HAMAP rule MF_00063
General rule information
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Accession | MF_00063 |
Dates | 1-JUN-2001 (Created)
14-MAY-2024 (Last updated, Version 36) |
Name | CysH |
Scope(s) |
Bacteria |
Template(s) | P17854 (CYSH_ECOLI); O05927 (CYSH_PSEAE); P9WIK3 (CYSH_MYCTU); P56891 (CYSH_RHIME); P94498 (CYSH1_BACSU); A0R0W2 (CYSH_MYCS2); [ 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 + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate; 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 + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol; 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. |