sulfur-oxidizing prokaryotes."
Hipp W.M., Pott A.S., Thum-Schmitz N., Faath I., Dahl C., Trueper H.G.
Microbiology 143:2891-2902(1997) [PubMed: 9308173] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 17899 / DSM 180 / D.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U84760 Genomic DNA. Translation: AAC35394.1.

3D structure databases

SMRO33998. Positions 7-408.
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12320.
BRENDA1.8.99.3. 2799.

Family and domain databases

InterProIPR011806. DsrA.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
[Graphical view]
PfamPF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
[Graphical view]
TIGRFAMsTIGR02064. dsrA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDSRA_CHRVI
AccessionPrimary (citable) accession number: O33998
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information