ID A0A0F2RRX2_9RHOB Unreviewed; 487 AA.
AC A0A0F2RRX2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=VR71_22360 {ECO:0000313|EMBL:KJS40786.1};
OS Roseovarius sp. BRH_c41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS40786.1, ECO:0000313|Proteomes:UP000033676};
RN [1] {ECO:0000313|EMBL:KJS40786.1, ECO:0000313|Proteomes:UP000033676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS40786.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS40786.1}.
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DR EMBL; LADY01000065; KJS40786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2RRX2; -.
DR PATRIC; fig|1629709.5.peg.4274; -.
DR Proteomes; UP000033676; 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}.
FT DOMAIN 19..171
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 267..434
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 487 AA; 53501 MW; 07607055CBA0F1AD CRC64;
MTMQTPDEIA PEAFTDARAA VDRLCQLYAA GTEFLCAAFA RALAGNLPIG RVRAYYPEIR
LTTGTYAKVD SRLSFGHVSN PGTYAATITR PDLFRAYLEQ QIGLLLVNHS VGVTIGTSDT
PMPVHFAVAE DAGLSVPQEG AAEFTLRDYF DVPDLATTND DIVNGTWVSV PNGAAPLAPF
TAQRVDYSLA RLTHYTATDP RHFQNYVLFT NYQFYVSEFE TYARRMLGDA ESGYTAFVST
GNAEITGPDD PLPAPERLPQ MPAYHLKRAD GSGITLVNIG VGPSNAKTAT DHIAVLRPHA
WVMVGHCAGL RNSQSLGDFV LAHAYLREDR VLDADLPAWV PIPALAEIQI ALQDAVAAET
QLEGFDLKRV MRTGTVASVD NRNWELRDQS GPVQRLSQSR AIALDMESAT IAANGFRFRV
PYGTLLCVSD KPLQGELKLP GMASEFYKSQ VSRHLMIGIR AMESLRRMPL ERIHSRKLRS
FEETAFL
//
