ID   APT_ACTSZ               Reviewed;         180 AA.
AC   A6VMZ1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   02-SEP-2026, entry version 96.
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=Asuc_0970;
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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; CP000746; ABR74338.1; -; Genomic_DNA.
DR   RefSeq; WP_012072715.1; NC_009655.1.
DR   AlphaFoldDB; A6VMZ1; -.
DR   SMR; A6VMZ1; -.
DR   STRING; 339671.Asuc_0970; -.
DR   KEGG; asu:Asuc_0970; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_6; -.
DR   OrthoDB; 9803963at2; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000001114; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
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; IPR050120; Adenine_PRTase.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR000836; PRTase_dom.
DR   NCBIfam; TIGR01090; apt; 1.
DR   NCBIfam; NF002632; PRK02304.1-1; 1.
DR   NCBIfam; NF002634; PRK02304.1-3; 1.
DR   NCBIfam; NF002636; PRK02304.1-5; 1.
DR   PANTHER; PTHR11776; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11776:SF7; PHOSPHORIBOSYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 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..180
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000321332"
SQ   SEQUENCE   180 AA;  19561 MW;  098678BB9703B036 CRC64;
     MNKQLDLIKS SIKSIPNYPK EGIIFRDITS LTEIPEAFTA TVNLIAEAFR HKGITKIIGT
     ESRGFIFGAP VAVALGLPFI LVRKPGKLPR EVISQSYQLE YGEDKLEIHA DAIQKGDNVL
     VIDDLLATGG TVEACIKLVN RLGGDVKHAA FVINLPDLGG GERLRKQGVE PFTLVDFAGH
//