ID A0A010SMC5_PSEFL Unreviewed; 487 AA.
AC A0A010SMC5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=HK44_012165 {ECO:0000313|EMBL:EXF92303.1};
OS Pseudomonas fluorescens HK44.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF92303.1, ECO:0000313|Proteomes:UP000022611};
RN [1] {ECO:0000313|EMBL:EXF92303.1, ECO:0000313|Proteomes:UP000022611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK44 {ECO:0000313|EMBL:EXF92303.1,
RC ECO:0000313|Proteomes:UP000022611};
RX PubMed=21742869; DOI=10.1128/JB.05530-11;
RA Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA Karpinets T.V., Brown S.D., Sayler G.S.;
RT "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT HK44.";
RL J. Bacteriol. 193:5009-5010(2011).
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:EXF92303.1}.
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DR EMBL; AFOY02000018; EXF92303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A010SMC5; -.
DR PATRIC; fig|1042209.11.peg.4842; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_026838_1_0_6; -.
DR OrthoDB; 7945729at2; -.
DR Proteomes; UP000022611; 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 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; 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:EXF92303.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01932, ECO:0000313|EMBL:EXF92303.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000022611}.
FT DOMAIN 13..169
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 272..454
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 487 AA; 54454 MW; D883FA6DC2508CA0 CRC64;
MTEAFIVVQT AEQAVDRLAA LHERATTALS QALKRYLKDR IEPDAEQRAM FRYPELRLTY
LCQGEVPQTT RAYAKVQLPG TYSITVTHPA AFRKYLLEQL VPLMHDFTVT VEVGVSEQNI
PYPYVVEQGD ELAGSGVTAA VLARVFPSTD LSAATDGIAD GLYDWENTDP LPLALFDAAR
VDFSLRRLVH YTGSDWRHVQ PWILLTNYHR YVDQFITHGL EQLRTDPRFV RMVLPGNVII
DKSMDHGEAS AIAAGVVWHR YQMPAYHLQA SDGHGVTLVN IGVGPSNAKN ITDHLAVLRP
HCWLMIGHCG GLRQSQTIGD YVLAHAYMRR DGILDRVVPP NIPIPALAEV QLALQQAAAN
VTGEKGDDLK KRLRTGTVLT YDDRNWELRW AQERPLINLS RAVAVDMESG TIAAQGYRLR
VPYGTLLCVS DKPLHSEIKL PGSANAFYER AVSQHLKIGI AAVDLLRTEL NSLHSRKLRS
FDEPPFR
//