APT_STRPN
ID APT_STRPN Reviewed; 170 AA.
AC P63544; Q97PM8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=SP_1577;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(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 -!- INTERACTION:
CC P63544; P63588: aroD; NbExp=2; IntAct=EBI-2207316, EBI-2207290;
CC P63544; Q97SE7: gatB; NbExp=2; IntAct=EBI-2207316, EBI-2207023;
CC P63544; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207316, EBI-2207053;
CC P63544; P0A335: groEL; NbExp=2; IntAct=EBI-2207316, EBI-2207395;
CC P63544; Q97NV3: groES; NbExp=2; IntAct=EBI-2207316, EBI-2206949;
CC P63544; Q97S73: grpE; NbExp=2; IntAct=EBI-2207316, EBI-2207065;
CC P63544; Q97Q68: mecA; NbExp=2; IntAct=EBI-2207316, EBI-2207260;
CC P63544; P65946: pyrR; NbExp=2; IntAct=EBI-2207316, EBI-2207248;
CC P63544; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207316, EBI-2206983;
CC P63544; Q97QP2: xerS; NbExp=2; IntAct=EBI-2207316, EBI-2207218;
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; AE005672; AAK75663.1; -; Genomic_DNA.
DR PIR; F95183; F95183.
DR RefSeq; WP_001049323.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P63544; -.
DR SMR; P63544; -.
DR IntAct; P63544; 10.
DR STRING; 170187.SP_1577; -.
DR EnsemblBacteria; AAK75663; AAK75663; SP_1577.
DR GeneID; 60234426; -.
DR GeneID; 66806668; -.
DR KEGG; spn:SP_1577; -.
DR eggNOG; COG0503; Bacteria.
DR OMA; KPGIVFR; -.
DR PhylomeDB; P63544; -.
DR BioCyc; SPNE170187:G1FZB-1596-MON; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT CHAIN 1..170
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149465"
SQ SEQUENCE 170 AA; 18729 MW; C2C64EA945790C2F CRC64;
MNLKDYIATI ENYPKEGITF RDISPLMADG NAYSYAVREI VQYATDKKVD MIVGPEARGF
IVGCPVAFEL GIGFAPVRKP GKLPREVISA DYEKEYGVDT LTMHADAIKP GQRVLIVDDL
LATGGTVKAT IEMIEKLGGV MAGCAFLVEL DELNGREKIG DYDYKVLMHY
