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Database: UniProt
Entry: A0A1X6YNZ6_9RHOB
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ID   A0A1X6YNZ6_9RHOB        Unreviewed;       491 AA.
AC   A0A1X6YNZ6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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:SLN27141.1};
GN   ORFNames=CLV79_101126 {ECO:0000313|EMBL:PSK88291.1}, LOS8367_00960
GN   {ECO:0000313|EMBL:SLN27141.1};
OS   Limimaricola soesokkakensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Limimaricola.
OX   NCBI_TaxID=1343159 {ECO:0000313|EMBL:SLN27141.1, ECO:0000313|Proteomes:UP000193495};
RN   [1] {ECO:0000313|EMBL:SLN27141.1, ECO:0000313|Proteomes:UP000193495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8367 {ECO:0000313|EMBL:SLN27141.1,
RC   ECO:0000313|Proteomes:UP000193495};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSK88291.1, ECO:0000313|Proteomes:UP000240624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29956 {ECO:0000313|EMBL:PSK88291.1,
RC   ECO:0000313|Proteomes:UP000240624};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) 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; PYGB01000001; PSK88291.1; -; Genomic_DNA.
DR   EMBL; FWFY01000002; SLN27141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6YNZ6; -.
DR   OrthoDB; 7945729at2; -.
DR   Proteomes; UP000193495; Unassembled WGS sequence.
DR   Proteomes; UP000240624; 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:SLN27141.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01932, ECO:0000313|EMBL:SLN27141.1}.
FT   DOMAIN          23..172
FT                   /note="AMP nucleoside phosphorylase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10423"
FT   DOMAIN          268..438
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   491 AA;  54875 MW;  8ACE40674B1768BB CRC64;
     MERTLKIQTP PSPAAEAFTD PEAALARLKE IYETASRFLC ERFTETLRGG VPETRFRAFY
     PEIRFSTATF AQADSRLSFG HVAEPGTYAT TVTRPELFGN YLMQQMRLLI ENHGVPVVIG
     ASETPMPVHF AVANDASVTV PQDGAMDFHL RDVFDVPDLS TTHDDIVNGN GFTYPDGARP
     LSPFTAQRID YSLARLAHYT ATDPTHFQNH VLFTNYQFYV EEFEAYARHV LADPESGYTS
     FVGPNNQVIR DPEGAMHIPA KMPQMPTYHL KRANGQGITL VNIGVGPSNA KTATDHIAVL
     RPHAWLMVGH CAGLRNSQRL GDFVLAHGYL REDHVLDDDL PVWVPIPALA EIQIALEDAV
     AQVTALEGYE LKRIMRTGTV ATIDNRNWEL RDQSGPVQRL SQSRAVALDM ESATIAANGF
     RFRVPYGTLL CVSDKPLHGE LKLPGMASDF YKTQVARHLM IGIRAMERLR EMPLERIHSR
     KLRSFEETAF L
//
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