ID   APT_BACC2               Reviewed;         170 AA.
AC   B7IIS0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=BCG9842_B0708;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) 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: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}.
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DR   EMBL; CP001186; ACK94881.1; -; Genomic_DNA.
DR   RefSeq; WP_000346215.1; NC_011772.1.
DR   AlphaFoldDB; B7IIS0; -.
DR   SMR; B7IIS0; -.
DR   EnsemblBacteria; ACK94881; ACK94881; BCG9842_B0708.
DR   GeneID; 67509044; -.
DR   KEGG; bcg:BCG9842_B0708; -.
DR   HOGENOM; CLU_063339_3_0_9; -.
DR   OMA; KPGIVFR; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000006744; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-UniRule.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT   CHAIN           1..170
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_1000116163"
SQ   SEQUENCE   170 AA;  18630 MW;  A491A98F47D58FF7 CRC64;
     MDFKQHIAIV PDYPKEGIVF KDITPLMNDG KAYKAATDAI VEYAKERDID VVVGPEARGF
     IIGCPVSYAL EVGFAPVRKL GKLPREVITV DYGKEYGKDV LTIHKDAIKP GQRVLITDDL
     LATGGTIEAT IKLVEELGGV VAGIAFLVEL TYLDGRKMLD GYDVLVLEKY