ID   APT_ACTPJ               Reviewed;         179 AA.
AC   B0BSS1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   04-NOV-2026, entry version 88.
DE   RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004};
DE            Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004};
DE            EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004};
GN   Name=apt {ECO:0000255|HAMAP-Rule:MF_00004};
GN   OrderedLocusNames=APJL_0274;
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03;
RX   PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA   Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA   Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA   Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA   Zhao G.-P., Chen H.;
RT   "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT   serotype 3 prevalent in China.";
RL   PLoS ONE 3:E1450-E1450(2008).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC       AMP, that is energically less costly than de novo synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00004}.
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:0000255|HAMAP-Rule:MF_00004};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABY68873.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000687; ABY68873.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005596155.1; NC_010278.1.
DR   AlphaFoldDB; B0BSS1; -.
DR   SMR; B0BSS1; -.
DR   GeneID; 48598419; -.
DR   KEGG; apj:APJL_0274; -.
DR   HOGENOM; CLU_063339_3_0_6; -.
DR   OMA; AAACQMV; -.
DR   UniPathway; UPA00588; UER00646.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006168; P:adenine salvage; IEA:InterPro.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniRule.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   FunFam; 3.40.50.2020:FF:000004; Adenine phosphoribosyltransferase; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR   InterPro; IPR005764; Ade_phspho_trans.
DR   InterPro; IPR050120; Adenine_PRTase.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR000836; PRTase_dom.
DR   NCBIfam; NF002632; apt; 1.
DR   NCBIfam; TIGR01090; apt; 1.
DR   NCBIfam; NF002634; PRK02304.1-3; 1.
DR   NCBIfam; NF002636; PRK02304.1-5; 1.
DR   PANTHER; PTHR11776; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11776:SF7; PHOSPHORIBOSYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT   CHAIN           1..179
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000334708"
SQ   SEQUENCE   179 AA;  19491 MW;  35ADB04389F50485 CRC64;
     MNQLDLIKSS IKSIPDYPKA GIIFRDITSL LEVPEAFKAT VDAIVAEFKD KGITKVVGTE
     SRGFIFGAPV ALALGVPFVL VRKPKKLPRA VISQSYALEY GEDTLEIHLD SVKENDNVLM
     VDDLLATGGT IDATAKLIRR LGGKVEHAAF VIWLPDLGGK ERLEKEGINS FTLVEFAGH
//