ID   AMPPA_PYRHO             Reviewed;         503 AA.
AC   O59251;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 135.
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=PH1598;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA30710.1; -; Genomic_DNA.
DR   PIR; F71038; F71038.
DR   RefSeq; WP_010885672.1; NC_000961.1.
DR   AlphaFoldDB; O59251; -.
DR   SMR; O59251; -.
DR   STRING; 70601.gene:9378588; -.
DR   EnsemblBacteria; BAA30710; BAA30710; BAA30710.
DR   GeneID; 1442451; -.
DR   KEGG; pho:PH1598; -.
DR   eggNOG; arCOG02013; Archaea.
DR   OrthoDB; 9827at2157; -.
DR   Proteomes; UP000000752; 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_0000059092"
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;  53977 MW;  7DCE91203C847783 CRC64;
     MRAKVKILKI KTGSFNVFIS PRDAEEWKLH PNDLVKIESG KRSIYASVAI GDFIEDGEVG
     LSQDILSSYQ FSEGEVVSIT PSGTPESVKY IKKKMKGEKL RKVEIETIIR DIVDRKLRNT
     EISAFITAIE INGLSMDEIA ALTIAMAETG DMLDIDRKPI MDVHSIGGVP GNKTNILVVP
     IVAAAGLTIP KTSSRAITSA AGTADVVEVL TNVKLSLDEI KRIVEKIGAC LVWGGALNLA
     PADDLTIHVE RRLSLDPRGL MLASIMSKKY AIGSQYILID IPTGKGAKVE TMDEARTLAK
     DFIELGKKLG QYVEVAITYG GQPIGYAIGP ALEAKEALET LMTGKGPGSL VEKATGLAGI
     LLEMGGVAPK GMGKKVAKEI LESGKAYEKM KEIIEEQGGD PNIKPEDIPI GDKTYTIHAQ
     TGGYVTGIDN RAITAIAREA GAPEDKGAGV RLHVKVGEKV KEGDPLITIH AESESRLEKA
     IVLARRLEPI KIEGMVLQVI GNI
//