(data stored in ACNUC7421 zone)

SWISSPROT: APT_ECO57

ID   APT_ECO57               Reviewed;         183 AA.
AC   Q8XD48;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, 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};
GN   OrderedLocusNames=Z0586, ECs0522;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation
CC       of AMP, that is energically less costly than de novo synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00004}.
CC   -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha-
CC       D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP 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
CC       phosphoribosyltransferase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00004}.
DR   EMBL; AE005174; AAG54818.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33945.1; -; Genomic_DNA.
DR   PIR; B90694; B90694.
DR   PIR; F85544; F85544.
DR   RefSeq; NP_308549.1; NC_002695.1.
DR   RefSeq; WP_001301904.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; Q8XD48; -.
DR   SMR; Q8XD48; -.
DR   STRING; 155864.Z0586; -.
DR   EnsemblBacteria; AAG54818; AAG54818; Z0586.
DR   EnsemblBacteria; BAB33945; BAB33945; BAB33945.
DR   GeneID; 914626; -.
DR   KEGG; ece:Z0586; -.
DR   KEGG; ecs:ECs0522; -.
DR   PATRIC; fig|386585.9.peg.628; -.
DR   eggNOG; ENOG4109003; Bacteria.
DR   eggNOG; COG0503; LUCA.
DR   HOGENOM; HOG000036776; -.
DR   KO; K00759; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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   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;
DR   PRODOM; Q8XD48.
DR   SWISS-2DPAGE; Q8XD48.
KW   Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage;
KW   Transferase.
FT   CHAIN         1    183       Adenine phosphoribosyltransferase.
FT                                /FTId=PRO_0000149381.
SQ   SEQUENCE   183 AA;  19872 MW;  AB45F0A04216A817 CRC64;
     MTATAQQLEY LKNSIKSIQD YPKPGILFRD VTSLLEDPKA YALSIDLLVE RYKNAGINKV
     VGTEARGFLF GAPVALGLGV GFVPVRKPGK LPRETISETY DLEYGTDQLE IHVDAIKPGD
     KVLVVDDLLA TGGTIEATVK LIRRLGGEVA DAAFIINLFD LGGEQRLEKQ GITSYSLVPF
     PGH
//

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