ID   CYSH_BACAA              Reviewed;         226 AA.
AC   C3P516;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE            Short=APS reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE            EC=1.8.4.10 {ECO:0000255|HAMAP-Rule:MF_00063};
DE   AltName: Full=5'-adenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE   AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
GN   Name=cysH {ECO:0000255|HAMAP-Rule:MF_00063}; OrderedLocusNames=BAA_1510;
OS   Bacillus anthracis (strain A0248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=592021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A0248;
RA   Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA   Brettin T.;
RT   "Genome sequence of Bacillus anthracis A0248.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-
CC       phosphosulfate (APS) using thioredoxin as an electron donor.
CC       {ECO:0000255|HAMAP-Rule:MF_00063}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00063};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00063};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00063};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate. {ECO:0000255|HAMAP-Rule:MF_00063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00063}.
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DR   EMBL; CP001598; ACQ50421.1; -; Genomic_DNA.
DR   RefSeq; WP_000958999.1; NC_012659.1.
DR   AlphaFoldDB; C3P516; -.
DR   SMR; C3P516; -.
DR   GeneID; 45021420; -.
DR   KEGG; bai:BAA_1510; -.
DR   HOGENOM; CLU_044089_2_1_9; -.
DR   OMA; PIARWTQ; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043866; F:adenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:InterPro.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:UniProtKB-UniRule.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR011798; APS_reductase.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF000857; PAPS_reductase; 1.
DR   TIGRFAMs; TIGR02055; APS_reductase; 1.
DR   TIGRFAMs; TIGR00434; cysH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT   CHAIN           1..226
FT                   /note="Adenosine 5'-phosphosulfate reductase"
FT                   /id="PRO_1000117921"
FT   ACT_SITE        221
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT   BINDING         112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT   BINDING         113
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT   BINDING         195
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT   BINDING         198
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   226 AA;  26393 MW;  3FF2A81C8BCA282A CRC64;
     MLTYETWEEN ETKGALSVLS WAYKEYKSEI VYACSFGVEG MVLLDLINQV NPSAKVVFLD
     TNVHFQETYE LIQKVRERFP SLNIIEKQPK LTLDEQDKLH GDKLWESNPN LCCKIRKILP
     LEESLANEKA WISGLRREQS ETRKHTKFIN QDHRFQSIKV CPLIHWTWKE VWRYVYKHSL
     PYNSLHDIGY PSIGCEKCTL PVGEGGDSRD GRWAGKVKTE CGLHYQ