APT2_YEAST
ID APT2_YEAST Reviewed; 181 AA.
AC P36973; Q04090;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Adenine phosphoribosyltransferase 2;
DE Short=APRT 2;
DE EC=2.4.2.7;
GN Name=APT2; OrderedLocusNames=YDR441C; ORFNames=D9461.27;
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=7941749; DOI=10.1002/yea.320100510;
RA Yuryev A., Corden J.L.;
RT "A Saccharomyces cerevisiae gene encoding a potential adenine
RT phosphoribosyltransferase.";
RL Yeast 10:659-662(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 POSSIBLE LACK OF CATALYTIC ACTIVITY.
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 [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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis. May lack
CC catalytic activity.
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 -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; L14434; AAA62848.1; -; Genomic_DNA.
DR EMBL; U33007; AAB64883.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12278.1; -; Genomic_DNA.
DR PIR; S69721; S69721.
DR RefSeq; NP_010729.3; NM_001180749.3.
DR AlphaFoldDB; P36973; -.
DR SMR; P36973; -.
DR BioGRID; 32497; 115.
DR DIP; DIP-2056N; -.
DR IntAct; P36973; 4.
DR STRING; 4932.YDR441C; -.
DR iPTMnet; P36973; -.
DR MaxQB; P36973; -.
DR PaxDb; P36973; -.
DR PRIDE; P36973; -.
DR EnsemblFungi; YDR441C_mRNA; YDR441C; YDR441C.
DR GeneID; 852051; -.
DR KEGG; sce:YDR441C; -.
DR SGD; S000002849; APT2.
DR VEuPathDB; FungiDB:YDR441C; -.
DR eggNOG; KOG1712; Eukaryota.
DR GeneTree; ENSGT00940000176759; -.
DR HOGENOM; CLU_063339_3_2_1; -.
DR InParanoid; P36973; -.
DR OMA; QHARVEM; -.
DR BioCyc; YEAST:YDR441C-MON; -.
DR UniPathway; UPA00588; UER00646.
DR PRO; PR:P36973; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P36973; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0002055; F:adenine binding; IBA:GO_Central.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0006168; P:adenine salvage; IBA:GO_Central.
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 InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Glycosyltransferase; Purine salvage;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..181
FT /note="Adenine phosphoribosyltransferase 2"
FT /id="PRO_0000149518"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 57
FT /note="G -> A (in Ref. 1; AAA62848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 19986 MW; 58AB48E13BADF8B3 CRC64;
MSISESYAKE IKTAFRQFTD FPIEGEQFED FLPIIGNPTL FQKLVHTFKT HLEEKFGKEK
IDFIAGIEAR GLLFGPSLAL ALGVGFVPIR RVGKLPGECA SITFTKLDHE EIFEMQVEAI
PFDSNVVVVD DVLATGGTAY AAGDLIRQVG AHILEYDFVL VLDSLHGEEK LSAPIFSILH
S
