HAMAP rule MF_00063
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00063 |
| Accession | MF_00063 |
| Dates | 28-FEB-2005 (Created)
03-SEP-2024 (Last updated, Version 25) |
| Name | CysH |
| Scope(s) |
Bacteria |
| Template(s) | P17854; O05927; P9WIK3; P56891; P94498; A0R0W2; [ Recover all ] |
| Triggered by |
HAMAP; MF_00063 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | CYSH |
| case <FTGroup:1> | |
| Protein name | RecName: Full=Adenosine 5'-phosphosulfate reductase; Short=APS reductase; EC=1.8.4.10; AltName: Full=5'-adenylylsulfate reductase; AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase; |
| else | |
| Protein name | RecName: Full=Phosphoadenosine 5'-phosphosulfate reductase; Short=PAPS reductase; EC=1.8.4.8; AltName: Full=3'-phosphoadenylylsulfate reductase; AltName: Full=PAPS reductase, thioredoxin dependent; AltName: Full=PAPS sulfotransferase; AltName: Full=PAdoPS reductase; |
| end case | |
| Gene name | Name=cysH; |
Comments
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| case <FTGroup:1> | |
| FUNCTION | Catalyzes the formation of sulfite from adenosine 5'- phosphosulfate (APS) using thioredoxin as an electron donor. |
| CATALYTIC ACTIVITY | Reaction=[thioredoxin]-disulfide + sulfite + AMP + 2 H(+) = adenosine 5'-phosphosulfate + [thioredoxin]-dithiol; Xref=Rhea:RHEA:21976, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:58243, ChEBI:CHEBI:456215; EC=1.8.4.10; |
| COFACTOR | Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit.; |
| PATHWAY | Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate. |
| else | |
| FUNCTION | Catalyzes the formation of sulfite from phosphoadenosine 5'- phosphosulfate (PAPS) using thioredoxin as an electron donor. |
| CATALYTIC ACTIVITY | Reaction=[thioredoxin]-disulfide + sulfite + adenosine 3',5'- bisphosphate + 2 H(+) = [thioredoxin]-dithiol + 3'-phosphoadenylyl sulfate; Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA- COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=1.8.4.8; |
| PATHWAY | Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3. |
| end case | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the PAPS reductase family. CysH subfamily. |
Keywords
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| Cytoplasm | |
| Oxidoreductase | |
| case <FTGroup:1> | |
| Iron | |
| Iron-sulfur | |
| Metal-binding | |
| end case | |
Gene Ontology
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| GO:0004604; Molecular function:phosphoadenylyl-sulfate reductase (thioredoxin) activity | |
| case <FTGroup:1> | |
| GO:0051539; Molecular function:4 iron, 4 sulfur cluster binding | |
| end case | |
| GO:0019379; Biological process:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) | |
| GO:0070814; Biological process:hydrogen sulfide biosynthetic process | |
| GO:0005737; Cellular component:cytoplasm | |
Cross-references
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| Pfam | PF01507; PAPS_reduct; 1; |
| PIRSF | PIRSF000857; PAPS_reductase; 1; |
| NCBIfam | TIGR00434; cysH; 1; |
| NCBIfam | TIGR02055; APS_reductase; 0-1; |
| NCBIfam | TIGR02057; PAPS_reductase; 0-1; |
Features
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| From: CYSH_PSEAE (O05927) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 256 | 256 | /note="Nucleophile; cysteine thiosulfonate intermediate" | C | ||||||||
| BINDING | 139 | 139 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | 1 | |||||||
| BINDING | 140 | 140 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | 1 | |||||||
| BINDING | 228 | 228 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | 1 | |||||||
| BINDING | 231 | 231 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | 1 | |||||||
Additional information
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| Size range | 200-300 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | The presence of an iron-sulfur cluster determines the APS specificity of the sulfate-reducing enzymes and thus separates the APS- and PAPS-dependent assimilatory sulfate reduction pathways. See PubMed:11940598. |