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Database: UniProt
Entry: A0A091G7G6_9AVES
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ID   A0A091G7G6_9AVES        Unreviewed;       155 AA.
AC   A0A091G7G6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   RecName: Full=Adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00017366};
DE            EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
DE   Flags: Fragment;
GN   ORFNames=N303_10613 {ECO:0000313|EMBL:KFO77873.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO77873.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO77873.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO77873.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1. {ECO:0000256|ARBA:ARBA00004659}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00008391}.
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DR   EMBL; KL447840; KFO77873.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091G7G6; -.
DR   STRING; 55661.A0A091G7G6; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006168; P:adenine salvage; IEA:InterPro.
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   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};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:KFO77873.1};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO77873.1}.
FT   DOMAIN          11..133
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO77873.1"
FT   NON_TER         155
FT                   /evidence="ECO:0000313|EMBL:KFO77873.1"
SQ   SEQUENCE   155 AA;  16990 MW;  E722170AF1E950E2 CRC64;
     LCSDISPLLK DPVAFRTLID LLEDHLRASF PKIDYIAGLD SRGFLIGPPL AQRLGIGFIL
     IRKKGKLPGP TESVSYTLEY GKAELEIQSD AVEPGQKVVI VDDLLATGGT MCAASELMKR
     LKAEVLECLV VIELKLLKGS EKLNCIPFYS LLQFD
//
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