ID A4F9S2_SACEN Unreviewed; 241 AA. AC A4F9S2; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 02-SEP-2026, entry version 112. 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 ECO:0000313|EMBL:CAM00797.1}; GN OrderedLocusNames=SACE_1475 {ECO:0000313|EMBL:CAM00797.1}; OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / OS NBRC 13426 / NCIMB 8594 / NRRL 2338). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Saccharopolyspora. OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM00797.1, ECO:0000313|Proteomes:UP000006728}; RN [1] {ECO:0000313|EMBL:CAM00797.1, ECO:0000313|Proteomes:UP000006728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}; RX PubMed=17369815; DOI=10.1038/nbt1297; RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., RA Haydock S.F., Leadlay P.F.; RT "Complete genome sequence of the erythromycin-producing bacterium RT Saccharopolyspora erythraea NRRL23338."; RL Nat. Biotechnol. 25:447-453(2007). 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 + 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: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}. 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; AM420293; CAM00797.1; -; Genomic_DNA. DR RefSeq; WP_009948062.1; NC_009142.1. DR AlphaFoldDB; A4F9S2; -. DR STRING; 405948.SACE_1475; -. DR GeneID; 306458333; -. DR KEGG; sen:SACE_1475; -. DR eggNOG; COG0175; Bacteria. DR HOGENOM; CLU_044089_2_0_11; -. DR OrthoDB; 9794018at2; -. DR Proteomes; UP000006728; 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:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:UniProtKB-UniRule. DR CDD; cd23945; 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_dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. 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 {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:UP000006728}. FT ACT_SITE 237 FT /note="Nucleophile; cysteine thiosulfonate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 128 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 129 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 211 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 214 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" SQ SEQUENCE 241 AA; 25986 MW; AF59354AD6204723 CRC64; MTAETTTNVG VRRSDEELRA LAEEAAPRLA EATAEEALRW AADTFGENLI VASNMQDAVL VDLAAKASPG VDVLFLETGY HFAETIGTRD AVAQVYDVSI VNAVPEQSVA EQDAGEGPNL FERDPNRCCF LRKVVPLRNT LARYEAWVTG VRRVEAPTRA NTPVVTWDDR NGLVKINPLA AWSDEEMDAY IAEHGVLVNP LVPAGYPSIG CRPCTAKPAP GADPRSGRWA GNSKTECGLH G //