APT_SALTY
ID APT_SALTY Reviewed; 183 AA.
AC Q8ZRA2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004};
DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004};
DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004};
GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=STM0483;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00004};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00004}.
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DR EMBL; AE006468; AAL19437.1; -; Genomic_DNA.
DR RefSeq; NP_459478.1; NC_003197.2.
DR RefSeq; WP_000127350.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRA2; -.
DR SMR; Q8ZRA2; -.
DR STRING; 99287.STM0483; -.
DR PaxDb; Q8ZRA2; -.
DR EnsemblBacteria; AAL19437; AAL19437; STM0483.
DR GeneID; 1252003; -.
DR KEGG; stm:STM0483; -.
DR PATRIC; fig|99287.12.peg.516; -.
DR HOGENOM; CLU_063339_3_0_6; -.
DR OMA; KPGIVFR; -.
DR PhylomeDB; Q8ZRA2; -.
DR BioCyc; SENT99287:STM0483-MON; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IBA:GO_Central.
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 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 Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..183
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149445"
SQ SEQUENCE 183 AA; 19985 MW; 0A0EB6040CF13FFE CRC64;
MTATAQQLEF LKNSIKSIQD YPKPGILFRD VTSLLEDPKA YALSIELLVE RYKNAGITKV
VGTEARGFLF GAPVALGLGV GFVPVRKPRK LPRETIAETY ELEYGTDQLE IHVDAIKPGD
NVLVVDDLLA TGGTIEATVK LIRRLGGKVT DAAFIINLFD LGGEQRLEKQ GITCYSLVPF
PGH
