A0A6I3S9G5 · A0A6I3S9G5_9BURK
- ProteinDissimilatory sulfite reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids681 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Respiratory sulfite reductase that catalyzes the reduction of sulfite to sulfide in a single step, consuming six electrons in the process.
Catalytic activity
- [protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide = [protein]-dithiol + 2 AH2 + H+ + sulfite
RHEA-COMP:10593 + 2 CHEBI:13193 + 3 CHEBI:15377 + CHEBI:29919 = RHEA-COMP:10594 CHEBI:29950 Position: C1CHEBI:29950 Position: C2+ 2 CHEBI:17499 + CHEBI:15378 + CHEBI:17359
Cofactor
Protein has several cofactor binding sites:
Note: Exposure to oxygen reduces copper binding and leads to the formation of a disulfide bond between the two Cys residues that bind the copper ion.
Note: Binds 8 heme c groups covalently per monomer.
Pathway
Sulfur metabolism; sulfite reduction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 145 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 148 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 149 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 161 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 209 | substrate | ||||
Sequence: K | ||||||
Binding site | 286 | substrate | ||||
Sequence: Y | ||||||
Binding site | 303 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 306 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 307 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 340 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 343 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 344 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 349 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 361 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 364 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 365 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 367 | substrate | ||||
Sequence: R | ||||||
Binding site | 399 | Cu+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 411 | Fe (UniProtKB | ChEBI) of heme c 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 418 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 421 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 422 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 425 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 445 | heme c 6 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 448 | heme c 6 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 449 | Fe (UniProtKB | ChEBI) of heme c 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 462 | Fe (UniProtKB | ChEBI) of heme c 8 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 467 | heme c 7 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 470 | heme c 7 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 471 | Fe (UniProtKB | ChEBI) of heme c 7 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 478 | Cu+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 499 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 545 | heme c 8 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 561 | heme c 8 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 562 | Fe (UniProtKB | ChEBI) of heme c 8 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 646 | Fe (UniProtKB | ChEBI) of heme c 7 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | copper ion binding | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | sulfite reductase activity | |
Biological Process | anaerobic respiration | |
Biological Process | hydrogen sulfide biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDissimilatory sulfite reductase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Sutterellaceae > Parasutterella
Accessions
- Primary accessionA0A6I3S9G5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MLRETRKTAIGLGLAAAMATSCVYA | ||||||
Chain | PRO_5031680577 | 26-681 | Dissimilatory sulfite reductase | |||
Sequence: ADGQPLPTPKVNEITQKVWANPDLTEPTKGIRTLQDYIVQEKELWDFLFQNHPIFATYGKDGRVIGTPVISTRGSEYLGEGNAQKYSAHQDGNRPMASQYRLGQRSILDFPNKFVGPEKCGECHAIQYEQWKRSRHAKTVRFPGEHPEVDNDLKKKLYGSEASILPDGITADVIYATIGTPRTKYGYIDGWLVRGSYHVRDGLLKDGTGKVVAGGNQFSRGWAEWLTPEKAKEIQKLIPDFPTELSQFGPSASHQWGMTSYGSTYEGKLLFQAASSYCEVCHAFKFDFKDKKEFFAALGNPKELQKHTISRGIACEECHGEGGHLVGNTNNMSTNCDRCHQRLNFIEDEVDRPDAKGKLEKAFNAKTKSSCPSCGTEGAQLFMSKHYEKGMRCVTCHDPHEVTSNDWTSGVTRPAIRKNCQDCHTTQAQMVANADTHSKVDCIACHMPFTMSCENFTAIQRPDMAGFDAVRRSHLFKIMVDPDKKMMNPGPGQSRASNSKGWRISRDEEGHGYVDLMWSCARTSIADFTVVEGKGCHSPFQSELDQGLIYQDQKEIYGEVMKWQNPIKEGHQKNVEALTRINKLLEVTKLTPEQRTEAMLLIDKAGEIIKQVQDDGSWGVHAFNYTKQRVETAQAYLTKAQSIIDQGGYKAVKATK |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 144-166 | Cytochrome c-552/4 | ||||
Sequence: KCGECHAIQYEQWKRSRHAKTVR | ||||||
Domain | 415-453 | Doubled CXXCH motif | ||||
Sequence: GMRCVTCHDPHEVTSNDWTSGVTRPAIRKNCQDCHTTQA |
Sequence similarities
Belongs to the multiheme cytochrome c family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length681
- Mass (Da)76,173
- Last updated2020-08-12 v1
- ChecksumC569DB90891543CD