P45574 · DSVA_NITV2

Function

function

Part of the complex that catalyzes the reduction of sulfite to sulfide. The alpha and beta subunits may have arisen by gene duplication. They both bind 2 iron-sulfur clusters, but the alpha subunit seems to be catalytically inactive, due to substitutions along the putative substrate access channel, and because it binds sirohydrochlorin (the dematallated form of siroheme) instead of siroheme.

Features

Showing features for binding site.

143750100150200250300350400
TypeIDPosition(s)Description
Binding site177[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site183[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site221[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site225[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site284[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site303[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site306[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site309[4Fe-4S] cluster 2 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functiondissimilatory sulfite reductase activity
Molecular Functionheme binding
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sulfite reductase, dissimilatory-type subunit alpha
  • Alternative names
    • Desulfoviridin subunit alpha
    • Dissimilatory sulfite reductase subunit alpha
      (dSiR alpha
      )
    • Hydrogensulfite reductase subunit alpha

Gene names

    • Name
      dsvA
    • Synonyms
      dsrA
    • Ordered locus names
      DVU_0402

Organism names

Accessions

  • Primary accession
    P45574
  • Secondary accessions
    • Q46581

Proteomes

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00000800302-437Sulfite reductase, dissimilatory-type subunit alpha

Proteomic databases

Interaction

Subunit

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

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P45574dsvB P455755EBI-9016991, EBI-9016987
BINARY P45574dsvC P455733EBI-9016991, EBI-9017020

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain294-3224Fe-4S ferredoxin-type

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    437
  • Mass (Da)
    49,091
  • Last updated
    2007-01-23 v3
  • Checksum
    4AED624D4B13A21F
MAKHATPKLDQLESGPWPSFVSDIKQEAAYRAANPKGLDYQVPVDCPEDLLGVLELSYDEGETHWKHGGIVGVFGYGGGVIGRYCDQPEKFPGVAHFHTVRVAQPSGKYYSADYLRQLCDIWDLRGSGLTNMHGSTGDIVLLGTQTPQLEEIFFELTHNLNTDLGGSGSNLRTPESCLGKSRCEFACYDSQAACYELTMEYQDELHRPAFPYKFKFKFDACPNGCVASIARSDFSVIGTWKDDIKIDAEAVKAYVAGEFKPNAGAHSGRDWGKFDIEAEVVNRCPSKCMKWDGSKLSIDNKECVRCMHCINTMPRALHIGDERGASILCGAKAPILDGAQMGSLLVPFVAAEEPFDEIKEVVEKIWDWWMEEGKNRERLGETMKRLSFQKLLEVTEIAPVPQHVKEPRTNPYIFFKEEEVPGGWDRDITEYRKRHLR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict22in Ref. 3; AA sequence
Sequence conflict26in Ref. 3; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U16723
EMBL· GenBank· DDBJ
AAA70107.1
EMBL· GenBank· DDBJ
Genomic DNA
AE017285
EMBL· GenBank· DDBJ
AAS94885.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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