APT_MUSPA
ID APT_MUSPA Reviewed; 180 AA.
AC P47956;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000250|UniProtKB:P07741};
DE Short=APRT;
DE EC=2.4.2.7 {ECO:0000250|UniProtKB:P07741};
GN Name=Aprt {ECO:0000250|UniProtKB:P07741};
OS Mus pahari (Gairdner's shrew-mouse) (Coelomys pahari).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Coelomys.
OX NCBI_TaxID=10093;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9023989; DOI=10.1038/hdy.1997.3;
RA Fieldhouse D., Yazdani F., Golding G.B.;
RT "Substitution rate variation in closely related rodent species.";
RL Heredity 78:21-31(1997).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC {ECO:0000250|UniProtKB:P07741}.
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:0000250|UniProtKB:P07741};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000250|UniProtKB:P07741}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; U28721; AAA68957.1; -; Genomic_DNA.
DR AlphaFoldDB; P47956; -.
DR SMR; P47956; -.
DR UniPathway; UPA00588; UER00646.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; ISS:UniProtKB.
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 Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01090; apt; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; Glycosyltransferase; Phosphoprotein;
KW Purine salvage; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P36972"
FT CHAIN 2..180
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149507"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P36972"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 60
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
SQ SEQUENCE 180 AA; 19712 MW; A8F43EB56F4D2CBF CRC64;
MSESELKLVA RRIRSFPDFP IPGVLFRDIS PLLKDPDSFR ASIRLLASHL KSTHSGKIDY
IAGLDSRGFL FGPSLAQELG VGCVLIRKQG KLPGPTISAS YALEYGKAEL EIQKDALEPG
QRVVIVDDLL ATGGTMFAAC DLLHQLRAEV VECVSLVELT SLKGRERLGP IPFFSLLQYD
