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
//
