AC   MF_00063;
DC   Protein; auto
TR   HAMAP; MF_00063; -; 1; level=0
XX
Names: CysH
XX
ID   CYSH
case <FTGroup:1>
DE   RecName: Full=Adenosine 5'-phosphosulfate reductase;
DE            Short=APS reductase;
DE            EC=1.8.4.10;
DE   AltName: Full=5'-adenylylsulfate reductase;
DE   AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase;
else
DE   RecName: Full=Phosphoadenosine 5'-phosphosulfate reductase;
DE            Short=PAPS reductase;
DE            EC=1.8.4.8;
DE   AltName: Full=3'-phosphoadenylylsulfate reductase;
DE   AltName: Full=PAPS reductase, thioredoxin dependent;
DE   AltName: Full=PAPS sulfotransferase;
DE   AltName: Full=PAdoPS reductase;
end case
GN   Name=cysH;
XX
case <FTGroup:1>
CC   -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-
CC       phosphosulfate (APS) using thioredoxin as an electron donor.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + AMP + 2 H(+) + sulfite =
CC         [thioredoxin]-dithiol + adenosine 5'-phosphosulfate;
CC         Xref=Rhea:RHEA:21976, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:58243, ChEBI:CHEBI:456215;
CC         EC=1.8.4.10;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate.
else
CC   -!- FUNCTION: Catalyzes the formation of sulfite from phosphoadenosine 5'-
CC       phosphosulfate (PAPS) using thioredoxin as an electron donor.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2
CC         H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol;
CC         Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=1.8.4.8;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 3/3.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
XX
DR   Pfam; PF01507; PAPS_reduct; 1; trigger=no
DR   PIRSF; PIRSF000857; PAPS_reductase; 1; trigger=no
DR   NCBIfam; TIGR00434; cysH; 1; trigger=no
DR   NCBIfam; TIGR02055; APS_reductase; 0-1; trigger=no
DR   NCBIfam; TIGR02057; PAPS_reductase; 0-1; trigger=no
XX
KW   Cytoplasm
KW   Oxidoreductase
case <FTGroup:1>
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
end case
XX
GO   GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity
case <FTGroup:1>
GO   GO:0051539; F:4 iron, 4 sulfur cluster binding
end case
GO   GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
GO   GO:0005737; C:cytoplasm
XX
FT   From: CYSH_PSEAE (O05927)
FT   ACT_SITE        256
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT   Condition: C
FT   BINDING         139
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 1; Condition: C
FT   BINDING         140
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 1; Condition: C
FT   BINDING         228
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 1; Condition: C
FT   BINDING         231
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 1; Condition: C
XX
Size: 200-300;
Related: None;
Template: P17854; O05927; P9WIK3; P56891; P94498; A0R0W2;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACSU
Plasmid: 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.
XX
# Revision 1.35 2023/06/01
//