ID   A3V2K2_9RHOB            Unreviewed;       493 AA.
AC   A3V2K2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=SKA53_12138 {ECO:0000313|EMBL:EAQ07583.1};
OS   Yoonia vestfoldensis SKA53.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Yoonia.
OX   NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ07583.1, ECO:0000313|Proteomes:UP000004507};
RN   [1] {ECO:0000313|EMBL:EAQ07583.1, ECO:0000313|Proteomes:UP000004507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA53 {ECO:0000313|EMBL:EAQ07583.1,
RC   ECO:0000313|Proteomes:UP000004507};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (JAN-2006) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAQ07583.1}.
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DR   EMBL; AAMS01000002; EAQ07583.1; -; Genomic_DNA.
DR   RefSeq; WP_007206369.1; NZ_CH672414.1.
DR   AlphaFoldDB; A3V2K2; -.
DR   STRING; 314232.SKA53_12138; -.
DR   eggNOG; COG0775; Bacteria.
DR   HOGENOM; CLU_026838_1_0_5; -.
DR   OrthoDB; 7945729at2; -.
DR   Proteomes; UP000004507; 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   Glycosidase {ECO:0000313|EMBL:EAQ07583.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01932, ECO:0000313|EMBL:EAQ07583.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004507}.
FT   DOMAIN          26..174
FT                   /note="AMP nucleoside phosphorylase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10423"
FT   DOMAIN          276..440
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   493 AA;  54528 MW;  E80C3305ED497E1B CRC64;
     MNAPQKVVIR TPDLPPHEAF TDPKKAVVRL NELYAASVRF LSENFVAALR DGQPDGRFRA
     FYPEIRLTTT THAKMDSRLS FGHVAEPGIY ATTVTRPDLF QSYLEQQIDL LLKSHGVPVV
     IGTSDTVIPV HFAVANDAGV TVPQDGSMEF NLRDNFDVPD LSTTHDAIVN GAGFTYPDGA
     RPLAPFTAQR IDYSLARLSH YTATAPEHFQ NHVLFTNYQF YVEEFEAFAR KMLADPASGY
     TSFVSTGNVE ITAHDGPLPV PAKLPQMPTY HLKRPGGAGI TLVNIGVGPS NAKTATDHIA
     VLRPHAWLMV GHCAGLRNSQ RLGDFVLAHA YLREDHVLDD DLPVWVPIPA LAEIQIALQT
     AVADVTQLEG YDLKQIMRTG TVATIDNRNW ELREQAGPVQ RLSQSRAIAL DMESATIAAN
     GFRFRVPYGT LLCVSDKPLH GELKLPGMAS EFYKTQVAAH LMIGIRAMEL LREMPLERIH
     SRKLRSFEET AFL
//