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 27-MAR-2024, entry version 104. 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=Suden_1118; OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira OS denitrificans (strain ATCC 33889 / DSM 1251)). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Sulfurimonadaceae; Sulfurimonas. OX NCBI_TaxID=326298; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33889 / DSM 1251; 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., Hemp J., RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A., RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E., RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A., RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D., RA Sprinkle R., Stephens J., Thomas P., Vaughn R., 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 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}. 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; WP_011372748.1; NC_007575.1. DR AlphaFoldDB; Q30RI5; -. DR SMR; Q30RI5; -. DR STRING; 326298.Suden_1118; -. DR KEGG; tdn:Suden_1118; -. DR eggNOG; COG0503; Bacteria. DR HOGENOM; CLU_063339_3_0_7; -. DR OrthoDB; 9803963at2; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002714; 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 NCBIfam; TIGR01090; apt; 1. DR PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR32315:SF3; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; PRTase-like; 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..182 FT /note="Adenine phosphoribosyltransferase" FT /id="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 //