ID K8Y140_9LEPT Unreviewed; 245 AA. AC K8Y140; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 14-DEC-2022, entry version 42. 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=LSS_08254 {ECO:0000313|EMBL:EKT87353.1}; OS Leptospira santarosai serovar Shermani str. LT 821. OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=758847 {ECO:0000313|EMBL:EKT87353.1, ECO:0000313|Proteomes:UP000035800}; RN [1] {ECO:0000313|EMBL:EKT87353.1, ECO:0000313|Proteomes:UP000035800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT 821 {ECO:0000313|EMBL:EKT87353.1}; RX PubMed=23041083; DOI=10.1016/j.gene.2012.09.074; RA Chou L.F., Chen Y.T., Lu C.W., Ko Y.C., Tang C.Y., Pan M.J., Tian Y.C., RA Chiu C.H., Hung C.C., Yang C.W.; RT "Sequence of Leptospira santarosai serovar Shermani genome and prediction RT of virulence-associated genes."; RL Gene 511:364-370(2012). RN [2] {ECO:0000313|Proteomes:UP000035800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT821 {ECO:0000313|Proteomes:UP000035800}; RA Chou L.-F., Chen T.-W., Ko Y.-C., Pan M.-J., Tian Y.-C., Chiu C.-H., RA Tang P., Hung C.-C., Yang C.-W.; RT "Potential impact on kidney infection: a whole-genome analysis of RT Leptospira santarosai serovar Shermani."; RL Emerg. Microbes Infect. 3:e82-e82(2014). 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|HAMAP-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; CP006694; EKT87353.1; -; Genomic_DNA. DR RefSeq; WP_004459854.1; NZ_CP006694.1. DR AlphaFoldDB; K8Y140; -. DR STRING; 758847.LSS_08254; -. DR EnsemblBacteria; EKT87353; EKT87353; LSS_08254. DR GeneID; 29738970; -. DR KEGG; lst:LSS_08254; -. DR PATRIC; fig|758847.3.peg.1734; -. DR OrthoDB; 674332at2; -. DR Proteomes; UP000035800; Chromosome I. 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: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; -; 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 Pfam; PF01507; PAPS_reduct; 1. DR PIRSF; PIRSF000857; PAPS_reductase; 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}. FT DOMAIN 31..204 FT /note="PAPS_reduct" FT /evidence="ECO:0000259|Pfam:PF01507" FT ACT_SITE 225 FT /note="Nucleophile; cysteine thiosulfonate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 115 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 116 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 198 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 201 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" SQ SEQUENCE 245 AA; 28084 MW; 45BB381F7CD51997 CRC64; MLPQELEQKL ALLSLEDSLE WISNEYGETA AFSTSLGLED QVITHVIYTR NLKIRIFTLD TGRLFNETYD LHKLTNASYG RKIETYFPDT ASVQNLINTK GPDSFYDSVE NRKECCYIRK VEPLNRALVG TKLWITGIRS EQSDSRNSLT KVELDSSRNI LKYHPLLDWS LERTQDFIDT YRIPTNVLHK KGFPSIGCAP CTRAVQPGED IRAGRWWWEA SNQECGLHVV DGKLVRQKSG PKRAI //