A0A4V5NK33 · A0A4V5NK33_9GAMM
- ProteinSoxAX cytochrome complex subunit A
- GenesoxA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids286 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the intermediary formation of conspicuous sulfur globules inside of the cells.
Catalytic activity
- L-cysteinyl-[SoxY protein] + thiosulfate + 2 Fe(III)-[cytochrome c] = S-sulfosulfanyl-L-cysteinyl-[SoxY protein] + 2 Fe(II)-[cytochrome c] + 2 H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 heme group per subunit.
Note: Binds 2 heme groups per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 101 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 132 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: C | ||||||
Binding site | 200 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 203 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 204 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 243 | substrate | ||||
Sequence: R | ||||||
Active site | 247 | Cysteine persulfide intermediate | ||||
Sequence: C | ||||||
Binding site | 247 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytochrome complex | |
Cellular Component | periplasmic space | |
Molecular Function | electron transfer activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor | |
Molecular Function | transferase activity | |
Biological Process | sulfur oxidation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSoxAX cytochrome complex subunit A
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Chromatiales > Thioalkalibacteraceae > Guyparkeria
Accessions
- Primary accessionA0A4V5NK33
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MKRLFSSMIAASVLATGGAMA | ||||||
Chain | PRO_5020526713 | 22-286 | SoxAX cytochrome complex subunit A | |||
Sequence: EPANPSDPEEFRQLMVEFYQERYPDVPFEEYNNGVYAIDEDARSQWEGMMVFPETDQYVAAGEELWNEYRLPNGKPLSSCLGEAKGLRAKYPYFNEKDGEVHSLGLDIINCQKNAGEEAEKVWDPKNNYKKLANVLAYLASESNGMTNNVQINSEGAKAAYNRGKEAWFRRTGRLDNSCADCHQYHGGKYVRAERLHMNLGNTTHFPLFRYSKGSMFTLHKRIYGCFRDTGTVPFAQYSPYYRDLEFFMSYNDNELELNGPGIRK |
Interaction
Subunit
Heterodimer of SoxA and SoxX.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 83-167 | Cytochrome c | ||||
Sequence: GEELWNEYRLPNGKPLSSCLGEAKGLRAKYPYFNEKDGEVHSLGLDIINCQKNAGEEAEKVWDPKNNYKKLANVLAYLASESNGM |
Sequence similarities
Belongs to the SoxA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length286
- Mass (Da)32,708
- Last updated2019-07-31 v1
- Checksum6D84B9B99A539FAA