ID D5VS65_METIM Unreviewed; 501 AA.
AC D5VS65;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=Metin_0751 {ECO:0000313|EMBL:ADG13418.1};
OS Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG13418.1, ECO:0000313|Proteomes:UP000002061};
RN [1] {ECO:0000313|EMBL:ADG13418.1, ECO:0000313|Proteomes:UP000002061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of Methanocaldococcus infernus ME.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002009; ADG13418.1; -; Genomic_DNA.
DR RefSeq; WP_013100164.1; NC_014122.1.
DR AlphaFoldDB; D5VS65; -.
DR STRING; 573063.Metin_0751; -.
DR GeneID; 9131763; -.
DR KEGG; mif:Metin_0751; -.
DR eggNOG; arCOG02013; Archaea.
DR HOGENOM; CLU_025040_6_0_2; -.
DR OrthoDB; 9827at2157; -.
DR Proteomes; UP000002061; 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; 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 {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_02132};
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 255
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 167
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 193..198
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 202
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 263
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 287
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
SQ SEQUENCE 501 AA; 55045 MW; 4E8FC4940E17BAB7 CRC64;
MLFLKVRLLD IDLLDLVLIN PEDIKASQYF PGDRVVLIYK NKEEIGTIYS STLVNRGEIG
ITKELAKSLK VKEGELITIK HADKPRSLAY IKKKMDKNKL SKEEIFLIVD EMVNNKLTNI
EISAFVTSLY INGMDMDEIE ALTIRMAETG EMVEWESLVF DVHSIGGVPG NKYALLTVPI
VASAGLKIPK TSSRAITSAA GTADVMEVLT RVDLSIEEIK NVVKETNGCL VWGGALNLAP
ADDITINVER PLGIDPKPLL LSSVMAKKLA MGVSKLLIDI PIGREVKVKD EKEGNKLARE
FIELGERLNI TTECALTYGN QPIGRAIGPA LEAKEALETL EDPYKGANSL VDKATHLAGI
LLEMGGIAPA GEGKEVAEEL LFRKAHDKFM DIIVAQGGKE VRSEEIEVGK YFIDIVSPKD
GYVIELSNNK ITKIAKEAGA PNDKKAGVYL NVKVGDKVEK GDLLFTIYSS SEDRLKNAIK
LARTLYPIKV EGILIKRIVR F
//
