ID A0A222E3J5_9RHOB Unreviewed; 494 AA.
AC A0A222E3J5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:ASP20779.1};
GN ORFNames=ANTHELSMS3_02101 {ECO:0000313|EMBL:ASP20779.1};
OS Antarctobacter heliothermus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Antarctobacter.
OX NCBI_TaxID=74033 {ECO:0000313|EMBL:ASP20779.1, ECO:0000313|Proteomes:UP000203589};
RN [1] {ECO:0000313|EMBL:ASP20779.1, ECO:0000313|Proteomes:UP000203589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS3 {ECO:0000313|EMBL:ASP20779.1,
RC ECO:0000313|Proteomes:UP000203589};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Antarctobacter heliothermus Strain SMS3 Isolated from a
RT culture of the Diatom Skeletonema marinoi.";
RL Submitted (JUL-2017) 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; CP022540; ASP20779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222E3J5; -.
DR KEGG; aht:ANTHELSMS3_02101; -.
DR OrthoDB; 7945729at2; -.
DR Proteomes; UP000203589; 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 Glycosidase {ECO:0000313|EMBL:ASP20779.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01932, ECO:0000313|EMBL:ASP20779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000203589}.
FT DOMAIN 26..179
FT /note="AMP nucleoside phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10423"
FT DOMAIN 279..441
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 494 AA; 55069 MW; D65FC3181CD8E5C8 CRC64;
MQDTAENLEI ITPEVPGEES FDDSGAAVAR LIELYDTAAV FLRDAFLQAM TMGHPGTRLR
AFYPEIRLTT TRFDKIDSRL SFGHVTQPGT YATTVTRPQL FRDYLMQQID LLLGNHGVKV
RIGLSDTPMP VHFAVANFPD VNVPQEGAAS FALRDVFDVP DLTTTNDDIV NGEAQPAPDG
TLPLAPFTAQ RVDYSLARLS HYTATDPEHF QNHVLFTNYQ FYVDEFEAYA RAMLADPNSG
YTSFVSTGNA EITDPDTVLH PPIRMPQMPT YHLKRPKQAG ITLVNIGVGP SNAKTATDHI
AVMRSHAWLM VGHCAGLRNS QSLGDYVLAH AYLREDKVLD DDLPVWVPIP ALAEIQIALE
NAVAKETQLD GFDLKRVMRT GTVASLDNRN WELREQSGPV KRLSQSRAIA LDMESATIAA
NGFRFRVPYG TLLCVSDRPL HGELKLPGMA SDFYKSQVSR HLRIGIRAME TLREMPLERI
HSRKLRSFEE TAFL
//
