ID A0A0H3FUQ2_KLEAK Unreviewed; 484 AA.
AC A0A0H3FUQ2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 OrderedLocusNames=EAE_23205 {ECO:0000313|EMBL:AEG99540.1};
OS Klebsiella aerogenes (strain ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235
OS / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56)
OS (Enterobacter aerogenes).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1028307 {ECO:0000313|EMBL:AEG99540.1, ECO:0000313|Proteomes:UP000008881};
RN [1] {ECO:0000313|Proteomes:UP000008881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 /
RC NCIMB 10102 / NCTC 10006 {ECO:0000313|Proteomes:UP000008881};
RA Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.;
RT "Complete sequence of Enterobacter aerogenes KCTC 2190.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG99540.1, ECO:0000313|Proteomes:UP000008881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 /
RC NCIMB 10102 / NCTC 10006 {ECO:0000313|Proteomes:UP000008881};
RX PubMed=22493190; DOI=10.1128/JB.00028-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Enterobacter aerogenes KCTC 2190.";
RL J. Bacteriol. 194:2373-2374(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002824; AEG99540.1; -; Genomic_DNA.
DR RefSeq; WP_015365878.1; NC_015663.1.
DR RefSeq; YP_004594819.1; NC_015663.1.
DR AlphaFoldDB; A0A0H3FUQ2; -.
DR GeneID; 66603143; -.
DR KEGG; eae:EAE_23205; -.
DR PATRIC; fig|1028307.3.peg.4597; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_026838_1_0_6; -.
DR OrthoDB; 7945729at2; -.
DR Proteomes; UP000008881; 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 Glycosidase {ECO:0000313|EMBL:AEG99540.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01932, ECO:0000313|EMBL:AEG99540.1}.
FT DOMAIN 12..167
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 269..432
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 484 AA; 54239 MW; EE998F39E274B02C CRC64;
MNQKAVSLTP EQALSQLEAQ YERAVNALRK AIGEYIHHNI LPDEIARAEG LFVYPQLSVS
WDGAEHKALK TRAWGRFTHA GCYTTTITNP KLFRAYLLEQ LTLLYQDYGA HISVGNSQHE
IPFPYVIDGS ALTLDRSMSA GLTRYFPTTE LSQIGDETAD GLFHATEYYP LSHFDARRVD
FSLARLKHYT GTPVEHFQPY VLFTNYTRYV DEFVSWGCSQ ILDPDSPYIA LSCAGGIWIT
ADTEAPEEAI SDLAWKKHQM PAWHLITNDG QGITLINIGV GPANAKNICD HLAVLRPDVW
LMIGHCGGLR ESQSIGDYVL AHAYLRDDHV LDAVLPPDIP IPSIAEVQRA LYDATKQVSG
MPGEEVKQRL RTGTVVTTDD RNWELRYSAS ALRFNLSRAV AIDMESATIA AQGYRFRVPY
GTLLCVSDKP LHGEIKLPGQ ANRFYEGAIS EHLQIGIRAI DLLRAEGDHM HSRKLRTFNE
PPFR
//
