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Database: UniProt
Entry: A0A0N0J4U5_9PROT
LinkDB: A0A0N0J4U5_9PROT
Original site: A0A0N0J4U5_9PROT 
ID   A0A0N0J4U5_9PROT        Unreviewed;       182 AA.
AC   A0A0N0J4U5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893, ECO:0000256|HAMAP-Rule:MF_00004};
DE            Short=APRT {ECO:0000256|HAMAP-Rule:MF_00004};
DE            EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893, ECO:0000256|HAMAP-Rule:MF_00004};
GN   Name=apt {ECO:0000256|HAMAP-Rule:MF_00004};
GN   ORFNames=D621_21410 {ECO:0000313|EMBL:KPF41695.1};
OS   beta proteobacterium AAP51.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523421 {ECO:0000313|EMBL:KPF41695.1, ECO:0000313|Proteomes:UP000037990};
RN   [1] {ECO:0000313|EMBL:KPF41695.1, ECO:0000313|Proteomes:UP000037990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP51 {ECO:0000313|EMBL:KPF41695.1,
RC   ECO:0000313|Proteomes:UP000037990};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:0000256|ARBA:ARBA00003968, ECO:0000256|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:0000256|ARBA:ARBA00000868, ECO:0000256|HAMAP-
CC         Rule:MF_00004};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1. {ECO:0000256|ARBA:ARBA00004659,
CC       ECO:0000256|HAMAP-Rule:MF_00004}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00004}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00008391, ECO:0000256|HAMAP-
CC       Rule:MF_00004}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPF41695.1}.
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DR   EMBL; LJHT01000133; KPF41695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0J4U5; -.
DR   PATRIC; fig|1523421.3.peg.750; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000037990; Unassembled WGS sequence.
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   NCBIfam; TIGR01090; apt; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00004};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00004};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_00004};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00004}.
FT   DOMAIN          46..158
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   182 AA;  19813 MW;  8F0CEAE7F3F769F6 CRC64;
     MATTAPADYI RSHIRTVPHW PVPGVMFRDI TPLLANPRVF RVLIDQFVHR YFDVQPAAIA
     GLDARGFIIG SVVAYELNVG FVPIRKKGKL PFTTVEETYE LEYGSATVEM HTDAVKPGDR
     VVLIDDLIAT GGTMMAGKKL LERLGAQVLE GAAIVDLPEL GGSSKLREAG LPLFTLVDFA
     GH
//
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