ID B2HIT5_MYCMM Unreviewed; 244 AA. AC B2HIT5; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 04-NOV-2026, entry version 93. DE RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000256|ARBA:ARBA00029514, ECO:0000256|HAMAP-Rule:MF_00063}; DE Short=APS reductase {ECO:0000256|HAMAP-Rule:MF_00063}; DE EC=1.8.4.10 {ECO:0000256|ARBA:ARBA00024386, ECO:0000256|HAMAP-Rule:MF_00063}; DE AltName: Full=5'-adenylylsulfate reductase {ECO:0000256|ARBA:ARBA00032041, ECO:0000256|HAMAP-Rule:MF_00063}; DE AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000256|ARBA:ARBA00030894, ECO:0000256|HAMAP-Rule:MF_00063}; GN Name=cysH_1 {ECO:0000313|EMBL:ACC41842.1}; GN Synonyms=cysH {ECO:0000256|HAMAP-Rule:MF_00063}; GN OrderedLocusNames=MMAR_3417 {ECO:0000313|EMBL:ACC41842.1}; OS Mycobacterium marinum (strain ATCC BAA-535 / M). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group. OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41842.1, ECO:0000313|Proteomes:UP000001190}; RN [1] {ECO:0000313|EMBL:ACC41842.1, ECO:0000313|Proteomes:UP000001190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190}; RX PubMed=18403782; DOI=10.1101/gr.075069.107; RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A., RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.; RT "Insights from the complete genome sequence of Mycobacterium marinum on the RT evolution of Mycobacterium tuberculosis."; RL Genome Res. 18:729-741(2008). CC -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'- CC phosphosulfate (APS) using thioredoxin as an electron donor. CC {ECO:0000256|ARBA:ARBA00024298, 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; CP000854; ACC41842.1; -; Genomic_DNA. DR RefSeq; WP_012395059.1; NC_010612.1. DR AlphaFoldDB; B2HIT5; -. DR STRING; 216594.MMAR_3417; -. DR KEGG; mmi:MMAR_3417; -. DR eggNOG; COG0175; Bacteria. DR HOGENOM; CLU_044089_2_0_11; -. DR OMA; AAWTRKQ; -. DR OrthoDB; 9794018at2; -. DR Proteomes; UP000001190; 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 CDD; cd23945; PAPS_reductase; 1. DR FunFam; 3.40.50.620:FF:000136; Probable 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00063}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00063}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00063}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00063}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00063}; Reference proteome {ECO:0000313|Proteomes:UP000001190}. FT DOMAIN 49..218 FT /note="Phosphoadenosine phosphosulphate reductase" FT /evidence="ECO:0000259|Pfam:PF01507" FT REGION 221..244 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 235..244 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 239 FT /note="Nucleophile; cysteine thiosulfonate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 130 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 131 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 213 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" FT BINDING 216 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063" SQ SEQUENCE 244 AA; 26764 MW; B6545399A3F3C35C CRC64; MSDQPNETQL RELAARGAAE MEGASATDLL RWADEHFGGI NGPRGWATCN YVVASNMQDA VLIDLASKVR PGVPVIFLDT GYHFAETIGT RDAIEAVYDI RVLNISPEHT VAEQDKLLGK DLFARDPNEC CRLRKVVPLT NALRGYAAWI TGLRRVESPT RANAPVISFD EAFKLVKINP LVSWTDQDVQ DYIQSNNVLV NPLVDEGYPS IGCAPCTAKP AVGEDPRSGR WRGRTKTECG LHAS //