ID   APT_BLOFL               Reviewed;         183 AA.
AC   Q7VRB8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
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}; OrderedLocusNames=Bfl300;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83371.1; -; Genomic_DNA.
DR   RefSeq; WP_011126579.1; NC_005061.1.
DR   AlphaFoldDB; Q7VRB8; -.
DR   SMR; Q7VRB8; -.
DR   STRING; 203907.Bfl300; -.
DR   EnsemblBacteria; CAD83371; CAD83371; Bfl300.
DR   KEGG; bfl:Bfl300; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_6; -.
DR   OMA; KPGIVFR; -.
DR   OrthoDB; 1532478at2; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000002192; 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.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..183
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000149370"
SQ   SEQUENCE   183 AA;  20283 MW;  6954E86205FF4768 CRC64;
     MISHTDHQLT LIKENIKFIP NYPKQGILFR DITALLENPH AYSACIKLLA DHYKNHQLTK
     IVGVEARGFL FGSPLALILK LGFIPARKAG RLPRNTISES YVLEYGTGCL EMHNDSIIPG
     DRVLIVDDLL ATGGTIKAVV KLIRRLGGEV YHAAFVIDLE KLGGKLLLEK IGVHPYSLVI
     FSD