ID   AMPPA_METMP             Reviewed;         505 AA.
AC   Q6M0E4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=MMP0327;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF29883.1; -; Genomic_DNA.
DR   RefSeq; WP_011170271.1; NC_005791.1.
DR   AlphaFoldDB; Q6M0E4; -.
DR   SMR; Q6M0E4; -.
DR   STRING; 267377.MMP0327; -.
DR   PRIDE; Q6M0E4; -.
DR   EnsemblBacteria; CAF29883; CAF29883; MMP0327.
DR   GeneID; 2761854; -.
DR   KEGG; mmp:MMP0327; -.
DR   PATRIC; fig|267377.15.peg.330; -.
DR   eggNOG; arCOG02013; Archaea.
DR   HOGENOM; CLU_025040_6_0_2; -.
DR   OMA; DVWRRMI; -.
DR   OrthoDB; 43931at2157; -.
DR   BioCyc; MMAR267377:MMP_RS01745-MON; -.
DR   Proteomes; UP000000590; 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; 3.40.1030.10; -; 1.
DR   Gene3D; 3.90.1170.30; -; 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   PANTHER; PTHR10515; PTHR10515; 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; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   SUPFAM; SSF54680; SSF54680; 1.
DR   TIGRFAMs; TIGR03327; AMP_phos; 1.
DR   TIGRFAMs; TIGR02645; ARCH_P_rylase; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..505
FT                   /note="AMP phosphorylase"
FT                   /id="PRO_0000314722"
FT   ACT_SITE        258
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT   BINDING         170
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT   BINDING         196..201
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT   BINDING         205
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT   BINDING         266
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT   BINDING         290
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
SQ   SEQUENCE   505 AA;  54597 MW;  466AEE8D187F9B8C CRC64;
     MLFLNAKFID LDLGENAVIV NEDDLKGTSY YPQDRVLIES HAGSVIGNIY STKTMVQKGE
     VGMLVSELAE ISISEGEEVK LRHAEKPESI PFIKKKMDGQ VLNPHEIRTI IDEIVSKKLS
     NIELSAFVSS TYINGMNMDE IGEMTKRIAE TGDMISWEKN LVVDIHSIGG VPGNKYALLS
     IPILAAAGIT IPKTSSRAIT SPAGTADVME VLTNVELKED EIKRIVKTTN GCLVWGGGVN
     LAPADDIIIN VERPVSIDPQ PQLLASVMAK KIATGIKYSV IDIPVGKGVK IKNEAEGAKL
     ARKFIELGEL LNIKVECVLT YGGQPLGRAI GPALEAKEAI EALQDPKNAP KSLIEKALSL
     AGILLELGGA AQIGEGQNLA WEILESGRAL EKFNQIIIEQ GGTPKKPEEI ELGDYIEEII
     APIDGYVTDI NNTGITNVVK EAGAPRDKKA GLLLNSKIGN KVKKGDVLYT IYSGSEERLV
     SAVNLARRVY PVKVEGMLIE RISKF