ID O44095_DROSU Unreviewed; 181 AA.
AC O44095;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00017366};
DE EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
DE Flags: Fragment;
GN Name=Aprt {ECO:0000313|EMBL:AAB87885.1,
GN ECO:0000313|FlyBase:FBgn0023247};
OS Drosophila subobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7241 {ECO:0000313|EMBL:AAB87885.1};
RN [1] {ECO:0000313|EMBL:AAB87885.1}
RP NUCLEOTIDE SEQUENCE.
RA Zeng L.-W., Comeron J.M., Chen B., Kreitman M.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAB87885.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9720289; DOI=10.1023/A:1017035109224;
RA Zeng L.-W., Comeron J.M., Chen B., Kreitman M.;
RT "The molecular clock revisited: the rate of synonymous vs. replacement
RT change in Drosophila.";
RL Genetica 102:369-382(1998).
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; AF025800; AAB87885.1; -; mRNA.
DR AlphaFoldDB; O44095; -.
DR FlyBase; FBgn0023247; Dsub\Aprt.
DR UniPathway; UPA00588; UER00646.
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 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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:AAB87885.1};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAB87885.1}.
FT DOMAIN 46..160
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT NON_TER 181
FT /evidence="ECO:0000313|EMBL:AAB87885.1"
SQ SEQUENCE 181 AA; 19886 MW; F34786596C31F726 CRC64;
MSQISAEDKL DYVKSKIGEY PNFPKEGILF RDIFGALTDP KACVYLRDLL VQYIKQNQPE
VEVIVGLDSR GFLFNLLLAT ELGVGCAPIR KKGKLAGEVV AVEYQLEYGS DTFELQRAAI
QPGQKVVIVD DLLATGGSLL AASQLVRKVG GVVLESLVVM ELVDLDGRKK LDCKVHSLIK
Y
//
