ID   APT_RHILW               Reviewed;         181 AA.
AC   B5ZY62;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Rleg2_2775;
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304;
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(2010).
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; CP001191; ACI56045.1; -; Genomic_DNA.
DR   RefSeq; WP_003581166.1; NC_011369.1.
DR   AlphaFoldDB; B5ZY62; -.
DR   SMR; B5ZY62; -.
DR   STRING; 395492.Rleg2_2775; -.
DR   EnsemblBacteria; ACI56045; ACI56045; Rleg2_2775.
DR   KEGG; rlt:Rleg2_2775; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_5; -.
DR   OMA; KPGIVFR; -.
DR   OrthoDB; 1532478at2; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000008330; 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; Transferase.
FT   CHAIN           1..181
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_1000088995"
SQ   SEQUENCE   181 AA;  19518 MW;  14382D47D301E0C6 CRC64;
     MDKNTTSELA ASIRSIPDYP KPGIIFRDIT TLLGNPRAFR RAVDELVQPY AGTKIDKIAG
     MEARGFILGG AVAHQLSSGF VPIRKKGKLP HETVRIAYSL EYGVDEMEMH RDAVQPGEKV
     ILVDDLIATG GTAVGATKLL RQIGAEVVGA CFVIDLPDLG GRKKLEELGV VVHTLVEFSG
     H