ID   APT_SHEON               Reviewed;         183 AA.
AC   Q8EFG1;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=SO_2012;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN55062.2; -; Genomic_DNA.
DR   RefSeq; NP_717618.2; NC_004347.2.
DR   RefSeq; WP_011072096.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EFG1; -.
DR   SMR; Q8EFG1; -.
DR   STRING; 211586.SO_2012; -.
DR   PaxDb; Q8EFG1; -.
DR   KEGG; son:SO_2012; -.
DR   PATRIC; fig|211586.12.peg.1931; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_6; -.
DR   OrthoDB; 1532478at2; -.
DR   PhylomeDB; Q8EFG1; -.
DR   BioCyc; SONE211586:G1GMP-1854-MON; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0002055; F:adenine binding; IBA:GO_Central.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0006168; P:adenine salvage; IBA:GO_Central.
DR   GO; GO:0044209; P:AMP salvage; IBA:GO_Central.
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..183
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000149446"
SQ   SEQUENCE   183 AA;  19746 MW;  722F70E4851F68C8 CRC64;
     MAMNTETLSL IKQSIKTIPN YPKEGILFRD VTSLLENATA YKATIDLLVE HYRSKGFTKI
     VGTEARGFLF GAPLALGLGI GFVPVRKPGK LPRATISQSY ELEYGHDSLE IHTDAITAND
     KVLVVDDLLA TGGTIEATVK LIRQLGGEVQ DAAFVISLPD LGGEARLTAL GLELVKLCEF
     EGE