ID A0A483CQ79_9EURY Unreviewed; 514 AA.
AC A0A483CQ79;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=AMP phosphorylase {ECO:0000256|HAMAP-Rule:MF_02132};
DE Short=AMPpase {ECO:0000256|HAMAP-Rule:MF_02132};
DE EC=2.4.2.57 {ECO:0000256|HAMAP-Rule:MF_02132};
DE AltName: Full=Nucleoside monophosphate phosphorylase {ECO:0000256|HAMAP-Rule:MF_02132};
DE Short=NMP phosphorylase {ECO:0000256|HAMAP-Rule:MF_02132};
GN ORFNames=CUJ86_00610 {ECO:0000313|EMBL:TAJ45285.1};
OS Methanofollis fontis.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanomicrobiales; Methanomicrobiaceae; Methanofollis.
OX NCBI_TaxID=2052832 {ECO:0000313|EMBL:TAJ45285.1, ECO:0000313|Proteomes:UP000292580};
RN [1] {ECO:0000313|EMBL:TAJ45285.1, ECO:0000313|Proteomes:UP000292580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FWC-SCC2 {ECO:0000313|EMBL:TAJ45285.1,
RC ECO:0000313|Proteomes:UP000292580};
RA Teng N.-H., Lai M.-C., Chen S.-C.;
RT "Isolation and Characterization of Methanofollis Species from Methane Seep
RT Offshore SW Taiwan.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_02132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + phosphate = alpha-D-ribose 1,5-bisphosphate + adenine;
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:0000256|HAMAP-Rule:MF_02132};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP + phosphate = cytosine + alpha-D-ribose 1,5-bisphosphate;
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:0000256|HAMAP-Rule:MF_02132};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UMP + phosphate = 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:0000256|HAMAP-Rule:MF_02132};
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. Type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02132}.
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:TAJ45285.1}.
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DR EMBL; PGCL01000001; TAJ45285.1; -; Genomic_DNA.
DR RefSeq; WP_130645631.1; NZ_PGCL01000001.1.
DR AlphaFoldDB; A0A483CQ79; -.
DR OrthoDB; 9827at2157; -.
DR Proteomes; UP000292580; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; IPR017872; Pyrmidine_PPase_CS.
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 NCBIfam; NF003338; PRK04350.1; 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 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.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_02132}; Reference proteome {ECO:0000313|Proteomes:UP000292580};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02132}.
FT DOMAIN 425..492
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 169
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 195..200
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 204
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 265
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 289
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
SQ SEQUENCE 514 AA; 55357 MW; 8392BFBCC56D29B1 CRC64;
MKLTTRLIDI EHRGVLLHSA DAREISVRGG DRVEVKNRVT GESISAFVDT TASLIDPGVI
GVYRPTQVQI DVLEAAEVEV RAADRPTTLD YIKKKMDGGR LTKDETYAII KDVVADVLSP
SELTAYIIST YINPLDMDEV EYLTRAMVDT GERLHFPSYP IVDKHSIGGV PGNKITLLIV
PIVAAAGLKI PKTSSRAITG AGGTADLMEV LAPVEFSAAE VQQMTERVGA VIVWGGATNI
APADDRFITI EYPFKIDARG QMLASVMAKK FAVGANVVAI DIPVGEHTKV PTIEEGRKLA
REFIELGERL GMRVECALTY GESLVGHTIG PRLEVREALS VLEGANEPNS LIQKSLSIAG
IILEMSGKAA PGEGYRVAGE ILESGRAYEK MRQIIEVQGG DPDVKAADIL PGQFSYVVKA
PGNGYVIELN NRALISIARA AGAPQDAGAG IFIHAKKGTQ VEAGEPIFTV YADRQWRLQK
ALEEGRRLMP IVVEGMLLDR LPGRHWGGGG SYGE
//
