(data stored in ACNUC7421 zone)

SWISSPROT: APT_ECODH

ID   APT_ECODH               Reviewed;         183 AA.
AC   B1XFQ6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 65.
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=ECDH10B_0425;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB01596.1; -; Genomic_DNA.
DR   RefSeq; WP_000127356.1; NC_010473.1.
DR   ProteinModelPortal; B1XFQ6; -.
DR   SMR; B1XFQ6; -.
DR   EnsemblBacteria; ACB01596; ACB01596; ECDH10B_0425.
DR   KEGG; ecd:ECDH10B_0425; -.
DR   eggNOG; ENOG4109003; Bacteria.
DR   eggNOG; COG0503; LUCA.
DR   HOGENOM; HOG000036776; -.
DR   KO; K00759; -.
DR   OMA; CAPIRKK; -.
DR   UniPathway; UPA00588; UER00646.
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; B1XFQ6.
DR   SWISS-2DPAGE; B1XFQ6.
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT   CHAIN         1    183       Adenine phosphoribosyltransferase.
FT                                /FTId=PRO_1000088969.
SQ   SEQUENCE   183 AA;  19859 MW;  AB45F0B5A219480D CRC64;
     MTATAQQLEY LKNSIKSIQD YPKPGILFRD VTSLLEDPKA YALSIDLLVE RYKNAGITKV
     VGTEARGFLF GAPVALGLGV GFVPVRKPGK LPRETISETY DLEYGTDQLE IHVDAIKPGD
     KVLVVDDLLA TGGTIEATVK LIRRLGGEVA DAAFIINLFD LGGEQRLEKQ GITSYSLVPF
     PGH
//

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