APT_HELPY
ID APT_HELPY Reviewed; 179 AA.
AC O25296;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=HP_0572;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07640.1; -; Genomic_DNA.
DR PIR; D64591; D64591.
DR RefSeq; NP_207367.1; NC_000915.1.
DR RefSeq; WP_001006135.1; NC_018939.1.
DR AlphaFoldDB; O25296; -.
DR SMR; O25296; -.
DR IntAct; O25296; 2.
DR STRING; 85962.C694_02950; -.
DR PaxDb; O25296; -.
DR EnsemblBacteria; AAD07640; AAD07640; HP_0572.
DR KEGG; hpy:HP_0572; -.
DR PATRIC; fig|85962.47.peg.617; -.
DR eggNOG; COG0503; Bacteria.
DR OMA; KPGIVFR; -.
DR PhylomeDB; O25296; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000000429; 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..179
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149394"
SQ SEQUENCE 179 AA; 19845 MW; A9EF879DDBA6F9AA CRC64;
MNETLKEELL QSIREVKDYP KKGILFKDIT TLLNYPKLFN KLIDTLKKRY LALNIDFIVG
IEARGFILGS ALAYALGVGF VPVRKKGKLP AHTLSQSYSL EYGSDSIEIH SDAFRGIKGV
RVVLIDDLLA TGGTALASLE LIKALQAECI EACFLIGLKE LPGIQLLEER VKTFCLLEC