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UniProtKB/Swiss-Prot entry O33998

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DSRA_CHRVI
Primary accession number O33998
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 41)
Name and origin of the protein
Protein name Sulfite reductase, dissimilatory-type subunit alpha
Synonyms EC 1.8.99.3
Hydrogensulfite reductase subunit alpha
Gene name
Name: dsrA
From
Chromatium vinosum (Allochromatium vinosum) [TaxID: 1049] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae; Allochromatium.
Protein existence 4: Predicted;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 17899 / DSM 180 / D;
PubMed=9308173 [NCBI, ExPASy, EBI, Israel, Japan]
Hipp W.M., Pott A.S., Thum-Schmitz N., Faath I., Dahl C., Trueper H.G.;
"Towards the phylogeny of APS reductases and sirohaem sulfite reductases in sulfate-reducing and sulfur-oxidizing prokaryotes.";
Microbiology 143:2891-2902(1997).
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.
  • COFACTOR: Binds 2 sirohemes per subunit.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U84760; AAC35394.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase O33998.
Enzyme and pathway databases
BioCyc MetaCyc:MON-12320; -.
Family and domain databases
InterPro IPR011806; DsrA.
IPR006067; Nir_Sir_4Fe4S.
Graphical view of domain structure.
Pfam PF01077; NIR_SIR; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02064; dsrA; 1.
BLOCKS O33998.
Other
ProtoNet O33998.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Heme; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   417  417     Sulfite reductase, dissimilatory-type subunit alpha. PRO_0000080026
METAL   170   170        Iron (heme axial ligand) (Potential). 
METAL   176   176        Iron (heme axial ligand) (Potential). 
METAL   214   214        Iron (heme axial ligand) (Potential). 
METAL   218   218        Iron (heme axial ligand) (Potential). 
METAL   264   264        Iron-sulfur (4Fe-4S) (Potential). 
METAL   284   284        Iron-sulfur (4Fe-4S) (Potential). 
METAL   287   287        Iron-sulfur (4Fe-4S) (Potential). 
METAL   290   290        Iron-sulfur (4Fe-4S) (Potential). 
Sequence information
Length: 417 AA [This is the length of the unprocessed precursor] Molecular weight: 46791 Da [This is the MW of the unprocessed precursor] CRC64: 474680A622F37B40 [This is a checksum on the sequence] 
        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
O33998 in FASTA format

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