ID   APT1_YEAST              Reviewed;         187 AA.
AC   P49435; D6VZF2; Q6Q5A3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 3.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Adenine phosphoribosyltransferase 1 {ECO:0000303|PubMed:9357956};
DE            Short=APRT 1 {ECO:0000303|PubMed:9357956};
DE            EC=2.4.2.7 {ECO:0000269|PubMed:9864350};
GN   Name=APT1 {ECO:0000303|PubMed:9357956}; OrderedLocusNames=YML022W;
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].
RC   STRAIN=DS1;
RX   PubMed=7642142; DOI=10.1016/0378-1119(95)00239-3;
RA   Alfonzo J.D., Sahota A., Deeley M.C., Ranjekar P., Taylor M.W.;
RT   "Cloning and characterization of the adenine phosphoribosyltransferase-
RT   encoding gene (APT1) from Saccharomyces cerevisiae.";
RL   Gene 161:81-85(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Taylor M.W., Alfonzo J.D.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [4]
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   [5]
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   [6]
RP   COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC 24903;
RX   PubMed=9357956; DOI=10.1016/s0167-4838(97)00068-x;
RA   Alfonzo J.D., Sahota A., Taylor M.W.;
RT   "Purification and characterization of adenine phosphoribosyltransferase
RT   from Saccharomyces cerevisiae.";
RL   Biochim. Biophys. Acta 1341:173-182(1997).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=9864350; DOI=10.1128/jb.181.1.347-352.1999;
RA   Alfonzo J.D., Crother T.R., Guetsova M.L., Daignan-Fornier B., Taylor M.W.;
RT   "APT1, but not APT2, codes for a functional adenine
RT   phosphoribosyltransferase in Saccharomyces cerevisiae.";
RL   J. Bacteriol. 181:347-352(1999).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [9]
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).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11] {ECO:0007744|PDB:1G2P, ECO:0007744|PDB:1G2Q}
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 3-187 OF APOENZYME AND IN COMPLEX
RP   WITH SUBSTRATE ANALOG, HOMODIMERIZATION, AND MUTAGENESIS OF ARG-69; ARG-89;
RP   LYS-90; LYS-93; TYR-103; GLU-106; TYR-107 AND GLY-108.
RX   PubMed=11535055; DOI=10.1021/bi010465h;
RA   Shi W., Tanaka K.S.E., Crother T.R., Taylor M.W., Almo S.C., Schramm V.L.;
RT   "Structural analysis of adenine phosphoribosyltransferase from
RT   Saccharomyces cerevisiae.";
RL   Biochemistry 40:10800-10809(2001).
RN   [12] {ECO:0007744|PDB:5VJN, ECO:0007744|PDB:5VJP}
RP   X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 3-187.
RX   PubMed=29178779; DOI=10.1021/acschembio.7b00601;
RA   Harris L.D., Harijan R.K., Ducati R.G., Evans G.B., Hirsch B.M.,
RA   Schramm V.L.;
RT   "Synthesis of bis-Phosphate Iminoaltritol Enantiomers and Structural
RT   Characterization with Adenine Phosphoribosyltransferase.";
RL   ACS Chem. Biol. 13:152-160(2018).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC       AMP, that is energically less costly than de novo synthesis.
CC       {ECO:0000269|PubMed:9357956, ECO:0000269|PubMed:9864350}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7;
CC         Evidence={ECO:0000269|PubMed:9864350};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9357956};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11535055,
CC       ECO:0000269|PubMed:9357956, ECO:0000269|PubMed:9864350}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 11200 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; U16781; AAA89075.1; -; Genomic_DNA.
DR   EMBL; Z46659; CAA86633.1; -; Genomic_DNA.
DR   EMBL; AY558232; AAS56558.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09876.1; -; Genomic_DNA.
DR   PIR; S49755; S49755.
DR   RefSeq; NP_013690.1; NM_001182380.1.
DR   PDB; 1G2P; X-ray; 1.75 A; A=1-187.
DR   PDB; 1G2Q; X-ray; 1.50 A; A/B=1-187.
