ID AMPPA_METBU Reviewed; 506 AA. AC Q12Z64; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 05-JUL-2017, entry version 73. DE RecName: Full=AMP phosphorylase {ECO:0000255|HAMAP-Rule:MF_02132}; DE Short=AMPpase {ECO:0000255|HAMAP-Rule:MF_02132}; DE EC=2.4.2.57 {ECO:0000255|HAMAP-Rule:MF_02132}; DE AltName: Full=Nucleoside monophosphate phosphorylase {ECO:0000255|HAMAP-Rule:MF_02132}; DE Short=NMP phosphorylase {ECO:0000255|HAMAP-Rule:MF_02132}; GN OrderedLocusNames=Mbur_0255; OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / OS ACE-M). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M; RX PubMed=19404327; DOI=10.1038/ismej.2009.45; RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S., RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., RA Ting L., Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., RA Ivanova N., Dalin E., Martinez M., Lapidus A., Hauser L., Land M., RA Thomas T., Cavicchioli R.; RT "The genome sequence of the psychrophilic archaeon, Methanococcoides RT burtonii: the role of genome evolution in cold adaptation."; RL ISME J. 3:1012-1035(2009). CC -!- FUNCTION: Catalyzes the conversion of AMP and phosphate to adenine CC and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase CC activity toward CMP and UMP in addition to AMP. Functions in an CC archaeal AMP degradation pathway, together with R15P isomerase and CC RubisCO. {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- CATALYTIC ACTIVITY: AMP + phosphate = adenine + alpha-D-ribose CC 1,5-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- CATALYTIC ACTIVITY: CMP + phosphate = cytosine + alpha-D-ribose CC 1,5-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- CATALYTIC ACTIVITY: UMP + phosphate = uracil + alpha-D-ribose 1,5- CC bisphosphate. {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside CC phosphorylase family. Type 2 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_02132}. 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; CP000300; ABE51262.1; -; Genomic_DNA. DR RefSeq; WP_011498424.1; NC_007955.1. DR ProteinModelPortal; Q12Z64; -. DR SMR; Q12Z64; -. DR STRING; 259564.Mbur_0255; -. DR EnsemblBacteria; ABE51262; ABE51262; Mbur_0255. DR GeneID; 3998750; -. DR KEGG; mbu:Mbur_0255; -. DR eggNOG; arCOG02013; Archaea. DR eggNOG; COG0213; LUCA. DR HOGENOM; HOG000252767; -. DR KO; K18931; -. DR OMA; VHSIGGV; -. DR OrthoDB; POG093Z01M3; -. DR Proteomes; UP000001979; Chromosome. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0004645; F:phosphorylase activity; IEA:InterPro. DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:InterPro. DR GO; GO:0046125; P:pyrimidine deoxyribonucleoside metabolic process; IEA:InterPro. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro. DR Gene3D; 3.40.1030.10; -; 1. DR HAMAP; MF_02132; AMP_phosphorylase; 1. DR InterPro; IPR017713; AMP_phosphorylase. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR013102; PYNP_C. DR InterPro; IPR017872; Pyrmidine_PPase_CS. DR InterPro; IPR013466; Thymidine/AMP_Pase. DR InterPro; IPR000053; Thymidine/pyrmidine_PPase. DR PANTHER; PTHR10515; PTHR10515; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR Pfam; PF01568; Molydop_binding; 1. DR Pfam; PF07831; PYNP_C; 1. DR PIRSF; PIRSF000478; TP_PyNP; 2. DR SMART; SM00941; PYNP_C; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR SUPFAM; SSF54680; SSF54680; 1. DR TIGRFAMs; TIGR03327; AMP_phos; 1. DR TIGRFAMs; TIGR02645; ARCH_P_rylase; 1. DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 506 AMP phosphorylase. FT /FTId=PRO_0000314720. FT NP_BIND 194 199 AMP. {ECO:0000255|HAMAP-Rule:MF_02132}. FT ACT_SITE 256 256 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02132}. FT BINDING 168 168 AMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02132}. FT BINDING 203 203 AMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02132}. FT BINDING 264 264 AMP. {ECO:0000255|HAMAP-Rule:MF_02132}. FT BINDING 288 288 AMP. {ECO:0000255|HAMAP-Rule:MF_02132}. SQ SEQUENCE 506 AA; 55123 MW; A44D08052CF1DFDA CRC64; MQLKVQPIDV KVGKYKVILN TIDAKELGVH EGDRVRIKNH VTLTAIVDFT EDMISPGMIG LYHEVKEALS KEWTETVEVF PAEKPKSTYI IRKTMDGQKL TKEEIDILVK DIVEENLAEI EIAAFLTATY INDMTDDETE WLTRAMIDSG DKLEFDTHPI MDKHSIGGVP GNKISLLIVP IVAANGLLIP KTSSRAITGA GGTADLMEIL APVEFDAAEI KRMTEEVGGV LVWGGATNIA PADDKLIKVE YPLSIDPHCQ MLASIMAKKG AIGADHVVMD IPTGPGTKIK NVQEGRKLAR DLINLGDRLG MDVDCALTYG ASPVGRTIGP ALEVIEALKV LESFEGPNSL IEKSASLAGM LLEMGNVAGK DKGYDLAIET LKNGKALTKF KEIIKIQGGN PDVTHKDISV GEFTEDIIAP NNGYILEMDN KRLVQIARLA GAPNDKGAGI LLHRKQGEPL KEGDPVMTIY AEKKSKLENA VKSAKERPPF IVEGMMLERI QSFKEI //