ID A0A0B8YD50_9SPHI Unreviewed; 175 AA. AC A0A0B8YD50; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 13-NOV-2019, entry version 23. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00004, ECO:0000256|SAAS:SAAS01090472}; DE Short=APRT {ECO:0000256|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000256|HAMAP-Rule:MF_00004, ECO:0000256|SAAS:SAAS01090463}; 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; Bacteroidetes; 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 CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000256|HAMAP-Rule:MF_00004, ECO:0000256|SAAS:SAAS01090470}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1- CC diphosphate + adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; CC EC=2.4.2.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00004, CC ECO:0000256|SAAS:SAAS01124295}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00004, CC ECO:0000256|SAAS:SAAS01090473}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00004, CC ECO:0000256|SAAS:SAAS01090458}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00004, CC ECO:0000256|SAAS:SAAS01090474}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000256|HAMAP- CC Rule:MF_00004, ECO:0000256|SAAS:SAAS01090468}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KHJ38455; KHJ38455; PBAC_12450. DR PATRIC; fig|1122941.3.peg.1248; -. 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 Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00004, KW ECO:0000256|SAAS:SAAS01090459}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00004, KW ECO:0000256|SAAS:SAAS01090465, ECO:0000313|EMBL:KHJ38455.1}; KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_00004, KW ECO:0000256|SAAS:SAAS01090461}; KW Reference proteome {ECO:0000313|Proteomes:UP000031461}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00004, KW ECO:0000256|SAAS:SAAS01090460, ECO:0000313|EMBL:KHJ38455.1}. FT DOMAIN 29 147 Pribosyltran. {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 //