ID CYSH_BACP2 Reviewed; 233 AA. AC A8FD22; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, entry version 96. 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}; GN OrderedLocusNames=BPUM_1456; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). 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 + sulfite + AMP + 2 H(+) = adenosine CC 5'-phosphosulfate + [thioredoxin]-dithiol; Xref=Rhea:RHEA:21976, CC Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:58243, ChEBI:CHEBI:456215; EC=1.8.4.10; CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000813; ABV62139.1; -; Genomic_DNA. DR RefSeq; WP_012009902.1; NC_009848.4. DR AlphaFoldDB; A8FD22; -. DR SMR; A8FD22; -. DR STRING; 315750.BPUM_1456; -. DR PaxDb; 315750-BPUM_1456; -. DR GeneID; 5620719; -. DR KEGG; bpu:BPUM_1456; -. DR eggNOG; COG0175; Bacteria. DR HOGENOM; CLU_044089_2_1_9; -. DR OrthoDB; 9772604at2; -. DR Proteomes; UP000001355; 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:UniProtKB-EC. DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019344; P:L-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; cd23945; PAPS_reductase; 1. DR FunFam; 3.40.50.620:FF:000095; Phosphoadenosine phosphosulfate reductase; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00063; CysH; 1. DR InterPro; IPR011798; APS_reductase. DR InterPro; IPR004511; PAPS/APS_Rdtase. DR InterPro; IPR002500; PAPS_reduct_dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR02055; APS_reductase; 1. DR NCBIfam; TIGR00434; cysH; 1. DR NCBIfam; NF002537; PRK02090.1; 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; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1..233 FT /note="Adenosine 5'-phosphosulfate reductase" FT /id="PRO_1000057429" FT ACT_SITE 229 FT /note="Nucleophile; cysteine thiosulfonate intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063" FT BINDING 120 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063" FT BINDING 121 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063" FT BINDING 203 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063" FT BINDING 206 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063" SQ SEQUENCE 233 AA; 26719 MW; 5932B0591BF6F218 CRC64; MLTYENWQEP SITFQEDDLY KGALSVLKWA YGHYGDQLVY ACSFGIEGIV LIDLIAKVKK DARIVFLDTG LHFKETYDTI DAVKERYPGL DIVLKTPELT VEEQNDQHGD QLWKTDPQSC CHMRKVIPLQ EALSGYPAWL SGLRREQSPK RAGTNFLNKD EKFKSVKVCP LIHWTWKDIW RYASREELTY NPLHDQGYPS IGCAPCTQPA FTAQDLRSGR WSGTAKTECG LHE //