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
//