ID A0A1D7NMR0_9SPHN Unreviewed; 478 AA.
AC A0A1D7NMR0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=BG023_112154 {ECO:0000313|EMBL:AOL95070.1};
OS Porphyrobacter sp. LM 6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=1896196 {ECO:0000313|EMBL:AOL95070.1, ECO:0000313|Proteomes:UP000094080};
RN [1] {ECO:0000313|EMBL:AOL95070.1, ECO:0000313|Proteomes:UP000094080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM 6 {ECO:0000313|EMBL:AOL95070.1,
RC ECO:0000313|Proteomes:UP000094080};
RA Hentchel K., Vargas G., Fiebig A., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (AUG-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; CP017113; AOL95070.1; -; Genomic_DNA.
DR RefSeq; WP_069310431.1; NZ_CP017113.1.
DR AlphaFoldDB; A0A1D7NMR0; -.
DR STRING; 1896196.BG023_112154; -.
DR KEGG; porl:BG023_112154; -.
DR PATRIC; fig|1896196.3.peg.2133; -.
DR OrthoDB; 7945729at2; -.
DR Proteomes; UP000094080; Chromosome.
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}.
FT DOMAIN 7..157
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 244..427
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 478 AA; 53129 MW; F28C1689C3D542B5 CRC64;
MIDIPSILEQ LQHHYDAAVR TLRDDVIAFG RDGTLPPQSR REDGSYAYPQ ITIRYAGVGA
PRDRSRAFGR LEMPGTYSTT VTRPDLFTKY LTEQLQLIAT EYEVDITVER SRQEIPFPYV
LDGEAGAAMV GTAPQDIATH FPSTDLALIG DELADGIEFD GLADMPLSLF DGLRTDYSLA
RLKHYTGSEV SDFQDFILFT NYHRYVDEFV NWGATQIGKD GYVALTGAAG LDIRTATTNA
QSQLNDTAWR KHQMPAYHLI REDGRGITLV NIGVGPSNAK TICDHLAVLR PHAWLMIGHC
GGLRSTQKIG DFVLAHAYLR DDHVLDVVLP PEVPIPPIAE VQQAMAYAAE KVAGVQGANL
KQRMRTGTVV TTDDRNWELR YSSSAKRFSQ SRAIAIDMES ATIATQGYRF RVPYGTLLCV
SDKPLHGEIK LPGQANKFYE EAIAAHLQMG IVACAMLRDE GDRLHSRKLR AFNEPPFR
//
