ID A0A1M5MBQ3_9RHOB Unreviewed; 494 AA.
AC A0A1M5MBQ3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN05443551_0459 {ECO:0000313|EMBL:SHG74641.1};
OS Marivita hallyeonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Marivita.
OX NCBI_TaxID=996342 {ECO:0000313|EMBL:SHG74641.1, ECO:0000313|Proteomes:UP000184221};
RN [1] {ECO:0000313|EMBL:SHG74641.1, ECO:0000313|Proteomes:UP000184221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29431 {ECO:0000313|EMBL:SHG74641.1,
RC ECO:0000313|Proteomes:UP000184221};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQXC01000001; SHG74641.1; -; Genomic_DNA.
DR RefSeq; WP_072775898.1; NZ_FQXC01000001.1.
DR AlphaFoldDB; A0A1M5MBQ3; -.
DR STRING; 996342.SAMN05443551_0459; -.
DR OrthoDB; 7945729at2; -.
DR Proteomes; UP000184221; 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:UP000184221}.
FT DOMAIN 26..179
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 277..441
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 494 AA; 54875 MW; 60C84F5E7A7112F5 CRC64;
MQDRVNSLEL LTPTAPAPEM FDDAKAAVNR LCDLYDISTR FLCNSFQTAM EQGHPGVRYR
AYYPEVRITT TTFAKVDSRL SFGHVAHPGT HAATITRPDL FRHYLEQQLS LLLENHGVPV
QIGMSDTPMP VHFAVANDET INVPQEGAAE FILRDVFDVP DLATTNDDIV NGVAQPGPDG
AEPLAPFTAQ RVDYSLARLS HYTATDPHHF QNHVLFTNYQ FYVAEFEAYA RAQLADPDSG
YTSFVSTGNV EITDPKALIT SASKMPQMPT YHLKRPGGAG ITLVNIGVGP SNAKTATDHI
AVLRPHAWLM VGHCAGLRNS QSLGDFVLAH AYLREDRVLD DDLPVWVPVP ALAEIQIALE
RAVATETQLE GYDLKRIMRT GTVASVDNRN WELRDQHGPV QRLSQSRAIA LDMESATIAA
NGFRFRVPYG TLLCVSDKPL HGELKLPGMA SDFYKTQVAR HLMIGIHAME HLREMPLERI
HSRKLRSFEE TAFL
//
