ID   APT_FRATT               Reviewed;         175 AA.
AC   Q5NII9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=FTT_0078;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG44711.1; -; Genomic_DNA.
DR   RefSeq; WP_003028608.1; NZ_CP010290.1.
DR   RefSeq; YP_169153.1; NC_006570.2.
DR   PDB; 5YW2; X-ray; 2.28 A; A/B/C/D=1-175.
DR   PDB; 5YW5; X-ray; 1.90 A; A/B/C/D=1-175.
DR   PDBsum; 5YW2; -.
DR   PDBsum; 5YW5; -.
DR   AlphaFoldDB; Q5NII9; -.
DR   SMR; Q5NII9; -.
DR   STRING; 177416.FTT_0078; -.
DR   DNASU; 3191768; -.
DR   EnsemblBacteria; CAG44711; CAG44711; FTT_0078.
DR   GeneID; 60806004; -.
DR   KEGG; ftu:FTT_0078; -.
DR   eggNOG; COG0503; Bacteria.
DR   OMA; KPGIVFR; -.
DR   BRENDA; 2.4.2.7; 14771.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000001174; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Glycosyltransferase; Purine salvage;
KW   Reference proteome; Transferase.
FT   CHAIN           1..175
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000149384"
FT   HELIX           1..7
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   HELIX           27..31
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   HELIX           35..49
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          55..60
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   HELIX           63..75
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          78..83
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          100..109
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          118..128
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   HELIX           130..141
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          145..155
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   HELIX           160..163
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   TURN            164..166
FT                   /evidence="ECO:0007829|PDB:5YW5"
FT   STRAND          169..175
FT                   /evidence="ECO:0007829|PDB:5YW5"
SQ   SEQUENCE   175 AA;  18795 MW;  253CEA24588DA900 CRC64;
     MNLDFIKSKI AAVPDFPKPG IMFRDITPLL ADPQGLRKTA EAMAQELKNK GIQPTIVAGT
     ESRGFIFGVA LAEVLGLGFV PVRKPGKLPR ATYSVKYDLE YGSDSLEIHQ DAFKVTDEVL
     VVDDLLATGG TAKATVDLIE KTQAKVAGLI FVMELDGLGG REVLAGYNVS ALIKF