ID A0A1I5L5V3_9RHOB Unreviewed; 494 AA.
AC A0A1I5L5V3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ORFNames=SAMN04488047_101462 {ECO:0000313|EMBL:SFO92236.1};
OS Tranquillimonas alkanivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tranquillimonas.
OX NCBI_TaxID=441119 {ECO:0000313|EMBL:SFO92236.1, ECO:0000313|Proteomes:UP000199356};
RN [1] {ECO:0000313|EMBL:SFO92236.1, ECO:0000313|Proteomes:UP000199356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19547 {ECO:0000313|EMBL:SFO92236.1,
RC ECO:0000313|Proteomes:UP000199356};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOXA01000001; SFO92236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5L5V3; -.
DR STRING; 441119.SAMN04488047_101462; -.
DR OrthoDB; 7945729at2; -.
DR Proteomes; UP000199356; Unassembled WGS sequence.
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:UP000199356}.
FT DOMAIN 27..175
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 271..441
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 494 AA; 55288 MW; C6F0882078275822 CRC64;
MNAPHRNLPV VTPPMPEPQA FTDAASAVER LCDLYDAASD FLCRKFSDAV QNGRPDARYR
AFYPEIRFST STYAATDSRL SFGHVPEPGT YSTTITRPDL FRKYLEQQIG LLMENHRVPV
TIGPSHTPMP VHFAVANDDR VTVPQEGVMD FTLRDVFDVP DLSTTHDDIV NGFGFAFEDG
SHPLAPFTAQ RIDYSLARLA HYTATAPEHF QNHVLFTNYQ FYIEEFDVFA RAALADKNSG
YTGFVGPGNV EITDPDGEMP VPQKLPQMPT YHLKRKDGGG ITLVNIGVGP SNAKTATDHI
AVLRPHAWLM VGHCAGLRNS QRLGDFVLAH GYLREDHVLD DDLPVWVPIP ALAEIQIALE
EAVERVTELE GYELKRIMRT GTVATIDNRN WELRDQSGPV QRLSQSRAIA LDMESATIAA
NGFRFRVPYG TLLCVSDKPL HGELKLPGMA SEFYRTQVAR HLLIGVRAME TLRDMPLERI
HSRKLRSFEE TAFL
//
