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Database: UniProt
Entry: A0A151WX75_9HYME
LinkDB: A0A151WX75_9HYME
Original site: A0A151WX75_9HYME 
ID   A0A151WX75_9HYME        Unreviewed;       187 AA.
AC   A0A151WX75;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893};
DE            EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
GN   ORFNames=ALC60_08460 {ECO:0000313|EMBL:KYQ52416.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ52416.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ52416.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ52416.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ52416.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ982675; KYQ52416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151WX75; -.
DR   STRING; 64791.A0A151WX75; -.
DR   Proteomes; UP000075809; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR018276; DDA1_N.
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; PF10172; DDA1; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:KYQ52416.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KYQ52416.1}.
FT   DOMAIN          41..132
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   DOMAIN          132..151
FT                   /note="DET1- and DDB1-associated protein 1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10172"
FT   REGION          161..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   187 AA;  21390 MW;  B518336A956F6E48 CRC64;
     MDKNDKLQIL KNAIKSYPDF PEPGIIFRDI FSAFNNIVAL RAMKDLIMEH ILFLEVDLVV
     GLDSRGFLFG PIICMELGKP FLPVRKKGKL PGKVTQQKYT LEYGEATFEL QTEFINEGTR
     VLIVDDLLAT GVIVTEKTTI LLRYLHQQWD KKNADRKREF LSTNGDSQDD ASTVRSKRPR
     LDLNNSL
//
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