DR   PDB; 5VJN; X-ray; 1.78 A; A/B=3-187.
DR   PDB; 5VJP; X-ray; 1.98 A; A/B=3-187.
DR   PDBsum; 1G2P; -.
DR   PDBsum; 1G2Q; -.
DR   PDBsum; 5VJN; -.
DR   PDBsum; 5VJP; -.
DR   AlphaFoldDB; P49435; -.
DR   SMR; P49435; -.
DR   BioGRID; 35147; 68.
DR   DIP; DIP-2057N; -.
DR   IntAct; P49435; 2.
DR   STRING; 4932.YML022W; -.
DR   iPTMnet; P49435; -.
DR   MaxQB; P49435; -.
DR   PaxDb; 4932-YML022W; -.
DR   PeptideAtlas; P49435; -.
DR   TopDownProteomics; P49435; -.
DR   EnsemblFungi; YML022W_mRNA; YML022W; YML022W.
DR   GeneID; 854986; -.
DR   KEGG; sce:YML022W; -.
DR   AGR; SGD:S000004484; -.
DR   SGD; S000004484; APT1.
DR   VEuPathDB; FungiDB:YML022W; -.
DR   eggNOG; KOG1712; Eukaryota.
DR   GeneTree; ENSGT00940000176759; -.
DR   HOGENOM; CLU_063339_1_0_1; -.
DR   InParanoid; P49435; -.
DR   OMA; ITHFVYH; -.
DR   OrthoDB; 231465at2759; -.
DR   BioCyc; MetaCyc:YML022W-MONOMER; -.
DR   BioCyc; YEAST:YML022W-MONOMER; -.
DR   BRENDA; 2.4.2.7; 984.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-74217; Purine salvage.
DR   UniPathway; UPA00588; UER00646.
DR   BioGRID-ORCS; 854986; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; P49435; -.
DR   PRO; PR:P49435; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P49435; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0002055; F:adenine binding; IBA:GO_Central.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IDA:SGD.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006168; P:adenine salvage; IMP:SGD.
DR   GO; GO:0044209; P:AMP salvage; IBA:GO_Central.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR   InterPro; IPR005764; Ade_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   NCBIfam; TIGR01090; apt; 1.
DR   PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR32315:SF3; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding;
KW   Nucleus; Phosphoprotein; Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..187
FT                   /note="Adenine phosphoribosyltransferase 1"
FT                   /id="PRO_0000149517"
FT   BINDING         133..137
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         69
FT                   /note="R->A: 4-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         89
FT                   /note="R->A: 2-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         90
FT                   /note="K->A: 30-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         93
FT                   /note="K->A: Small increase in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         103
FT                   /note="Y->F: 4-fold increase in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         106
FT                   /note="E->L: 1 million-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         106
FT                   /note="E->Q: 2-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         107
FT                   /note="Y->D: 2/3-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         107
FT                   /note="Y->F: Small decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         108
FT                   /note="G->A: Small decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   MUTAGEN         108
FT                   /note="G->H: 2/3-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11535055"
FT   CONFLICT        37
FT                   /note="P -> F (in Ref. 1; AAA89075)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2..13
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   HELIX           31..35
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   HELIX           37..54
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   STRAND          96..104
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   STRAND          109..115
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   STRAND          124..134
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   HELIX           136..147
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   STRAND          151..160
FT                   /evidence="ECO:0007829|PDB:1G2Q"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:1G2P"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:1G2P"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:1G2Q"
SQ   SEQUENCE   187 AA;  20587 MW;  68061D4BAA42EDEF CRC64;
     MSIASYAQEL KLALHQYPNF PSEGILFEDF LPIFRNPGLF QKLIDAFKLH LEEAFPEVKI
     DYIVGLESRG FLFGPTLALA LGVGFVPVRK AGKLPGECFK ATYEKEYGSD LFEIQKNAIP
     AGSNVIIVDD IIATGGSAAA AGELVEQLEA NLLEYNFVME LDFLKGRSKL NAPVFTLLNA
     QKEALKK
//