ID D8MU89_ERWBE Unreviewed; 486 AA.
AC D8MU89;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=AMP nucleosidase {ECO:0000256|HAMAP-Rule:MF_01932};
DE EC=3.2.2.4 {ECO:0000256|HAMAP-Rule:MF_01932};
GN Name=amn {ECO:0000256|HAMAP-Rule:MF_01932,
GN ECO:0000313|EMBL:CAX60396.1};
GN OrderedLocusNames=EbC_28650 {ECO:0000313|EMBL:CAX60396.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|EMBL:CAX60396.1, ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX60396.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60396.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond of AMP to
CC form adenine and ribose 5-phosphate. Involved in regulation of AMP
CC concentrations. {ECO:0000256|HAMAP-Rule:MF_01932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H2O = adenine + D-ribose 5-phosphate;
CC Xref=Rhea:RHEA:20129, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.2.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01932};
CC -!- SIMILARITY: Belongs to the AMP nucleosidase family. {ECO:0000256|HAMAP-
CC Rule:MF_01932}.
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DR EMBL; FP236843; CAX60396.1; -; Genomic_DNA.
DR RefSeq; WP_013202881.1; NC_014306.1.
DR AlphaFoldDB; D8MU89; -.
DR STRING; 634500.EbC_28650; -.
DR KEGG; ebi:EbC_28650; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_026838_1_0_6; -.
DR Proteomes; UP000008793; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0008714; F:AMP nucleosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044209; P:AMP salvage; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd17762; AMN; 1.
DR Gene3D; 3.30.1730.10; AMP nucleoside phosphorylase, N-terminal domain; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR HAMAP; MF_01932; AMP_nucleosidase; 1.
DR InterPro; IPR047039; AMN_phosphorylase.
DR InterPro; IPR037109; AMP_N_sf.
DR InterPro; IPR011271; AMP_nucleosidase.
DR InterPro; IPR018953; AMP_nucleoside_Pase_N.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR NCBIfam; TIGR01717; AMP-nucleosdse; 1.
DR PANTHER; PTHR43691:SF6; AMP NUCLEOSIDASE; 1.
DR PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1.
DR Pfam; PF10423; AMNp_N; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01932};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT DOMAIN 14..170
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 271..433
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 486 AA; 53778 MW; 286B8E92A499FB60 CRC64;
MTQPSAPKGL SVAEALDKLD ALYEEAVTAL RTAINTYISS GKLPEESARA NGLFVYPELR
VSWAGDESGH RLTRAFGRFT RPGSYATTVT RPALARHYLS EQLEMLTGEY PVTLEVKPSK
QEIPFPYVID GSNLGLDRTM SAGLAKHFPT TELAQIGDEN ADGLYQPGEE FPLSHFDALR
TDFSLARLRH YTGTPVEHFQ SYVLFTNYTR YVDEFVRWGC EQIADPASPY EALSCAGSIF
VTAETPNPQE AISGLAWKNH QMPAWHLIAK NGQGITLINI GVGPSNAKTI CDHLAVLRPH
TWLMIGHCGG LRESQSIGDY VLAHAYLRDD HVLDAVLPPD IPVPSIAEVQ RALYDATKHV
SGMPGDLVKQ RLRTGTVVTT DDRNWELRYS ASALRFNLSR AVAVDMESAT IAAQGYRFRV
PYGTLLCVSD KPLHGEIKLP GQANRFYEGA ISEHLQIGIC AIDLLRAEGD KLHSRKLRTF
NEPPFR
//
