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Database: UniProt
Entry: A0A0A7KG85_9DEIO
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ID   A0A0A7KG85_9DEIO        Unreviewed;       240 AA.
AC   A0A0A7KG85;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE            Short=APS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE            EC=1.8.4.10 {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=5'-adenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
GN   Name=cysH {ECO:0000256|HAMAP-Rule:MF_00063};
GN   ORFNames=QR90_02495 {ECO:0000313|EMBL:AIZ44219.1};
OS   Deinococcus radiopugnans.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ44219.1, ECO:0000313|Proteomes:UP000030634};
RN   [1] {ECO:0000313|Proteomes:UP000030634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA   Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT   "Hymenobacter sp. DG25B genome submission.";
RL   Submitted (NOV-2014) 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:0000256|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:0000256|HAMAP-Rule:MF_00063};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00063};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00063};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate. {ECO:0000256|ARBA:ARBA00024327, ECO:0000256|HAMAP-
CC       Rule:MF_00063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000256|ARBA:ARBA00009732, ECO:0000256|HAMAP-Rule:MF_00063}.
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DR   EMBL; CP010028; AIZ44219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A7KG85; -.
DR   STRING; 1182571.QR90_02495; -.
DR   KEGG; dsw:QR90_02495; -.
DR   HOGENOM; CLU_044089_2_0_0; -.
DR   Proteomes; UP000030634; Chromosome.
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:RHEA.
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: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; HUPs; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00434; cysH; 1.
DR   PANTHER; PTHR46509; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR   PANTHER; PTHR46509:SF1; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF000857; PAPS_reductase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00063}; Reference proteome {ECO:0000313|Proteomes:UP000030634}.
FT   DOMAIN          43..211
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        231
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT   BINDING         122
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT   BINDING         123
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT   BINDING         205
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT   BINDING         208
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   240 AA;  26032 MW;  98649FC89B4B58ED CRC64;
     MTAGVGKLRP ELPPPSIPSP PQARELKTLD LILWAITAHP DVLMPSAFNL NGVVLIDLAV
     RAGYRGQVVF VDTGYHFAET LQTRDRLAAR YAELEFVTLN AGASPEDGRT PPELYAADPD
     ACCAARKVAP LQEYLRHKNP SALLNARSRD QAATRAEIPS VEEGGARIKI NPLAEWTRQQ
     LEAYAAAHDL PVNPLYADGF LSVGCWPCTR AVRPGEDARA GRWAGQGKTE CGLWAGEGRL
//
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