ID   APT_ASHGO               Reviewed;         187 AA.
AC   Q756E2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Adenine phosphoribosyltransferase;
DE            Short=APRT;
DE            EC=2.4.2.7;
GN   Name=APT1; OrderedLocusNames=AER325W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC       AMP, that is energically less costly than de novo synthesis.
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS53005.1; -; Genomic_DNA.
DR   RefSeq; NP_985181.1; NM_210535.1.
DR   AlphaFoldDB; Q756E2; -.
DR   SMR; Q756E2; -.
DR   STRING; 33169.AAS53005; -.
DR   EnsemblFungi; AAS53005; AAS53005; AGOS_AER325W.
DR   GeneID; 4621394; -.
DR   KEGG; ago:AGOS_AER325W; -.
DR   eggNOG; KOG1712; Eukaryota.
DR   HOGENOM; CLU_063339_1_0_1; -.
DR   InParanoid; Q756E2; -.
DR   OMA; KPGIVFR; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding; Nucleus;
KW   Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..187
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000227898"
FT   BINDING         133..137
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   187 AA;  20434 MW;  ECCB97F1DF3DE7F1 CRC64;
     MSINEYAKEL KAALAQYPNF PKEGVLFEDF LPIFRSPQLF QKLIDAFKMH LAEAFPETKI
     DYLVGLESRG FLFGPSLALA IGAGFVPVRK AGKLPGQVVK TTYVKEYEED VFEMQVDSIP
     VGATVVVVDD ILATGGSAGA AGDLIKQLGA TILEFIFVME LDFLKGREKL QAPVFTLLQG
     QEEALGN