ID   APT_ALKOO               Reviewed;         172 AA.
AC   A8MGN2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   02-SEP-2026, 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};
GN   OrderedLocusNames=Clos_1715;
OS   Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS   OhILAs)).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC   Natronincolaceae; Alkaliphilus.
OX   NCBI_TaxID=350688;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OhILAs;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA   Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT   "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL   Submitted (OCT-2007) 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; CP000853; ABW19255.1; -; Genomic_DNA.
DR   RefSeq; WP_012159567.1; NC_009922.1.
DR   AlphaFoldDB; A8MGN2; -.
DR   SMR; A8MGN2; -.
DR   STRING; 350688.Clos_1715; -.
DR   KEGG; aoe:Clos_1715; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_9; -.
DR   OrthoDB; 9803963at2; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000000269; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002055; F:adenine binding; IEA:TreeGrafter.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016208; F:AMP binding; IEA:TreeGrafter.
DR   GO; GO:0006168; P:adenine salvage; IEA:InterPro.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniRule.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   FunFam; 3.40.50.2020:FF:000004; Adenine phosphoribosyltransferase; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR   InterPro; IPR005764; Ade_phspho_trans.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR000836; PRTase_dom.
DR   InterPro; IPR050054; UPRTase/APRTase.
DR   NCBIfam; TIGR01090; apt; 1.
DR   NCBIfam; NF002633; PRK02304.1-2; 1.
DR   NCBIfam; NF002634; PRK02304.1-3; 1.
DR   NCBIfam; NF002636; PRK02304.1-5; 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..172
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_1000057028"
SQ   SEQUENCE   172 AA;  18935 MW;  A91BA7197F4F1F67 CRC64;
     MDLKSKIRQI EGFPKEGISF KDITTVLKEG EALQYVTDQL TEQLKDLNID IIVGPEARGF
     LVGTPVAYKL GVGFVPVRKP GKLPAETLTY EYELEYGTDS LQIHKDSIRP GQRVAIVDDL
     LATGGTVLAT AKMVEALGGQ VVSMNFLIEL TGLKGRDILK GYEIKSLVEY EF
//