ID   AMPPA_METJA             Reviewed;         503 AA.
AC   Q58081;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 144.
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=MJ0667;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB98662.1; -; Genomic_DNA.
DR   PIR; C64383; C64383.
DR   RefSeq; WP_010870172.1; NC_000909.1.
DR   AlphaFoldDB; Q58081; -.
DR   SMR; Q58081; -.
DR   STRING; 243232.MJ_0667; -.
DR   PaxDb; 243232-MJ_0667; -.
DR   EnsemblBacteria; AAB98662; AAB98662; MJ_0667.
DR   GeneID; 1451533; -.
DR   KEGG; mja:MJ_0667; -.
DR   eggNOG; arCOG02013; Archaea.
DR   HOGENOM; CLU_025040_6_0_2; -.
DR   InParanoid; Q58081; -.
DR   OrthoDB; 9827at2157; -.
DR   PhylomeDB; Q58081; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..503
FT                   /note="AMP phosphorylase"
FT                   /id="PRO_0000059088"
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;  54722 MW;  EFBB97D4A9ADEE18 CRC64;
     MLFLKVRVLD IDLENLVLIN SEDLKSSQYF PQDRVVVEFK GKEVIGILHS STTLINRGEI
     GLPQKVVKEL GVKEGDIVTI KHAEKPKSLP YIRKKMDGNK LKKEEIFEII DEMVDGKLTN
     IEISAFVTSL YINGMDMDEI EAMTIRMAET GEMVNWEGHI FDVHSIGGVP GNKYALLVVP
     IVASAGLKIP KTSSRAITSA AGTADVVEVL TRVDLTIEEI KRVVKETNGC MVWGGALDLA
     PADDITINVE RPLGIDPEPL LLSSVMAKKL AMGVNKLLID IPTGYGAKVK SIKEASSLAR
     KFIELSDRLR IVTECAITYG GQPIGRAIGP ALEAKEALLA LEDYTQAPTS LVEKSISLAG
     ILLEMGGVAP TGEGKELAED LLARGKAHDK FMEIIVAQGG KEVSSDEIEV GKYKADIHSP
     IDGYVTRISN AGITKIAKEA GAPNDKKAGI YLNVKVGNKV EKGDVLYTIY SDSEERLKSA
     IKLARILYPI KVEGMLLQKI SRF
//