ID A0A0B8YD50_9SPHI Unreviewed; 175 AA. AC A0A0B8YD50; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 22-FEB-2023, entry version 29. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000256|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000256|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000256|HAMAP-Rule:MF_00004, GN ECO:0000313|EMBL:KHJ38455.1}; GN ORFNames=PBAC_12450 {ECO:0000313|EMBL:KHJ38455.1}; OS Pedobacter glucosidilyticus. OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1122941 {ECO:0000313|EMBL:KHJ38455.1, ECO:0000313|Proteomes:UP000031461}; RN [1] {ECO:0000313|EMBL:KHJ38455.1, ECO:0000313|Proteomes:UP000031461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD6b {ECO:0000313|EMBL:KHJ38455.1, RC ECO:0000313|Proteomes:UP000031461}; RA Poehlein A., Daniel R., Simeonova D.D.; RT "Draft genome sequence of Pedobacter glucosidilyticus DD6b."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of CC AMP, that is energically less costly than de novo synthesis. CC {ECO:0000256|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:0000256|ARBA:ARBA00000868, ECO:0000256|HAMAP- CC Rule:MF_00004}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP CC from adenine: step 1/1. {ECO:0000256|ARBA:ARBA00004659, CC ECO:0000256|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase CC family. {ECO:0000256|ARBA:ARBA00008391, ECO:0000256|HAMAP- CC Rule:MF_00004}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KHJ38455.1}. 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; JMTN01000009; KHJ38455.1; -; Genomic_DNA. DR RefSeq; WP_039450225.1; NZ_JMTN01000009.1. DR AlphaFoldDB; A0A0B8YD50; -. DR STRING; 1122941.PBAC_12450; -. DR EnsemblBacteria; KHJ38455; KHJ38455; PBAC_12450. DR PATRIC; fig|1122941.3.peg.1248; -. DR OrthoDB; 9803963at2; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000031461; Unassembled WGS sequence. 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 PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR32315:SF3; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; PRTase-like; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00004}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_00004}; KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP- KW Rule:MF_00004}; Reference proteome {ECO:0000313|Proteomes:UP000031461}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00004}. FT DOMAIN 29..147 FT /note="Phosphoribosyltransferase" FT /evidence="ECO:0000259|Pfam:PF00156" SQ SEQUENCE 175 AA; 19612 MW; 2A19FD886D2542BA CRC64; MIEQQIKETV RDVMDFPKPG IVFKDITPIL KNQELCTQII DAFVERLSGL AFDAIAGIES RGFLFGLMLA NRLNKPFIPI RKAGKLPYKT VKQSYNLEYG SATIEMHEDA FEPRTKILIH DDLLATGGTV EATSLLIQKM KGEIAGFSFI ISLDFLRGKD LIKPYADKVV ALAEY //