ID   APT_CRIGR               Reviewed;         180 AA.
AC   P47952;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Adenine phosphoribosyltransferase {ECO:0000250|UniProtKB:P07741};
DE            Short=APRT;
DE            EC=2.4.2.7 {ECO:0000250|UniProtKB:P07741};
GN   Name=APRT {ECO:0000250|UniProtKB:P07741};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Ovary;
RX   PubMed=8440233; DOI=10.1002/j.1460-2075.1993.tb05671.x;
RA   Sage E., Drobetsky E.A., Moustacchi E.;
RT   "8-methoxypsoralen induced mutations are highly targeted at crosslinkable
RT   sites of photoaddition on the non-transcribed strand of a mammalian
RT   chromosomal gene.";
RL   EMBO J. 12:397-402(1993).
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|UniProtKB:P07741}.
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:0000250|UniProtKB:P07741};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1. {ECO:0000250|UniProtKB:P07741}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; X58958; CAA41729.1; -; Genomic_DNA.
DR   EMBL; X58959; CAA41729.1; JOINED; Genomic_DNA.
DR   EMBL; X58960; CAA41729.1; JOINED; Genomic_DNA.
DR   EMBL; X58961; CAA41729.1; JOINED; Genomic_DNA.
DR   EMBL; X58962; CAA41729.1; JOINED; Genomic_DNA.
DR   RefSeq; XP_003495138.1; XM_003495090.2.
DR   RefSeq; XP_007622098.1; XM_007623908.1.
DR   AlphaFoldDB; P47952; -.
DR   SMR; P47952; -.
DR   STRING; 10029.XP_007622098.1; -.
DR   Ensembl; ENSCGRT00001010906; ENSCGRP00001006920; ENSCGRG00001009398.
DR   GeneID; 100765665; -.
DR   KEGG; cge:100765665; -.
DR   CTD; 353; -.
DR   eggNOG; KOG1712; Eukaryota.
DR   GeneTree; ENSGT00390000017259; -.
DR   OMA; KPGIVFR; -.
DR   OrthoDB; 1291050at2759; -.
DR   UniPathway; UPA00588; UER00646.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0002055; F:adenine binding; IEA:Ensembl.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016208; F:AMP binding; IEA:Ensembl.
DR   GO; GO:0006168; P:adenine salvage; IEA:InterPro.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032263; P:GMP salvage; IEA:Ensembl.
DR   GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR   GO; GO:0032264; P:IMP salvage; IEA:Ensembl.
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   Acetylation; Cytoplasm; Glycosyltransferase; Phosphoprotein;
KW   Purine salvage; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
FT   CHAIN           2..180
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000149502"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
FT   MOD_RES         60
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
FT   MOD_RES         114
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
FT   MOD_RES         135
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
SQ   SEQUENCE   180 AA;  19404 MW;  6916B95B2332BDD4 CRC64;
     MAESELQLVA QRIRSFPDFP IPGVLFRDIS PLLKDPASFR ASIRLLASHL KSTHGGKIDY
     IAGLDSRGFL FGPSLAQELG LGCVLIRKRG KLPGPTVSAS YALEYGKAEL EIQKDALEPG
     QKVVVVDDLL ATGGTMCAAC ELLGQLQAEV VECVSLVELT SLKGREKLGS VPFFSLLQYE