ID   MET16_YEAST             Reviewed;         261 AA.
AC   P18408; D6W4G8; Q06212;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   24-JAN-2024, entry version 193.
DE   RecName: Full=Phosphoadenosine phosphosulfate reductase;
DE            EC=1.8.4.8;
DE   AltName: Full=3'-phosphoadenylylsulfate reductase;
DE   AltName: Full=PAPS reductase, thioredoxin dependent;
DE   AltName: Full=PAdoPS reductase;
GN   Name=MET16; OrderedLocusNames=YPR167C; ORFNames=P9325.8;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2203779; DOI=10.1016/s0021-9258(18)55427-2;
RA   Thomas D., Barbey R., Surdin-Kerjan Y.;
RT   "Gene-enzyme relationship in the sulfate assimilation pathway of
RT   Saccharomyces cerevisiae. Study of the 3'-phosphoadenylylsulfate reductase
RT   structural gene.";
RL   J. Biol. Chem. 265:15518-15524(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: The NADP dependent reduction of PAPS into sulfite involves
CC       thioredoxin which probably plays the role of a thiol carrier.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2
CC         H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol;
CC         Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=1.8.4.8;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 3/3.
CC   -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; J05591; AAA34774.1; -; Genomic_DNA.
DR   EMBL; U25840; AAB68154.1; -; Genomic_DNA.
DR   EMBL; AY693236; AAT93255.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11584.1; -; Genomic_DNA.
DR   PIR; S59826; S59826.
DR   RefSeq; NP_015493.1; NM_001184264.1.
DR   PDB; 2OQ2; X-ray; 2.10 A; A/B/C/D=1-261.
DR   PDBsum; 2OQ2; -.
DR   AlphaFoldDB; P18408; -.
DR   SMR; P18408; -.
DR   BioGRID; 36340; 110.
DR   DIP; DIP-6611N; -.
DR   IntAct; P18408; 1.
DR   STRING; 4932.YPR167C; -.
DR   MaxQB; P18408; -.
DR   PaxDb; 4932-YPR167C; -.
DR   PeptideAtlas; P18408; -.
DR   EnsemblFungi; YPR167C_mRNA; YPR167C; YPR167C.
DR   GeneID; 856296; -.
DR   KEGG; sce:YPR167C; -.
DR   AGR; SGD:S000006371; -.
DR   SGD; S000006371; MET16.
DR   VEuPathDB; FungiDB:YPR167C; -.
DR   eggNOG; KOG0189; Eukaryota.
DR   HOGENOM; CLU_044089_0_1_1; -.
DR   InParanoid; P18408; -.
DR   OMA; PIARWTQ; -.
DR   OrthoDB; 1429290at2759; -.
DR   BioCyc; MetaCyc:YPR167C-MONOMER; -.
DR   BioCyc; YEAST:YPR167C-MONOMER; -.
DR   UniPathway; UPA00140; UER00206.
DR   BioGRID-ORCS; 856296; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P18408; -.
DR   PRO; PR:P18408; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P18408; Protein.
DR   GO; GO:0005737; C:cytoplasm; IC:SGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0098624; F:3'-phosphoadenylylselenate reductase activity; TAS:Reactome.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IDA:SGD.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IMP:CACAO.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IDA:SGD.
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; IPR011800; PAPS_reductase_CysH.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00434; cysH; 1.
DR   NCBIfam; TIGR02057; PAPS_reductase; 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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Cysteine biosynthesis;
KW   Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..261
FT                   /note="Phosphoadenosine phosphosulfate reductase"
FT                   /id="PRO_0000100662"
FT   CONFLICT        242..261
FT                   /note="KTECGIHEASRFAQFLKQDA -> RPSVEFMKPADSRNF (in Ref. 1;
FT                   AAA34774)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           14..24
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           30..40
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           52..64
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   STRAND          72..76
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           83..96
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           115..122
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           131..138
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           140..149
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   STRAND          153..156
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           165..169
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   TURN            186..189
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           192..202
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           208..212
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   TURN            232..236
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:2OQ2"
FT   HELIX           251..253
FT                   /evidence="ECO:0007829|PDB:2OQ2"
SQ   SEQUENCE   261 AA;  30380 MW;  202AF2C20829513C CRC64;
     MKTYHLNNDI IVTQEQLDHW NEQLIKLETP QEIIAWSIVT FPHLFQTTAF GLTGLVTIDM
     LSKLSEKYYM PELLFIDTLH HFPQTLTLKN EIEKKYYQPK NQTIHVYKPD GCESEADFAS
     KYGDFLWEKD DDKYDYLAKV EPAHRAYKEL HISAVFTGRR KSQGSARSQL SIIEIDELNG
     ILKINPLINW TFEQVKQYID ANNVPYNELL DLGYRSIGDY HSTQPVKEGE DERAGRWKGK
     AKTECGIHEA SRFAQFLKQD A
//