MET16_SCHPO
ID MET16_SCHPO Reviewed; 266 AA.
AC Q10270;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable 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; ORFNames=SPAC13G7.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16436428; DOI=10.1099/mic.0.28398-0;
RA Fujita Y., Ukena E., Iefuji H., Giga-Hama Y., Takegawa K.;
RT "Homocysteine accumulation causes a defect in purine biosynthesis: further
RT characterization of Schizosaccharomyces pombe methionine auxotrophs.";
RL Microbiology 152:397-404(2006).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: The NADP dependent reduction of PAPS into sulfite involves
CC thioredoxin which probably plays the role of a thiol carrier (By
CC similarity). Required for methionine synthesis. {ECO:0000250,
CC ECO:0000269|PubMed:16436428}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Leads to methionine auxotrophy.
CC {ECO:0000269|PubMed:16436428}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA93594.1; -; Genomic_DNA.
DR PIR; S67435; S67435.
DR RefSeq; NP_593708.1; NM_001019139.2.
DR AlphaFoldDB; Q10270; -.
DR SMR; Q10270; -.
DR BioGRID; 279282; 18.
DR MINT; Q10270; -.
DR STRING; 4896.SPAC13G7.06.1; -.
DR iPTMnet; Q10270; -.
DR MaxQB; Q10270; -.
DR PaxDb; Q10270; -.
DR PRIDE; Q10270; -.
DR EnsemblFungi; SPAC13G7.06.1; SPAC13G7.06.1:pep; SPAC13G7.06.
DR GeneID; 2542836; -.
DR KEGG; spo:SPAC13G7.06; -.
DR PomBase; SPAC13G7.06; met16.
DR VEuPathDB; FungiDB:SPAC13G7.06; -.
DR eggNOG; KOG0189; Eukaryota.
DR HOGENOM; CLU_044089_0_1_1; -.
DR InParanoid; Q10270; -.
DR OMA; PIARWTQ; -.
DR PhylomeDB; Q10270; -.
DR UniPathway; UPA00140; UER00206.
DR PRO; PR:Q10270; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; ISO:PomBase.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
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); ISO:PomBase.
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; IPR011800; PAPS_reductase_CysH.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF000857; PAPS_reductase; 1.
DR TIGRFAMs; TIGR00434; cysH; 1.
DR TIGRFAMs; TIGR02057; PAPS_reductase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Methionine biosynthesis; NADP; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..266
FT /note="Probable phosphoadenosine phosphosulfate reductase"
FT /id="PRO_0000100661"
FT REGION 219..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 30561 MW; 6243A03A03317170 CRC64;
MSSIDTPANK LQAKTLFHPE HLEYINKQLS ELSPQDILKW CRWTLPSLFQ TSALGLSGLV
IMDMLSKMDM NVPLIFINTL HHFPETLDLL EKVKTKYPNV PVHVYRCAEA ANEKEFAQKF
GEKLWETDES RYDFLVKVEP ASRAYSDLNV LAVFTGRRRS QGGERGSLPI VQLDGPVLKI
NPLANWSFTE VHNYIITNNV PYNELLNKGY RSVGDWHSTQ PVREGEDERA GRWRGREKTE
CGLHSHPQSK FAQYMAELKK KETADQ
