ID AMPPA_METAR Reviewed; 503 AA. AC Q0W5A8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 97. 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=UNCMA_17660; ORFNames=RCIX1126; OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanocellales; Methanocellaceae; Methanocella. OX NCBI_TaxID=351160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22066 / NBRC 105507 / MRE50; RX PubMed=16857943; DOI=10.1126/science.1127062; RA Erkel C., Kube M., Reinhardt R., Liesack W.; RT "Genome of rice cluster I archaea -- the key methane producers in the rice RT rhizosphere."; RL Science 313:370-372(2006). CC -!- FUNCTION: Catalyzes the conversion of AMP and phosphate to adenine and CC ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CC CMP and UMP in addition to AMP. Functions in an archaeal AMP CC degradation pathway, together with R15P isomerase and RubisCO. CC {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate; CC Xref=Rhea:RHEA:36975, ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:68688, ChEBI:CHEBI:456215; EC=2.4.2.57; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02132}; CC -!- CATALYTIC ACTIVITY: CC Reaction=CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine; CC Xref=Rhea:RHEA:36987, ChEBI:CHEBI:16040, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:60377, ChEBI:CHEBI:68688; EC=2.4.2.57; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02132}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil; CC Xref=Rhea:RHEA:36991, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57865, ChEBI:CHEBI:68688; EC=2.4.2.57; CC Evidence={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; AM114193; CAJ36435.1; -; Genomic_DNA. DR RefSeq; WP_012036091.1; NC_009464.1. DR AlphaFoldDB; Q0W5A8; -. DR SMR; Q0W5A8; -. DR STRING; 351160.RCIX1126; -. DR GeneID; 5144338; -. DR KEGG; rci:RCIX1126; -. DR PATRIC; fig|351160.9.peg.1803; -. DR eggNOG; arCOG02013; Archaea. DR OrthoDB; 9827at2157; -. DR Proteomes; UP000000663; Chromosome. DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro. DR GO; GO:0016208; F:AMP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016763; F:pentosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006196; P:AMP catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046125; P:pyrimidine deoxyribonucleoside metabolic process; IEA:InterPro. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro. DR Gene3D; 1.20.970.50; -; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1. DR Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1. DR HAMAP; MF_02132; AMP_phosphorylase; 1. DR InterPro; IPR017713; AMP_phosphorylase. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf. DR InterPro; IPR035902; Nuc_phospho_transferase. DR InterPro; IPR036566; PYNP-like_C_sf. DR InterPro; IPR013102; PYNP_C. DR InterPro; IPR013466; Thymidine/AMP_Pase. DR InterPro; IPR000053; Thymidine/pyrmidine_PPase. DR NCBIfam; TIGR03327; AMP_phos; 1. DR NCBIfam; TIGR02645; ARCH_P_rylase; 1. DR PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1. DR PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR Pfam; PF07831; PYNP_C; 1. DR PIRSF; PIRSF000478; TP_PyNP; 1. DR SMART; SM00941; PYNP_C; 1. DR SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1. DR SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1. DR SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Reference proteome; Transferase. FT CHAIN 1..503 FT /note="AMP phosphorylase" FT /id="PRO_0000314733" FT ACT_SITE 256 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132" FT BINDING 168 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132" FT BINDING 194..199 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132" FT BINDING 203 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132" FT BINDING 264 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132" FT BINDING 288 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132" SQ SEQUENCE 503 AA; 54495 MW; FA8144704978BBBC CRC64; MKLRAQPYDI EVGRYEVIIN SADAEELGVL AGDRVQVKDK DTITAVVETT DAIVSPGKIG IYREAWESIK VVPDEVVEVL PAAKPKSVSF IRKKMDKQKL TSEEMHAIIE DIVDGNLTEV ELTAFVTASY IYTMDSDEIE WMTRAMVKTG DQISFDVHPV MDHHSIGGVP GNKISLCIVP IIAAAGLLIP KTSSRAITGA GGSADLMEIL CPVSFRADEI KKMTTKVGGC LVWGGATNIA PADDKIINVE YPLSIDPKSQ LLASVMAKKF AVGADTMVLD IPCGNETKIP TVQEGRKLAR DFMELGDRLG MKIECALTYG GTPLGRAIGG GVEVREAMVM LEKFEGPRSL LEKTIAISGM MLEMGGVAPK NEGAKMAVEL VKSGKALQKF KEIIEVQGGD PKVTSDMVPI GDKVATVLSP QDGYVLEISN KRLVYMCRLA GAPHDKGVGV ILHKKKGEYV KKGDGLFTLY ADKEWKLDAA IKESLRNPIM MVEGMILEKI EVV //