T2G899 · APRB_MEGG1
- ProteinAdenylylsulfate reductase subunit beta
- GeneaprB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids167 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Iron-sulfur cluster subunit of the adenylylsulfate reductase which catalyzes reversibly the reduction of adenosine 5'-phosphosulfate (APS) to sulfite and AMP during dissimilatory sulfate reduction. The iron-sulfur cluster 2 is thought to accept electrons from a still unknown electron donor and transfer electrons to the iron-sulfur cluster 1 of this protein and then onto the FAD of AprA.
Cofactor
Note: Binds 2 [4Fe-4S] clusters.
pH Dependence
Optimum pH is 7.4 for the adenylylsulfate reductase.
Redox Potential
E0 is about 0 mV for 4Fe-4S cluster 1 and is estimated to be lower than -400 mV for a fully reduced 4Fe-4S cluster 2.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 13 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 21 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 25 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 47 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 48 | Important for the electron transfer from the iron-sulfur cluster 1 to the FAD of AprA | ||||
Sequence: W | ||||||
Binding site | 50 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 53 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 57 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 152 | Important for interaction with AprA at the substrate channel entrance | ||||
Sequence: E | ||||||
Site | 159 | Important for interaction with AprA at the substrate channel entrance | ||||
Sequence: D | ||||||
Site | 163 | Important for interaction with AprA at the substrate channel entrance | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein heterodimerization activity | |
Biological Process | dissimilatory sulfate reduction | |
Biological Process | protein heterotetramerization |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylylsulfate reductase subunit beta
- Short namesAdoPSO(4) reductase subunit B
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Megalodesulfovibrio
Accessions
- Primary accessionT2G899
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000434042 | 1-167 | Adenylylsulfate reductase subunit beta | |||
Sequence: MPTFVDPSKCDGCKGGEKTACMYICPNDLMILDPEEMKAFNQEPEACWECYSCIKICPQGAITARPYADFAPMGGTCIPLRGSEDIMWTIKFRNGSVKRFKFPIRTTPEGSIKPFEGKPEAGDLENELLFTETALTVPQVALGQKAQIADAETSQCWFDLPCEGGNR |
Interaction
Subunit
Heterodimer composed of AprA and AprB (PubMed:19820092, PubMed:2158885).
The heterodimers can dimerize to form heterotetramers (PubMed:2158885).
The heterodimers can dimerize to form heterotetramers (PubMed:2158885).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | T2G899 | aprA T2G6Z9 | 3 | EBI-6409220, EBI-6409227 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-35 | 4Fe-4S ferredoxin-type 1 | ||||
Sequence: MPTFVDPSKCDGCKGGEKTACMYICPNDLMILDPE | ||||||
Domain | 38-67 | 4Fe-4S ferredoxin-type 2 | ||||
Sequence: KAFNQEPEACWECYSCIKICPQGAITARPY |
Domain
Consists of three sections from the N- to the C-terminus: [4Fe-4S] cluster-binding domain, beta-sheet and C-terminal tail. The beta-sheet and the C-terminal tail interact with AprA to stabilize the AprA/AprB heterodimer.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length167
- Mass (Da)18,445
- Last updated2013-11-13 v1
- Checksum4CE816D5DD932C50
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 4 | in Ref. 3; no nucleotide entry | ||||
Sequence: F → Y |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KF113859 EMBL· GenBank· DDBJ | AGS82786.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP006585 EMBL· GenBank· DDBJ | AGW12371.1 EMBL· GenBank· DDBJ | Genomic DNA |