ID   AMPPA_THEGJ             Reviewed;         503 AA.
AC   C5A1L9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=TGAM_1786;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
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}.
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DR   EMBL; CP001398; ACS34288.1; -; Genomic_DNA.
DR   RefSeq; WP_015859397.1; NC_012804.1.
DR   AlphaFoldDB; C5A1L9; -.
DR   SMR; C5A1L9; -.
DR   STRING; 593117.TGAM_1786; -.
DR   PaxDb; 593117-TGAM_1786; -.
DR   GeneID; 7987613; -.
DR   KEGG; tga:TGAM_1786; -.
DR   PATRIC; fig|593117.10.peg.1794; -.
DR   eggNOG; arCOG02013; Archaea.
DR   HOGENOM; CLU_025040_6_0_2; -.
DR   OrthoDB; 9827at2157; -.
DR   Proteomes; UP000001488; 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; 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   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.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..503
FT                   /note="AMP phosphorylase"
FT                   /id="PRO_1000212643"
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;  53823 MW;  B60C4422EF02B0BF CRC64;
     MRAKVRILDV FSGRYSVFIN EEEAKKAKLH PDDLVKVESG KKTIYGSLAI SNLVGPGEVG
     VSRDVLQLHS LSEGEVVTLT PVGTPESVRY IKKKMHGEKL RKVEIEAIVR DIVDRKLRDI
     EISSFVTALE INGLDMDEIA ALTIAMAETG DMLDIDRKPI MDVHSIGGVP GNKTNILVVP
     IVAAAGLTIP KTSSRAITSA AGTADVVEVF TNVSFSLDEI KRIVEKVGAC LVWGGALNLA
     PADDITIKAE RALSVDPRGL MLASIMSKKY AMGSQYVLID IPTGKGVKVE TMDEARALAR
     DFIELGKRLG QYVEVAITYG GQPIGHTVGP ALEAREALSA LMTGKGPGSL IEKALGLAGI
     LLEMGGVAPA GMGKKMAREI LESGKAYEKM KEIIEEQGGD PNIKPEDIQI GDKTYTFTAP
     TSGYVTGIDN RAITGIARAA GAPEDKGAGL ELYVKVGEKV KEGDPLFTIH AESEARLDQA
     IVFARRTEPI KIEGMVLQRI GNI
//