APT1_YEAST
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 03-AUG-2022, entry version 186.
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; 64.
DR DIP; DIP-2057N; -.
DR IntAct; P49435; 2.
DR STRING; 4932.YML022W; -.
DR iPTMnet; P49435; -.
DR MaxQB; P49435; -.
DR PaxDb; P49435; -.
DR PRIDE; P49435; -.
DR TopDownProteomics; P49435; -.
DR EnsemblFungi; YML022W_mRNA; YML022W; YML022W.
DR GeneID; 854986; -.
DR KEGG; sce:YML022W; -.
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; KPGIVFR; -.
DR BioCyc; MetaCyc:YML022W-MON; -.
DR BioCyc; YEAST:YML022W-MON; -.
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 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 Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01090; apt; 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
