APT_STRCO
ID APT_STRCO Reviewed; 182 AA.
AC P52561; Q9L294;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 130.
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=SCO1514;
GN ORFNames=SCL2.04c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=8825780; DOI=10.1046/j.1365-2958.1996.390919.x;
RA Chakraburtty R., White J., Takano E., Bibb M.J.;
RT "Cloning, characterization and disruption of a (p)ppGpp synthetase gene
RT (relA) of Streptomyces coelicolor A3(2).";
RL Mol. Microbiol. 19:357-368(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RA Loriaux A., Frare P., Brans A., Dusart J.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 142-182.
RC STRAIN=A3(2) / J802;
RX PubMed=8631867; DOI=10.1074/jbc.271.18.10627;
RA Martinez-Costa O.H., Arias P., Romero N.M., Parro V., Mellado R.P.,
RA Malpartida F.;
RT "A relA/spoT homologous gene from Streptomyces coelicolor A3(2) controls
RT antibiotic biosynthetic genes.";
RL J. Biol. Chem. 271:10627-10634(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB70916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X87267; CAA60716.1; -; Genomic_DNA.
DR EMBL; X85969; CAA59956.1; -; Genomic_DNA.
DR EMBL; AL939109; CAB70916.1; ALT_INIT; Genomic_DNA.
DR EMBL; X92520; CAA63298.1; -; Genomic_DNA.
DR PIR; S70689; S70689.
DR RefSeq; NP_625793.1; NC_003888.3.
DR RefSeq; WP_011027822.1; NC_003888.3.
DR RefSeq; WP_016325803.1; NZ_VNID01000021.1.
DR AlphaFoldDB; P52561; -.
DR SMR; P52561; -.
DR STRING; 100226.SCO1514; -.
DR GeneID; 1096940; -.
DR KEGG; sco:SCO1514; -.
DR PATRIC; fig|100226.15.peg.1523; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_3_11; -.
DR InParanoid; P52561; -.
DR PhylomeDB; P52561; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002055; F:adenine binding; IBA:GO_Central.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0006168; P:adenine salvage; IBA:GO_Central.
DR GO; GO:0044209; P:AMP salvage; IBA:GO_Central.
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..182
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149462"
FT CONFLICT 104..105
FT /note="YG -> VS (in Ref. 2; CAA59956)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="E -> K (in Ref. 2; CAA59956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 18599 MW; 40E68FD6E4730724 CRC64;
MTEPTGITEL LLSRIRDVAD YPEPGVVFKD ITPLLADPGA FAALTDALAE AAGRTGATKV
VGLEARGFIL GAPVALRAGL GFIPVRKAGK LPGATLSQAY DLEYGSAEIE VHAEDLTAGD
RVLVVDDVLA TGGTAEASLE LIRRAGAEVA GLAVLMELGF LGGRARLEPA LAGAPLEALL
TV
