ID   APT_MYCFP               Reviewed;         171 AA.
AC   Q9RFQ2; C4XE30;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=MBIO_0137;
OS   Mycoplasmopsis fermentans (strain ATCC 19989 / NBRC 14854 / NCTC 10117 /
OS   PG18) (Mycoplasma fermentans).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mycoplasmopsis.
OX   NCBI_TaxID=496833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18;
RX   PubMed=10601219; DOI=10.1128/jb.181.24.7597-7607.1999;
RA   Calcutt M.J., Lavrrar J.L., Wise K.S.;
RT   "IS1630 of Mycoplasma fermentans, a novel IS30-type insertion element that
RT   targets and duplicates inverted repeats of variable length and sequence
RT   during insertion.";
RL   J. Bacteriol. 181:7597-7607(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18;
RX   PubMed=19219498; DOI=10.1007/s00284-009-9362-6;
RA   Ishida N., Irikura D., Matsuda K., Sato S., Sone T., Tanaka M., Asano K.;
RT   "Molecular cloning and expression of a novel cholinephosphotransferase
RT   involved in glycoglycerophospholipid biosynthesis of Mycoplasma
RT   fermentans.";
RL   Curr. Microbiol. 58:535-540(2009).
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=BAH69402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF179373; AAF15560.1; -; Genomic_DNA.
DR   EMBL; AP009608; BAH69402.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_013526633.1; NC_021002.1.
DR   AlphaFoldDB; Q9RFQ2; -.
DR   SMR; Q9RFQ2; -.
DR   KEGG; mfp:MBIO_0137; -.
DR   PATRIC; fig|496833.3.peg.558; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_14; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000006810; 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   NCBIfam; TIGR01090; apt; 1.
DR   PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR32315:SF3; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..171
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000149409"
SQ   SEQUENCE   171 AA;  18850 MW;  2D16B6C644997B52 CRC64;
     MDLKKYIRDI ENFPKTGIMF KDISPLLANG KALNYTITEM AKLAQDVDVI VGPDARGFLF
     GTPTAAFLKK PFIMVRKPGK LPGDVISKSY DLEYGNNVLQ IQKGFIKKGQ TVAIIDDVLA
     TGGTTKAIIK LLEEQGAIVK KVILLLELVD LNGRQLITKD NDIEIVSLVK F
//