ID APT_SULDN Reviewed; 182 AA. AC Q30RI5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 04-NOV-2008, entry version 30. DE RecName: Full=Adenine phosphoribosyltransferase; DE Short=APRT; DE EC=2.4.2.7; GN Name=apt; OrderedLocusNames=Suden_1118; OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) OS (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfurimonas. OX NCBI_TaxID=326298; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18065616; DOI=10.1128/AEM.01844-07; RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., RA Hemp J., Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., RA Malfatti S.A., Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., RA Diaz E., Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., RA Long A., Mobberley J.M., Pantry S.N., Pazder G., Peterson S., RA Quintanilla J.D., Sprinkle R., Stephens J., Thomas P., Vaughn R., RA Weber M.J., Wooten L.L.; RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas RT denitrificans."; RL Appl. Environ. Microbiol. 74:1145-1156(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis (By CC similarity). CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000153; ABB44396.1; -; Genomic_DNA. DR RefSeq; YP_393631.1; -. DR GeneID; 3763667; -. DR GenomeReviews; CP000153_GR; Suden_1118. DR KEGG; tdn:Suden_1118; -. DR NMPDR; fig|326298.3.peg.1950; -. DR HOGENOM; Q30RI5; -. DR BioCyc; TDEN326298:TMDEN_1118-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:HAMAP. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. DR HAMAP; MF_00004; -; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR002375; Pr/py_Pribosyl_transf_CS. DR InterPro; IPR000836; PRibTrfase. DR Pfam; PF00156; Pribosyltran; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 182 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321414. SQ SEQUENCE 182 AA; 20042 MW; 5286AAFF3BD192E2 CRC64; MTLSNTERAI IESAIRDIKD FPKPGIVFKD ITTLLNNGKA FGVTMNHLYE KYKEYNLDYI AGIDARGFIF GAALAQMLGV GFVPIRKKGK LPYTTISEKY SLEYGFDEVE IHLDAFSAIP NARVLLVDDL IATGGTAAAS VKLINQAGAL CVEACFILCL SFLDGYKKLQ ELTEVYSLVE VK //