HAMAP rule MF_02023
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_02023 |
| Accession | MF_02023 |
| Dates | 01-APR-2015 (Created)
03-SEP-2024 (Last updated, Version 12) |
| Name | Sulfite_red |
| Scope(s) |
Bacteria Pseudomonadota |
| Template(s) | Q7MSJ8; Q8EJI6; [ Recover all ] |
| Triggered by |
HAMAP; MF_02023 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | MCCA |
| Protein name | RecName: Full=Dissimilatory sulfite reductase; EC=1.8.99.-; Flags: Precursor; |
Comments
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| FUNCTION | Respiratory sulfite reductase that catalyzes the reduction of sulfite to sulfide in a single step, consuming six electrons in the process. |
| CATALYTIC ACTIVITY | Reaction=[protein]-disulfide + hydrogen sulfide + 2 A + 3 H2O = [protein]-dithiol + sulfite + 2 AH2 + H(+); Xref=Rhea:RHEA:51676, Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:17499, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058; |
| COFACTOR | Name=Cu(+); Xref=ChEBI:CHEBI:49552; 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.; |
| COFACTOR | Name=heme c; Xref=ChEBI:CHEBI:61717; Note=Binds 8 heme c groups covalently per monomer.; |
| PATHWAY | Sulfur metabolism; sulfite reduction. |
| SUBCELLULAR LOCATION | Periplasm. |
| SIMILARITY | Belongs to the multiheme cytochrome c family. |
Keywords
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| Copper |
| Electron transport |
| Heme |
| Iron |
| Metal-binding |
| Oxidoreductase |
| Periplasm |
| Signal |
| Sulfate respiration |
| Transport |
Gene Ontology
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| GO:0005507; Molecular function:copper ion binding |
| GO:0020037; Molecular function:heme binding |
| GO:0005506; Molecular function:iron ion binding |
| GO:0016002; Molecular function:sulfite reductase activity |
| GO:0070814; Biological process:hydrogen sulfide biosynthetic process |
| GO:0042597; Cellular component:periplasmic space |
Cross-references
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| PROSITE | PS51008; MULTIHEME_CYTC; 2; |
| Pfam | PF14522; Cytochrome_C7; 1; |
| Pfam | PF09699; Paired_CXXCH_1; 1; |
| General | Signal; -; 1; |
Features
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| From: MCCA_WOLSU (Q7MSJ8) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 159 | 159 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="1" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 171 | 171 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="4" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 318 | 318 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="2" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 355 | 355 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="3" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 360 | 360 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="1" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 376 | 376 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="4" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 411 | 411 | /ligand="Cu(+)" /ligand_id="ChEBI:CHEBI:49552" |
C | ||||||||
| BINDING | 423 | 423 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="6" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 434 | 434 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="5" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 437 | 437 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="3" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 478 | 478 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="6" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 491 | 491 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="8" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 500 | 500 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="7" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 507 | 507 | /ligand="Cu(+)" /ligand_id="ChEBI:CHEBI:49552" |
C | ||||||||
| BINDING | 528 | 528 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="5" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 591 | 591 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="8" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 675 | 675 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="7" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 155 | 155 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="1" /note="covalent" |
C | ||||||||
| BINDING | 158 | 158 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="1" /note="covalent" |
C | ||||||||
| BINDING | 220 | 220 | /ligand="substrate" | K | ||||||||
| BINDING | 297 | 297 | /ligand="substrate" | Y | ||||||||
| BINDING | 314 | 314 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="2" /note="covalent" |
C | ||||||||
| BINDING | 317 | 317 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="2" /note="covalent" |
C | ||||||||
| BINDING | 351 | 351 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="3" /note="covalent" |
C | ||||||||
| BINDING | 354 | 354 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="3" /note="covalent" |
C | ||||||||
| BINDING | 372 | 372 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="4" /note="covalent" |
C | ||||||||
| BINDING | 375 | 375 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="4" /note="covalent" |
C | ||||||||
| BINDING | 378 | 378 | /ligand="substrate" | R | ||||||||
| BINDING | 430 | 430 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="5" /note="covalent" |
C | ||||||||
| BINDING | 433 | 433 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="5" /note="covalent" |
C | ||||||||
| BINDING | 474 | 474 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="6" /note="covalent" |
C | ||||||||
| BINDING | 477 | 477 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="6" /note="covalent" |
C | ||||||||
| BINDING | 496 | 496 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="7" /note="covalent" |
C | ||||||||
| BINDING | 499 | 499 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="7" /note="covalent" |
C | ||||||||
| BINDING | 574 | 574 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="8" /note="covalent" |
C | ||||||||
| BINDING | 590 | 590 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_label="8" /note="covalent" |
C | ||||||||
Additional information
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| Size range | 640-710 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |