ID   APT_BOVIN               Reviewed;         180 AA.
AC   Q56JW4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymphoid epithelium;
RA   Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT   "Analysis of sequences obtained from constructed full-length bovine cDNA
RT   libraries.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AY911367; AAW82131.1; -; mRNA.
DR   EMBL; BC102283; AAI02284.1; -; mRNA.
DR   RefSeq; NP_001020505.1; NM_001025334.2.
DR   AlphaFoldDB; Q56JW4; -.
DR   SMR; Q56JW4; -.
DR   STRING; 9913.ENSBTAP00000000841; -.
DR   PaxDb; Q56JW4; -.
DR   PeptideAtlas; Q56JW4; -.
DR   PRIDE; Q56JW4; -.
DR   GeneID; 519017; -.
DR   KEGG; bta:519017; -.
DR   CTD; 353; -.
DR   eggNOG; KOG1712; Eukaryota.
DR   HOGENOM; CLU_063339_3_2_1; -.
DR   InParanoid; Q56JW4; -.
DR   OrthoDB; 1291050at2759; -.
DR   TreeFam; TF300227; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0002055; F:adenine binding; IBA:GO_Central.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; ISS:UniProtKB.
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   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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Glycosyltransferase; Phosphoprotein;
KW   Purine salvage; Reference proteome; 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_0000240344"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
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         135
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07741"
SQ   SEQUENCE   180 AA;  19537 MW;  12594AF43DAFBCD4 CRC64;
     MADPELQLVA RRIRSFPNFP IPGVLFRDIS PVLKDPTSFR ASINLLANHL KKAHGGRIDY
     IAGLDSRGFL FGPSLAQELG LGCILIRKRG KLPGPTVCAS YALEYGKGEL EIQRDALEPG
     QKVVVVDDLL ATGGTMCAAC ELLGQLRAEV LECVSLVELT SLKGREKLGA VPFFSLLQYE