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P45574 (DSVA_DESVH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. 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 alpha
EC=1.8.99.3
Alternative name(s):
Desulfoviridin subunit alpha
Hydrogensulfite reductase subunit alpha
Gene names
Name:dsvA
Ordered Locus Names:DVU_0402
OrganismDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Reference proteome] [HAMAP]
Taxonomic identifier882 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio ›

Protein attributes

Sequence length437 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 – 437436Sulfite reductase, dissimilatory-type subunit alpha
PRO_0000080030

Regions

Domain294 – 322294Fe-4S ferredoxin-type

Sites

Metal binding1771Iron (heme axial ligand) Potential
Metal binding1831Iron (heme axial ligand) Potential
Metal binding2211Iron (heme axial ligand) Potential
Metal binding2251Iron (heme axial ligand) Potential
Metal binding2841Iron-sulfur (4Fe-4S) Potential
Metal binding3031Iron-sulfur (4Fe-4S) Potential
Metal binding3061Iron-sulfur (4Fe-4S) Potential
Metal binding3091Iron-sulfur (4Fe-4S) Potential

Experimental info

Sequence conflict221S → V AA sequence Ref.3
Sequence conflict261Q → K AA sequence Ref.3

Secondary structure

1 ................................................................................. 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45574 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4AED624D4B13A21F

FASTA43749,091
        10         20         30         40         50         60 
MAKHATPKLD QLESGPWPSF VSDIKQEAAY RAANPKGLDY QVPVDCPEDL LGVLELSYDE 

        70         80         90        100        110        120 
GETHWKHGGI VGVFGYGGGV IGRYCDQPEK FPGVAHFHTV RVAQPSGKYY SADYLRQLCD 

       130        140        150        160        170        180 
IWDLRGSGLT NMHGSTGDIV LLGTQTPQLE EIFFELTHNL NTDLGGSGSN LRTPESCLGK 

       190        200        210        220        230        240 
SRCEFACYDS QAACYELTME YQDELHRPAF PYKFKFKFDA CPNGCVASIA RSDFSVIGTW 

       250        260        270        280        290        300 
KDDIKIDAEA VKAYVAGEFK PNAGAHSGRD WGKFDIEAEV VNRCPSKCMK WDGSKLSIDN 

       310        320        330        340        350        360 
KECVRCMHCI NTMPRALHIG DERGASILCG AKAPILDGAQ MGSLLVPFVA AEEPFDEIKE 

       370        380        390        400        410        420 
VVEKIWDWWM EEGKNRERLG ETMKRLSFQK LLEVTEIAPV PQHVKEPRTN PYIFFKEEEV 

       430 
PGGWDRDITE YRKRHLR

« 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 2-26.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U16723 Genomic DNA. Translation: AAA70107.1.
AE017285 Genomic DNA. Translation: AAS94885.1.
PIRS21197.
RefSeqYP_009626.1. NC_002937.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10A/D1-437[»]
ProteinModelPortalP45574.
SMRP45574. Positions 5-436.
ModBaseSearch...

Protein-protein interaction databases

STRING882.DVU0402.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS94885; AAS94885; DVU_0402.
GeneID2796152.
KEGGdvu:DVU0402.
PATRIC32060772. VBIDesVul119526_0379.

Phylogenomic databases

eggNOGCOG2221.
KOK11180.
OMADIMLQGI.
ProtClustDBCLSK862600.

Enzyme and pathway databases

BioCycDVUL882:GJIL-422-MONOMER.
MetaCyc:MONOMER-12511.
BRENDA1.8.99.3. 1914.

Family and domain databases

InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR011806. 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.
PROSITEPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP45574.

Entry information

Entry nameDSVA_DESVH
AccessionPrimary (citable) accession number: P45574
Secondary accession number(s): Q46581
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 87 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

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