AMPPA_THEPD
ID AMPPA_THEPD Reviewed; 511 AA.
AC A1RWC3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
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=Tpen_0093;
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5;
RX PubMed=18263724; DOI=10.1128/jb.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABL77503.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000505; ABL77503.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A1RWC3; -.
DR SMR; A1RWC3; -.
DR STRING; 368408.Tpen_0093; -.
DR PRIDE; A1RWC3; -.
DR EnsemblBacteria; ABL77503; ABL77503; Tpen_0093.
DR KEGG; tpe:Tpen_0093; -.
DR eggNOG; arCOG02013; Archaea.
DR HOGENOM; CLU_025040_6_0_2; -.
DR Proteomes; UP000000641; 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 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..511
FT /note="AMP phosphorylase"
FT /id="PRO_0000314732"
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 262
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT BINDING 286
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
SQ SEQUENCE 511 AA; 55569 MW; C655AF7EA9714244 CRC64;
MKLKTRILPF ESAHYTVVLD QSVAKKLDVR PSDRVLVRFN GKTVVAIANI AKEFSHEHVG
VYVNIAKALG ISDGDEVEVE ATSPPASLQA IRKKLQGLSL ESDEIYQVVK DIVDGKLSEL
ELAAFVTAVH FQGMTPSEIY SFTLSMVETG QRLRLKRKPI LDKHSLGGVP GDKTSLLVVP
IIASLGFTIP KTSSRAITSA AGTADRMEVL APVNLSIDEI ERIVEKTNAC LVWGGALNLA
PADDIIIRVE YPLGIDPFYI PSILAKKLAV GSTHVVLDVP TGRGTKVKTL EEAKRISQSF
FEIARMFGMN LQAVATYAEE PIGHAIGPAL EAREALIALR ELRPGDLVDK AASLAGTLLE
MVGVENGYET AMEALRTGKA EKKLREIIEA QGGDPDVTPE EIPLGDKTYT LYSEEDGFVY
YIDNSLLANI GKIAGAPIDK GAGVYIHVKL GEKVRKGDPL LTVYSSSSAK LQAVERILED
SKPVLVGRTA GRRMLLERIQ YQPPRQLVLE R
