ID Q8U5F8_AGRFC Unreviewed; 501 AA.
AC Q8U5F8;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 2.
DT 27-MAR-2024, entry version 100.
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:AAK86815.2};
GN OrderedLocusNames=Atu1006 {ECO:0000313|EMBL:AAK86815.2};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK86815.2, ECO:0000313|Proteomes:UP000000813};
RN [1] {ECO:0000313|EMBL:AAK86815.2, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2] {ECO:0000313|EMBL:AAK86815.2, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE007869; AAK86815.2; -; Genomic_DNA.
DR RefSeq; NP_354030.2; NC_003062.2.
DR RefSeq; WP_010971329.1; NC_003062.2.
DR AlphaFoldDB; Q8U5F8; -.
DR STRING; 176299.Atu1006; -.
DR EnsemblBacteria; AAK86815; AAK86815; Atu1006.
DR KEGG; atu:Atu1006; -.
DR PATRIC; fig|176299.10.peg.1020; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_026838_1_0_5; -.
DR OrthoDB; 7945729at2; -.
DR PhylomeDB; Q8U5F8; -.
DR Proteomes; UP000000813; Chromosome circular.
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:UP000000813}.
FT DOMAIN 29..184
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 284..448
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 501 AA; 55252 MW; C5B9DAB0ECFA92C1 CRC64;
MTIAKPTIPP FTFISPEPFA PQSFTDPKEA VEALTALYER NTAFLINSFT DLAKGAPITG
RYRACYPQVS LETSTFGHVD SRLSYGHVTS PGVYTTTITR PDLFRHYLKE QLGLLIKNHG
VPVTVAESAT PIPLHFAFGE GAYVEAAAAS SLSDVPLRDL FDTPDLNNTD DLIANGEYDQ
VPGEPAPLAP FTAQRIDYSL ARLSHYTATS ASHFQNFVLF TNYQFYIDEF AAWARKLMAD
GGEGYTEFVE PGNIVTLAGS DRPTTDMTLA RLPQMPAYHL KKKGHAGITL VNIGVGPSNA
KTITDHIAVL RPHAWLMVGH CAGLRNSQRL GDYVLAHAYV REDHVLDDDL PVWVPIPALA
EVQLALEGAV AEVTGYEGFE LKRIMRTGTV ATIDNRNWEL RDQAGPVKRL SQSRAIALDM
ESATIAANGF RFRVPYGTLL CVSDKPLHGE LKLPGMATEF YRTQVAQHLQ IGIRAVQKLA
AMQKETLHSR KLRSFYETAF Q
//
