ID G7W3W0_PAETH Unreviewed; 701 AA.
AC G7W3W0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase {ECO:0000313|EMBL:AET58720.1};
GN OrderedLocusNames=HPL003_09795 {ECO:0000313|EMBL:AET58720.1};
OS Paenibacillus terrae (strain HPL-003).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=985665 {ECO:0000313|EMBL:AET58720.1, ECO:0000313|Proteomes:UP000005876};
RN [1] {ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA Shin S.H., Kim S., Kim J.Y.;
RT "Complete sequence of Paenibacillus terrae HPL-003.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HPL-003;
RA Shin S.H., Kim S., Kim J.Y.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AET58720.1, ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|EMBL:AET58720.1,
RC ECO:0000313|Proteomes:UP000005876};
RX PubMed=22328761; DOI=10.1128/JB.06668-11;
RA Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT Bacterium Isolated from Soil Found in Forest Residue.";
RL J. Bacteriol. 194:1266-1266(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-
CC phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001730};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000527};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; CP003107; AET58720.1; -; Genomic_DNA.
DR RefSeq; WP_014279453.1; NC_016641.1.
DR AlphaFoldDB; G7W3W0; -.
DR STRING; 985665.HPL003_09795; -.
DR KEGG; pta:HPL003_09795; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_4_1_9; -.
DR OrthoDB; 9775118at2; -.
DR Proteomes; UP000005876; Chromosome.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd07410; MPP_CpdB_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR041827; CpdB_N.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE_3'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 31..701
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5005132851"
FT DOMAIN 42..283
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 380..568
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT REGION 674..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 76603 MW; 3D9D15FD085A79DB CRC64;
MIFHKKWFRG LTAAVVACSM LVFSAAPSWA ASDSKDSGTV NLRIMETTDI HAALMNYDYY
ADKETNEYGL ISTAGLIKQA RSETRNSLLF DNGDLLQGNP LGDYMARSKT FEKEGGVHPV
YKMMNLMGYD AATVGNHEFN YGLDFLERSL KGADFPYVNA NVYYDDGGQG TKNYFTPYQI
LDKTVTDEKG QEHTIKVGVI GLVTPQITQW DESNLKGKVV TKDIVETAKK FIPQMKTEGA
EIIIVLAHTG YEDVPQTPLM ENAVKYLSKV DGINAILFGH AHKSFPGPDF KGMSGVDLDK
GTINGVPAVE ASSWGKELGI IDLSLEKKNR VWNVTSSQSE VRPVVNTTNP AVQQIKPEFK
LTEAVKDEHK GTLDYVRQPV GTTTAPINSY FALVQDDPSI QIVTNAQKWY VQNHLKGTEY
ENLPVLSAGA PFKAGGRNGA EYYTNIPEGT IAIKNVSDLY VYPNTVQAVE VTGAEIQEWL
EWSAGQFNRI DPKKTEEQSL INKDFPTYNF DVIDGVNYQI DVTQPARYDA KGTVIDPSAH
RIKDLQYNGK AIDPAQKFIV ATNNYRASSS KLANPDGKRI VMAAPDESRQ VVIDYIRTNG
TINPAADGNW SIAPFGEAKV TFESSPDAKD VLAGNQQISF LGSAADGFAK YSLKAGAKPN
AATTPVKETV APAKATAKPA VKATKPAVAK PAKTTKPKAS K
//
