ID   APT_LACLA               Reviewed;         170 AA.
AC   Q9CHT5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   25-MAY-2022, entry version 113.
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=LL0633;
GN   ORFNames=L22735;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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=AAK04731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005176; AAK04731.1; ALT_INIT; Genomic_DNA.
DR   PIR; A86704; A86704.
DR   RefSeq; NP_266789.1; NC_002662.1.
DR   RefSeq; WP_012897343.1; NC_002662.1.
DR   AlphaFoldDB; Q9CHT5; -.
DR   SMR; Q9CHT5; -.
DR   STRING; 272623.L22735; -.
DR   PaxDb; Q9CHT5; -.
DR   EnsemblBacteria; AAK04731; AAK04731; L22735.
DR   GeneID; 66441549; -.
DR   KEGG; lla:L22735; -.
DR   PATRIC; fig|272623.7.peg.677; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_9; -.
DR   OMA; KPGIVFR; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000002196; 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..170
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000149399"
SQ   SEQUENCE   170 AA;  18713 MW;  0C4F28013A26FDE0 CRC64;
     MELKDYIATI ENYPKEGVVF RDISPLMADG NAYNYAATEI VQYARDKEID MVVGPEARGF
     IIGCPVAFAL GVGFAPVRKP GKLPREVIEA TYEKEYGTDT LTMHSDSIKP GQRVLIVDDL
     LATGGTIAAT IELVEKMGGI VVGCAFLIEL DELKGREKIG DYDYKVLMHY