A0AAJ4E205 · A0AAJ4E205_9GAMM
- ProteinDissimilatory sulfite reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids678 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | 141 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 144 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 145 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 157 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 208 | substrate | ||||
Sequence: K | ||||||
Binding site | 285 | substrate | ||||
Sequence: Y | ||||||
Binding site | 302 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 305 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 306 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 339 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 342 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 343 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 348 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 360 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 363 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 364 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 366 | substrate | ||||
Sequence: R | ||||||
Binding site | 398 | Cu+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 410 | Fe (UniProtKB | ChEBI) of heme c 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 417 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 420 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 421 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 424 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 444 | heme c 6 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 447 | heme c 6 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 448 | Fe (UniProtKB | ChEBI) of heme c 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 461 | Fe (UniProtKB | ChEBI) of heme c 8 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 466 | heme c 7 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 469 | heme c 7 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 470 | Fe (UniProtKB | ChEBI) of heme c 7 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 477 | Cu+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 498 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 544 | heme c 8 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 560 | heme c 8 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 561 | Fe (UniProtKB | ChEBI) of heme c 8 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 645 | Fe (UniProtKB | ChEBI) of heme c 7 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
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 > Gammaproteobacteria > Alteromonadales > Shewanellaceae > Shewanella
Accessions
- Primary accessionA0AAJ4E205
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MKNWKLKAVASVLFCFGAVSNVSA | ||||||
Chain | PRO_5042303748 | 25-678 | Dissimilatory sulfite reductase | |||
Sequence: AGGKYNSIPEMGESAKNSIANYTGTEETKGVKSLQDYIVQEDELFDFLFNNHPMFKYHEDGNLIGEYHISDRGEEYLDTGNSPKYSARVGRPSAVQYRLGAKSTLDFPNNFVGPEKCAECHAVQYEKWQRSRHANVVRFPSEITDKEVPNGDLNAKLYGSEAAMLPDGIRANDVYAIIGTPRTKYGFLDSYLVRGTYHIRDGLLSEGTGKMVAGANQFSRGWAEWLTPEMAKKINKVIPEFPTTIEDFGDSGSHQWGMSSYGAKYEKELLFQPASSYCEMCHTFKFDFQSKEEYFAALGDSKKLQEHTISKGISCEECHGAGGHLDGGTGGMQSNCERCHQRFNFVDELADTEKGQEKMEYAFGVKMKSACPSCGTEGSQMFASAHYEKGMRCTTCHDPHEVTDGDFLSGFTKPLLKKQCVDCHEVQATIAENTDTHSKQTCQSCHMPAMGSCENFTATQFPDMAGFDAVRKSHMWKIDIHPERKTLNPPTGQPRDAAVKGWTVAKNEEDHNYLDLMWSCARTAVSDHDNVENKGCHSPFQSELETGLHYEDQLEIYGEVMKWQNPVKQVFADVEQALERIDQLLEVTKLSIEDKTQVLMLAEKAQETVDFIRKDGSWGVHGFRYSQKRLDAALTYVTQAQKILDGTGYSAKSH |
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length678
- Mass (Da)75,906
- Last updated2024-07-24 v1
- Checksum8327B2BEB5244DF3