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Database: UniProt
Entry: A0A0A0F392_9GAMM
LinkDB: A0A0A0F392_9GAMM
Original site: A0A0A0F392_9GAMM 
ID   A0A0A0F392_9GAMM        Unreviewed;       460 AA.
AC   A0A0A0F392;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=AMP nucleosidase {ECO:0000256|ARBA:ARBA00011985};
DE            EC=3.2.2.4 {ECO:0000256|ARBA:ARBA00011985};
DE   AltName: Full=AMP nucleosidase {ECO:0000256|ARBA:ARBA00031983};
GN   ORFNames=N799_06120 {ECO:0000313|EMBL:KGM57621.1};
OS   Lysobacter arseniciresistens ZS79.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM57621.1, ECO:0000313|Proteomes:UP000029989};
RN   [1] {ECO:0000313|EMBL:KGM57621.1, ECO:0000313|Proteomes:UP000029989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS79 {ECO:0000313|EMBL:KGM57621.1,
RC   ECO:0000313|Proteomes:UP000029989};
RX   PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA   Liu L., Zhang S., Luo M., Wang G.;
RT   "Genomic information of the arsenic-resistant bacterium Lysobacter
RT   arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT   genomes.";
RL   Stand. Genomic Sci. 10:88-88(2015).
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|ARBA:ARBA00000274};
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:KGM57621.1}.
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DR   EMBL; AVPT01000002; KGM57621.1; -; Genomic_DNA.
DR   RefSeq; WP_036207195.1; NZ_AVPT01000002.1.
DR   AlphaFoldDB; A0A0A0F392; -.
DR   STRING; 913325.N799_06120; -.
DR   eggNOG; COG1611; Bacteria.
DR   OrthoDB; 9801098at2; -.
DR   Proteomes; UP000029989; Unassembled WGS sequence.
DR   GO; GO:0008714; F:AMP nucleosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.30.1850.10; MoCo carrier protein-like; 1.
DR   InterPro; IPR031100; LOG_fam.
DR   InterPro; IPR037153; PpnN-like_sf.
DR   InterPro; IPR021826; PpnN_C.
DR   InterPro; IPR027820; PpnN_N.
DR   NCBIfam; NF038390; Nsidase_PpnN; 1.
DR   PANTHER; PTHR43393; CYTOKININ RIBOSIDE 5'-MONOPHOSPHATE PHOSPHORIBOHYDROLASE; 1.
DR   PANTHER; PTHR43393:SF1; PYRIMIDINE/PURINE NUCLEOTIDE 5'-MONOPHOSPHATE NUCLEOSIDASE; 1.
DR   Pfam; PF14793; DUF4478; 1.
DR   Pfam; PF03641; Lysine_decarbox; 1.
DR   Pfam; PF11892; PpnN_C; 1.
DR   SUPFAM; SSF102405; MCP/YpsA-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029989}.
FT   DOMAIN          15..119
FT                   /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT                   nucleosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14793"
FT   DOMAIN          341..459
FT                   /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT                   nucleosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11892"
SQ   SEQUENCE   460 AA;  50581 MW;  AA8BE5669E4FB344 CRC64;
     MTTPTNATLP TVNARIHPRG GLDILSRAEV AKLADATAGG MHDLLRRCAL AVLTSGSQSD
     DPRAAQELYP DFDIQVHQLD RGVRIDLRNA PAMAFVDGEI IRGVAELLAA TVRDLAYRAI
     ELGEEGGRDL DTSEGITDAV FGLLRNARVL HPSDPNLVVC WGGHSINRDE YMYTKEVGYQ
     LGLRELDICT GCGPGAMKGP MKGATIAHAK QRRRRGRYIG VTEPGIIAAE SPNPIVNHLV
     IMPDIEKRLE AFVRIGHGIV VFPGGVGTAE EILYLLGILL REENADVPFP LILTGPTASA
     PYFEQIDRFI RLTLGDAATE RYQIITGDPA AVAKRMAAGV RKVRDHRLAQ RDSFFFNWSI
     NIPLEFQQPF VPSHEAMAAL DLHHGRKPHE LAADLRRAFS GIVAGNVKED GMRRIEAHGP
     FLIHGDTDMM QSLDALLRAF VEQRRMKIAG EYRPCYRVVA
//
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