A0A271LQJ7 · A0A271LQJ7_9HYPH
- ProteinSoxAX cytochrome complex subunit A
- GenesoxA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids259 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
C-type diheme 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 liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO2 fixation.
Catalytic activity
- 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H+ + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
Cofactor
Note: Binds 2 heme groups per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 74 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 77 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 78 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 112 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: C | ||||||
Binding site | 175 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 178 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 179 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 216 | substrate | ||||
Sequence: R | ||||||
Active site | 220 | Cysteine persulfide intermediate | ||||
Sequence: C | ||||||
Binding site | 220 | 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 > Alphaproteobacteria > Hyphomicrobiales > Phyllobacteriaceae > Mesorhizobium
Accessions
- Primary accessionA0A271LQJ7
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MHALWRLAAVSAATICGIVSA | ||||||
Chain | PRO_5013170986 | 22-259 | SoxAX cytochrome complex subunit A | |||
Sequence: AGIEDGEKRSGFDFMTPETQALQADDMSNPGMLWVLQGEQLWQQAEGRADVACAGCHDNASRTMRGVAARYPAFEAARGRPIDLAGRINSCRAERQQAEALAPESDALLALTAYVAHQSRGMPITPATDPRLAPFRDNGRRLFQSRIGQLDLSCASCHDDNWGKRLGGSVIPQAHPTGYPLYRLEWQTVGSLQRRLRNCMVGVRAEPFAFGAPELVDLELHLTERARGLLVETPAVRP |
Interaction
Subunit
Heterodimer of SoxA and SoxX.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 58-145 | Cytochrome c | ||||
Sequence: QGEQLWQQAEGRADVACAGCHDNASRTMRGVAARYPAFEAARGRPIDLAGRINSCRAERQQAEALAPESDALLALTAYVAHQSRGMPI | ||||||
Domain | 160-250 | Cytochrome c | ||||
Sequence: GRRLFQSRIGQLDLSCASCHDDNWGKRLGGSVIPQAHPTGYPLYRLEWQTVGSLQRRLRNCMVGVRAEPFAFGAPELVDLELHLTERARGL |
Sequence similarities
Belongs to the SoxA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length259
- Mass (Da)28,258
- Last updated2017-12-20 v1
- ChecksumAD894396E38E121E