ID A0A2I0PSY2_9EURY Unreviewed; 507 AA.
AC A0A2I0PSY2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=CVV30_07270 {ECO:0000313|EMBL:PKL69360.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013817 {ECO:0000313|EMBL:PKL69360.1, ECO:0000313|Proteomes:UP000233367};
RN [1] {ECO:0000313|EMBL:PKL69360.1, ECO:0000313|Proteomes:UP000233367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-1 {ECO:0000313|EMBL:PKL69360.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKL69360.1}.
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DR EMBL; PGYM01000002; PKL69360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0PSY2; -.
DR Proteomes; UP000233367; Unassembled WGS sequence.
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 425..492
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 169
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 195..200
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 204
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 265
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
FT BINDING 289
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02132"
SQ SEQUENCE 507 AA; 54702 MW; 52B483057372CE30 CRC64;
MKFSAKILDI ATRGILLNRA DARSIGVLDG DRVQVINSKN SISSAALVQT TSTIAQQGTV
GIYRITNERL HLEDGDEIEI REARRPASLD FIKKKMDGVR LTKEETLTII KDVVSDDLSA
AELTAFITAS YINPLDMDEV EHLTRAMVET GEQIKFASRP IVDKHSIGGV PGNKISLLVV
PIIAASGLKI PKTSSRAITG AGGTADLMEV LAFVEFSASE VQQMTEKVGG AIVWGGATNI
APADDRIIIQ EYPFKIDARG QMLASVMAKK YAVGANIVVI DIPVGQHTKV ANMAEGRKLA
REFIELGERL NMKVECALTY GDIPVGHSIG PKLEVKEALR VLEGATEPNS FIQKSISLAG
IAFEMSGKAA RGTGAAMAQE ILANGKALEK FRQIIEIQGG DPLVKSEDII PGEHQFVIKA
PVSGYVIEMN NRSLVTLART AGAPQDRGAG ILLHAKKGKL VKAGEPLFTL FAERNWRLQN
AIEEGRRLMP VLVEGMLLDR VPSISEI
//
