ID   APT_MUSSI               Reviewed;         180 AA.
AC   P47957;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
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   Mus spicilegus (Steppe mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9023989; DOI=10.1038/hdy.1997.3;
RA   Fieldhouse D., Yazdani F., Golding G.B.;
RT   "Substitution rate variation in closely related rodent species.";
RL   Heredity 78:21-31(1997).
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; U28720; AAA68958.1; -; Genomic_DNA.
DR   AlphaFoldDB; P47957; -.
DR   SMR; P47957; -.
DR   Ensembl; ENSMSIT00000022649; ENSMSIP00000017914; ENSMSIG00000015264.
DR   GeneTree; ENSGT00390000017259; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000694415; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0002055; F:adenine binding; IEA:Ensembl.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; ISS:UniProtKB.
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; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P36972"
FT   CHAIN           2..180
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000149508"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36972"
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;  19724 MW;  A6AE4DBE0B456E42 CRC64;
     MSEPELKLVA RRIRSFPDFP IPGVLFRDIS PLLKDPDSFR ASIRLLASHL KSTHSGKIDY
     IAGLDSRGFL FGPSLAQELG VGCVLIRKQG KLPGPTVSAS YSLEYGKAEL EIQKDALEPG
     QRVVIVDDLL ATGGTMFAAC DLLHQLRAEV VECVSLVELT SLKGRERLGP IPFFSLLQYD