P45574 · DSVA_NITV2
- ProteinSulfite reductase, dissimilatory-type subunit alpha
- GenedsvA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids437 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 177 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 183 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 221 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 225 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 284 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 303 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 306 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 309 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | dissimilatory sulfite reductase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSulfite reductase, dissimilatory-type subunit alpha
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Nitratidesulfovibrio
Accessions
- Primary accessionP45574
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000080030 | 2-437 | Sulfite reductase, dissimilatory-type subunit alpha | |||
Sequence: AKHATPKLDQLESGPWPSFVSDIKQEAAYRAANPKGLDYQVPVDCPEDLLGVLELSYDEGETHWKHGGIVGVFGYGGGVIGRYCDQPEKFPGVAHFHTVRVAQPSGKYYSADYLRQLCDIWDLRGSGLTNMHGSTGDIVLLGTQTPQLEEIFFELTHNLNTDLGGSGSNLRTPESCLGKSRCEFACYDSQAACYELTMEYQDELHRPAFPYKFKFKFDACPNGCVASIARSDFSVIGTWKDDIKIDAEAVKAYVAGEFKPNAGAHSGRDWGKFDIEAEVVNRCPSKCMKWDGSKLSIDNKECVRCMHCINTMPRALHIGDERGASILCGAKAPILDGAQMGSLLVPFVAAEEPFDEIKEVVEKIWDWWMEEGKNRERLGETMKRLSFQKLLEVTEIAPVPQHVKEPRTNPYIFFKEEEVPGGWDRDITEYRKRHLR |
Proteomic databases
Interaction
Subunit
Heterohexamer of two alpha, two beta and two gamma subunits.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P45574 | dsvB P45575 | 5 | EBI-9016991, EBI-9016987 | |
BINARY | P45574 | dsvC P45573 | 3 | EBI-9016991, EBI-9017020 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length437
- Mass (Da)49,091
- Last updated2007-01-23 v3
- Checksum4AED624D4B13A21F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 22 | in Ref. 3; AA sequence | ||||
Sequence: S → V | ||||||
Sequence conflict | 26 | in Ref. 3; AA sequence | ||||
Sequence: Q → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U16723 EMBL· GenBank· DDBJ | AAA70107.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE017285 EMBL· GenBank· DDBJ | AAS94885.1 EMBL· GenBank· DDBJ | Genomic DNA |