ID   APT_CANAL               Reviewed;         188 AA.
AC   Q5ALX8; A0A1D8PGC1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Adenine phosphoribosyltransferase;
DE            Short=APRT;
DE            EC=2.4.2.7;
GN   Name=APT1; OrderedLocusNames=CAALFM_C201430WA;
GN   ORFNames=CaO19.1448, CaO19.9023;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017624; AOW27189.1; -; Genomic_DNA.
DR   RefSeq; XP_722498.1; XM_717405.1.
DR   AlphaFoldDB; Q5ALX8; -.
DR   SMR; Q5ALX8; -.
DR   STRING; 237561.Q5ALX8; -.
DR   PRIDE; Q5ALX8; -.
DR   GeneID; 3635842; -.
DR   KEGG; cal:CAALFM_C201430WA; -.
DR   CGD; CAL0000192887; APT1.
DR   VEuPathDB; FungiDB:C2_01430W_A; -.
DR   eggNOG; KOG1712; Eukaryota.
DR   HOGENOM; CLU_063339_1_0_1; -.
DR   InParanoid; Q5ALX8; -.
DR   OMA; KPGIVFR; -.
DR   OrthoDB; 1291050at2759; -.
DR   UniPathway; UPA00588; UER00646.
DR   PRO; PR:Q5ALX8; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
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..188
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000227899"
FT   BINDING         134..138
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   188 AA;  20877 MW;  8CA335A0D1F675F6 CRC64;
     MSDRVLEINA LAKELKANLK QFPNFPKEGI LFEDFLPIFT KPDLFNKLVK AFKLHVGEQK
     IDYVIGLESR GFLFGPTLAL ALNAGFVPVR KPGKLPGPTF KVEFQKEYGS DEFEIQQDVI
     PKGAKVLIVD DILATGGSAF GAGELAKKTG AEIVEYLFVM ELDFLKGRDK LDAPVYTLFG
     GQEEKFTE