ID F4BX26_METSG Unreviewed; 504 AA.
AC F4BX26;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=AMP phosphorylase {ECO:0000256|HAMAP-Rule:MF_02132};
DE Short=AMPpase {ECO:0000256|HAMAP-Rule:MF_02132};
DE EC=2.4.2.57 {ECO:0000256|HAMAP-Rule:MF_02132};
DE AltName: Full=Nucleoside monophosphate phosphorylase {ECO:0000256|HAMAP-Rule:MF_02132};
DE Short=NMP phosphorylase {ECO:0000256|HAMAP-Rule:MF_02132};
GN OrderedLocusNames=MCON_0583 {ECO:0000313|EMBL:AEB67416.1};
OS Methanothrix soehngenii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC
OS 103675 / OCM 69 / GP-6) (Methanosaeta concilii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=990316 {ECO:0000313|EMBL:AEB67416.1, ECO:0000313|Proteomes:UP000007807};
RN [1] {ECO:0000313|EMBL:AEB67416.1, ECO:0000313|Proteomes:UP000007807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6
RC {ECO:0000313|Proteomes:UP000007807};
RX PubMed=21571998; DOI=10.1128/JB.05031-11;
RA Barber R.D., Zhang L., Harnack M., Olson M.V., Kaul R., Ingram-Smith C.,
RA Smith K.S.;
RT "Complete genome sequence of Methanosaeta concilii, a specialist in
RT aceticlastic methanogenesis.";
RL J. Bacteriol. 193:3668-3669(2011).
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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_02132};
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. Type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02132}.
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DR EMBL; CP002565; AEB67416.1; -; Genomic_DNA.
DR RefSeq; WP_013718478.1; NC_015416.1.
DR AlphaFoldDB; F4BX26; -.
DR STRING; 990316.MCON_0583; -.
DR GeneID; 10460319; -.
DR KEGG; mcj:MCON_0583; -.
DR HOGENOM; CLU_025040_6_0_2; -.
DR InParanoid; F4BX26; -.
DR OrthoDB; 9827at2157; -.
DR Proteomes; UP000007807; 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 {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_02132}; Reference proteome {ECO:0000313|Proteomes:UP000007807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02132}.
FT DOMAIN 422..489
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
FT ACT_SITE 254
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 166
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 192..197
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 201
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 262
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 286
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
SQ SEQUENCE 504 AA; 53648 MW; AEFBAB46D32B7ADF CRC64;
MLLVRPFDIE IGQHKVMLNI VDARERGLNP GDRVRVRAKG AATTALLDTT TQMVKPGEIG
IFTEALKDLN NPVDVDILPA PRPASICHIK SLMDNEKLSE DQIRTIVQDI VDNNLSDIEL
AAYVTASYIH NMPSEEVVWL TKAMIETGER IHFDTHPVMD KHSIGGVPGN KVSLLIVPIV
AAAGLLIPKT SSRAITGAGG TADLMEVLAP VEFSAAEIKE ITEKVGGVIV WGGATNIAPA
DDKLIKAEYA LSIDPYSQML ASIMAKKGAV GADAVVVDMP VGPGTKLPTA DDGRTLAKDL
IDLGDKLGIR VECAMTFGGS PVGRTIGPAL EVREALTLLE NKPGPNSLRE KSLSLAGILL
EMGGVAGRGE GYAAAEEILS SGKAHAKLME IIAAQGGNPN VKSEDIVIGE NCEEILAPAG
GYVVAFYNKR LVELARMAGA PSDQKAGVII HKKMGERVKK GEPLITICSS SDWELDSAVR
DAKRSMPIVV EGMLLERYPR ITEL
//
