ID   AMPPA_PYRAB             Reviewed;         503 AA.
AC   Q9V163; G8ZJ29;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   27-MAR-2024, entry version 128.
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   Name=deoA; OrderedLocusNames=PYRAB05650; ORFNames=PAB1982;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAB49487.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ248284; CAB49487.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE69956.1; -; Genomic_DNA.
DR   PIR; H75175; H75175.
DR   RefSeq; WP_048146577.1; NC_000868.1.
DR   AlphaFoldDB; Q9V163; -.
DR   SMR; Q9V163; -.
DR   STRING; 272844.PAB1982; -.
DR   GeneID; 1495469; -.
DR   KEGG; pab:PAB1982; -.
DR   PATRIC; fig|272844.11.peg.602; -.
DR   eggNOG; arCOG02013; Archaea.
DR   HOGENOM; CLU_025040_6_0_2; -.
DR   OrthoDB; 9827at2157; -.
DR   PhylomeDB; Q9V163; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; IPR009010; Asp_de-COase-like_dom_sf.
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; SSF50692; ADC-like; 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_0000059090"
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;  54198 MW;  BDD7A239E1777362 CRC64;
     MRAKVRILNI RSGHFDVFIN PKDAQEWKLH PNDLVKIESG KRSIYGSVVI GDFVESGEVG
     LSLDILDAYQ FSEGELVSIT PSETPESVRY IKKKMRGEKL RKVEIETIVR DIVDRKLRNT
     EISALVTAIE VNGLDMDEIA ALTIAMAETG DMLDIDRKPI MDVHSIGGVP GNKTNIIVVP
     IVAAAGLTIP KTSSRAITSA AGTADVVEVF TNVTLSLDEI KRIVEKIGAC LVWGGALNLA
     PADDLTIHVE RRLSLDPRGL MLASIMSKKY AIGSQYILID IPTGKGAKVE TMEEARSLAK
     DFIELGKKLG QYVEVAITYG GQPIGYTVGP ALEAKEALET LMTGKGPGSL VEKALGLAGI
     LLEMGGVAPR GMGKKVAREI LESGKAYEKI KEIIEEQGGD PNIKPEDIPI GDKTYTIHAQ
     TSGYVTGIDN KAITAIAREA GAPEDKGAGV KLHVKVGEKV KEGDPLFTIH AESESRLDKA
     IILARRLEPI KIEGMVLQVL GNL
//