ID   APT_METVS               Reviewed;         173 AA.
AC   A6USF2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   04-NOV-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=apt2 {ECO:0000255|HAMAP-Rule:MF_00004};
GN   OrderedLocusNames=Mevan_1531;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanococci; Methanococcales; Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-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; CP000742; ABR55424.1; -; Genomic_DNA.
DR   RefSeq; WP_012066338.1; NC_009634.1.
DR   AlphaFoldDB; A6USF2; -.
DR   SMR; A6USF2; -.
DR   STRING; 406327.Mevan_1531; -.
DR   GeneID; 5325091; -.
DR   KEGG; mvn:Mevan_1531; -.
DR   eggNOG; arCOG00030; Archaea.
DR   HOGENOM; CLU_063339_3_0_2; -.
DR   OMA; AAACQMV; -.
DR   OrthoDB; 8323at2157; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000001107; 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   NCBIfam; NF009211; PRK12560.1; 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..173
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000329378"
SQ   SEQUENCE   173 AA;  19222 MW;  D6CE8FA5A5BE639D CRC64;
     MDLRKKIRII DDFPKKGISF KDVTPILKDP KSMKHTTKEI TKYLEDKNID VIVGPEARGF
     LFGILVAQEL DLGFVPVRKP GKLPFKTFSV DYALEYGLDR LEIHSDSIEK GQNVAVVDDL
     LATGGTVLGV TKLVEKIGGN VSALSFVIEL TNLNGRDKLK GYNVQSLVKY DDL
//