ID   C3LTE8_VIBCM            Unreviewed;       457 AA.
AC   C3LTE8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   OrderedLocusNames=VCM66_0856 {ECO:0000313|EMBL:ACP05174.1};
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112 {ECO:0000313|EMBL:ACP05174.1, ECO:0000313|Proteomes:UP000001217};
RN   [1] {ECO:0000313|EMBL:ACP05174.1, ECO:0000313|Proteomes:UP000001217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2 {ECO:0000313|EMBL:ACP05174.1,
RC   ECO:0000313|Proteomes:UP000001217};
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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};
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DR   EMBL; CP001233; ACP05174.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3LTE8; -.
DR   KEGG; vcm:VCM66_0856; -.
DR   HOGENOM; CLU_047550_0_0_6; -.
DR   Proteomes; UP000001217; Chromosome I.
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; IPR049788; PpnN.
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;
FT   DOMAIN          9..115
FT                   /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT                   nucleosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14793"
FT   DOMAIN          335..456
FT                   /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT                   nucleosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11892"
SQ   SEQUENCE   457 AA;  51078 MW;  133ADD9121417222 CRC64;
     MKEDTMIIQV SPAGSMDLLS QLEVERLKKT ASSDLYQLYR NCSLAVLNSG SHTDNSKELL
     DKYKNFDITV MRRERGIKLE LANPPEHAFV DGQIIKGIQE HLFSVLRDIV YVNMHLADSQ
     RLNLTNATHI TNLVFGILRN AGALIPGATP NLVVCWGGHS INEVEYQYTR EVGHELGLRE
     LNICTGCGPG AMEGPMKGAA VGHAKQRYSE YRYLGLTEPS IIAAEPPNPI VNELVIMPDI
     EKRLEAFVRM AHGIIIFPGG PGTAEELLYI LGIMMHPENA DQPMPIVLTG PKQSEAYFRS
     LDKFITDTLG EAARKHYSIV IDNPAEAARI MSNAMPLVRQ HRKDKEDAYS FNWSLKIEPE
     FQLPFEPNHE SMANLDLHLN QRPEVLAANL RRAFSGVVAG NVKAEGIREI ERHGPFEMHG
     DPVLMKKMDQ LLNDFVAQNR MKLPGGSAYE PCYKIVT
//