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P45575 (DSVB_DESVH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sulfite reductase, dissimilatory-type subunit beta

EC=1.8.99.3
Alternative name(s):
Desulfoviridin subunit beta
Hydrogensulfite reductase subunit beta
Gene names
Name:dsvB
Ordered Locus Names:DVU_0403
OrganismDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Reference proteome] [HAMAP]
Taxonomic identifier882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria.

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.

Subunit structure

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

Sequence similarities

Contains 1 4Fe-4S ferredoxin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 381380Sulfite reductase, dissimilatory-type subunit beta
PRO_0000080032

Regions

Domain249 – 276284Fe-4S ferredoxin-type

Sites

Metal binding2311Iron-sulfur (4Fe-4S) Potential
Metal binding2581Iron-sulfur (4Fe-4S) Potential
Metal binding2611Iron-sulfur (4Fe-4S) Potential
Metal binding2641Iron-sulfur (4Fe-4S) Potential

Secondary structure

.................................................................... 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45575 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 678A04F716050D63

FASTA38142,519
        10         20         30         40         50         60 
MAFISSGYNP EKPMANRITD IGPRKFDEFF PPVIAKNFGS WLYHEILEPG VLMHVAESGD 

        70         80         90        100        110        120 
KVYTVRVGAA RLMSITHIRE MCDIADKYCG GHLRFTTRNN VEFMVADEAS LKALKEDLAS 

       130        140        150        160        170        180 
RKFDGGSLKF PIGGTGAGVS NIVHTQGWVH CHTPATDASG PVKAIMDEVF EDFQSMRLPA 

       190        200        210        220        230        240 
PVRISLACCI NMCGAVHCSD IGVVGIHRKP PMIDHEWTDQ LCEIPLAVAS CPTAAVRPTK 

       250        260        270        280        290        300 
LEIGDKKVNT IAIKNERCMY CGNCYTMCPA LPISDGEGDG VVIMVGGKVS NRISMPKFSK 

       310        320        330        340        350        360 
VVVAYIPNEP PRWPSLTKTI KHIIEVYSAN AYKYERLGEW AERIGWERFF SLTGLEFSHH 

       370        380 
LIDDFRDPAY YTWRQSTQFK F 

« Hide

References

« Hide 'large scale' references
[1]"Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR."
Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G.
Appl. Environ. Microbiol. 61:290-296(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 2-16.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16723 Genomic DNA. Translation: AAA70108.1.
AE017285 Genomic DNA. Translation: AAS94886.1.
PIRS21238.
RefSeqYP_009627.1. NC_002937.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10B/E1-381[»]
ProteinModelPortalP45575.
SMRP45575. Positions 15-381.
ModBaseSearch...

Protein-protein interaction databases

STRING882.DVU0403.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS94886; AAS94886; DVU_0403.
GeneID2796153.
KEGGdvu:DVU0403.
PATRIC32060774. VBIDesVul119526_0380.

Phylogenomic databases

eggNOGCOG2221.
KOK11181.
OMAWLHCDIP.
ProtClustDBCLSK862601.

Enzyme and pathway databases

BioCycDVUL882:GJIL-423-MONOMER.
MetaCyc:MONOMER-12512.
BRENDA1.8.99.3. 1914.

Family and domain databases

InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR011808. DsrB.
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]
SUPFAMSSF55124. NiR_SiRalpha_1/3. 1 hit.
TIGRFAMsTIGR02066. dsrB. 1 hit.
PROSITEPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP45575.

Entry information

Entry nameDSVB_DESVH
AccessionPrimary (citable) accession number: P45575
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 91 of the entry and version 3 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