AMPP2_ARCFU
ID AMPP2_ARCFU Reviewed; 505 AA.
AC O28927;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=AMP phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_02132};
DE Short=AMPpase 2 {ECO:0000255|HAMAP-Rule:MF_02132};
DE EC=2.4.2.57 {ECO:0000255|HAMAP-Rule:MF_02132};
DE AltName: Full=Nucleoside monophosphate phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_02132};
DE Short=NMP phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_02132};
GN OrderedLocusNames=AF_1342;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB89902.1; -; Genomic_DNA.
DR PIR; E69417; E69417.
DR RefSeq; WP_010878839.1; NC_000917.1.
DR AlphaFoldDB; O28927; -.
DR SMR; O28927; -.
DR STRING; 224325.AF_1342; -.
DR EnsemblBacteria; AAB89902; AAB89902; AF_1342.
DR GeneID; 24794954; -.
DR KEGG; afu:AF_1342; -.
DR eggNOG; arCOG02013; Archaea.
DR HOGENOM; CLU_025040_6_0_2; -.
DR OMA; QMVASIM; -.
DR OrthoDB; 43931at2157; -.
DR PhylomeDB; O28927; -.
DR Proteomes; UP000002199; 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..505
FT /note="AMP phosphorylase 2"
FT /id="PRO_0000059086"
FT BINDING 169
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT BINDING 195..200
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT BINDING 204
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT BINDING 265
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
FT BINDING 289
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02132"
SQ SEQUENCE 505 AA; 54693 MW; A6FE00548E132F39 CRC64;
MKFRIKTLPL RTERIAVVLS QDDAAELGLL PGDRVKVSYD GKSFVAEVEI SQEFISSGEA
GVCTFTAETC SLSEECVVEI VPFARPKSVE YIRKKLNGAK YEREEIKDII GSISSDVLSD
IEISAFILAN EIVGMQNDEI QWMIEAMVEV GERVVFERGT VVDMHSIGGL PGNRFSLIAV
PTVAAAGLLI PKTASRAITT ASGTADTMEV LANVNLSVDE IKEITEEVGG VIAWNAPTGI
APADEKIIRV EYQLELSPKP HLMASVLSKK LGSGARFVAI DIPVGKKAKV ENVDVGRGFA
NAMMEIGRNL NLKVATALTD GSQPLGRAIG PALEAREVLE VMERKVEGDL LEKSLGIAGI
LFEMTGIATN GYQHARKIFE SGKTLEKFRE IVAAQGGDES VKAEDVAVGD KTYTLHAAKE
GYVREIDIAA LNEIARTAGA PKDKGAGVYV HKKRGEVVKV GDPLLTIYAE KEWKLDNAIE
VANTKQAFEI SGVIIERYTM GRWWS
