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Database: UniProt
Entry: A5DJY1_PICGU
LinkDB: A5DJY1_PICGU
Original site: A5DJY1_PICGU 
ID   A5DJY1_PICGU            Unreviewed;       348 AA.
AC   A5DJY1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE            EC=2.4.2.28 {ECO:0000256|HAMAP-Rule:MF_03155};
DE   AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE            Short=MTA phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE            Short=MTAP {ECO:0000256|HAMAP-Rule:MF_03155};
DE            Short=MTAPase {ECO:0000256|HAMAP-Rule:MF_03155};
GN   Name=MEU1 {ECO:0000256|HAMAP-Rule:MF_03155};
GN   ORFNames=PGUG_03582 {ECO:0000313|EMBL:EDK39484.1};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK39484.1, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK39484.1, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-
CC       thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate.
CC       Involved in the breakdown of MTA, a major by-product of polyamine
CC       biosynthesis. Responsible for the first step in the methionine salvage
CC       pathway after MTA has been generated from S-adenosylmethionine. Has
CC       broad substrate specificity with 6-aminopurine nucleosides as preferred
CC       substrates. {ECO:0000256|HAMAP-Rule:MF_03155}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC         thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03155};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC       thioadenosine (phosphorylase route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_03155}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_03155}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03155}.
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DR   EMBL; CH408158; EDK39484.1; -; Genomic_DNA.
DR   RefSeq; XP_001484201.1; XM_001484151.1.
DR   AlphaFoldDB; A5DJY1; -.
DR   STRING; 294746.A5DJY1; -.
DR   GeneID; 5125909; -.
DR   KEGG; pgu:PGUG_03582; -.
DR   VEuPathDB; FungiDB:PGUG_03582; -.
DR   eggNOG; KOG3985; Eukaryota.
DR   HOGENOM; CLU_054456_0_1_1; -.
DR   InParanoid; A5DJY1; -.
DR   OMA; ADPFCPE; -.
DR   OrthoDB; 168017at2759; -.
DR   UniPathway; UPA00904; UER00873.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   HAMAP; MF_01963; MTAP; 1.
DR   InterPro; IPR010044; MTAP.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR   NCBIfam; TIGR01694; MTAP; 1.
DR   PANTHER; PTHR42679; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR42679:SF2; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS01240; PNP_MTAP_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_03155};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03155};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_03155}; Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03155}.
FT   DOMAIN          38..297
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   BINDING         44
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT   BINDING         87..88
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT   BINDING         120..121
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT   BINDING         238
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT   BINDING         261..263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT   SITE            219
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT   SITE            274
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
SQ   SEQUENCE   348 AA;  38058 MW;  7F2E746438E20263 CRC64;
     MVQRRLTNNI TKLITMAAHR EHIELGSLPH HFDKPVPLAV IGGTGLYDLP NLKPVARLTI
     STPWGFPSAP ITISETDSGY AVAFLARHGQ HHDLLPTDVP SRANMAALKS LGVEAIIAFS
     AVGSLQQEIK PRDFVLPTQI IDRTKGIRPS TFFERGFVAH AMFGEPFDLT LSKIISENVP
     SSGFLEGFET DARPTFHTKH NTNNGEDLTL ICMEGPQFST RAESKLYRSW GGSVINMSAL
     PEAKLAREAE IAYQMICMST DYDSWNESED PVTVETVVGN LKANSANACK LAAHLIEVVS
     KDLALGTSGV GKGLKGSMKY SVSTSPHGVK KELLEKMHFL FPGYWPVQ
//
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