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Database: UniProt
Entry: W7R2R8_9ALTE
LinkDB: W7R2R8_9ALTE
Original site: W7R2R8_9ALTE 
ID   W7R2R8_9ALTE            Unreviewed;       452 AA.
AC   W7R2R8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, 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=DS2_02038 {ECO:0000313|EMBL:EWH11925.1};
OS   Catenovulum agarivorans DS-2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Catenovulum.
OX   NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH11925.1, ECO:0000313|Proteomes:UP000019276};
RN   [1] {ECO:0000313|EMBL:EWH11925.1, ECO:0000313|Proteomes:UP000019276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-2 {ECO:0000313|EMBL:EWH11925.1,
RC   ECO:0000313|Proteomes:UP000019276};
RX   PubMed=24604650;
RA   Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT   "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT   Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL   Genome Announc. 2:e00144-14(2014).
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:EWH11925.1}.
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DR   EMBL; ARZY01000002; EWH11925.1; -; Genomic_DNA.
DR   RefSeq; WP_035012948.1; NZ_ARZY01000002.1.
DR   AlphaFoldDB; W7R2R8; -.
DR   STRING; 1328313.DS2_02038; -.
DR   PATRIC; fig|1328313.3.peg.424; -.
DR   eggNOG; COG1611; Bacteria.
DR   OrthoDB; 9801098at2; -.
DR   Proteomes; UP000019276; 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:UP000019276}.
FT   DOMAIN          4..108
FT                   /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT                   nucleosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14793"
FT   DOMAIN          330..450
FT                   /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT                   nucleosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11892"
SQ   SEQUENCE   452 AA;  50688 MW;  0B8EFC2A60FCCF21 CRC64;
     MIVEINPLGS MDLLSQLEVD KLKQSSTSEL YRLYRNCSLA VLNVGSHTDS SAEIYDQFQD
     FDIDVIRRER GVKIKLINPP SHAFVDGELI VGIKELLFAV LRDILYTGVR LRDLSKIDLQ
     DPSHVTHYVF DIMRNAGAIK THTDPNMIVC WGGHSIREHE YQYTKDVGYQ MGLRGLNVCT
     GCGPGAMKGP MKGATIGHLK QRVNSARYLG LTEPSIIAAE PPNPIVNELV ILPDIEKRLE
     AFLRVAHGVV IFPGGAGTAE ELLYLLGIML HPANNKQCLP IVLTGPRESA NYFEELDNFI
     RATLGDEAAN MYTIIVDDPT KVAQHMKGYM TEVRNNRKQS GDAYHFNWSL KIDPAFQRPF
     IPNHQNVAEL DLHFSHEKSV LAANLRRTFS AIVAGNVKEE GIQEIARHGP FQINGDKKLM
     LMIDKLLKAF VEQGRMKLPG TKYEPCYQIV QI
//
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