ID R3W8A0_9ENTE Unreviewed; 515 AA.
AC R3W8A0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase {ECO:0000313|EMBL:EOL44016.1};
GN ORFNames=UC3_01646 {ECO:0000313|EMBL:EOL44016.1};
OS Enterococcus phoeniculicola ATCC BAA-412.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158610 {ECO:0000313|EMBL:EOL44016.1, ECO:0000313|Proteomes:UP000013785};
RN [1] {ECO:0000313|EMBL:EOL44016.1, ECO:0000313|Proteomes:UP000013785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-412 {ECO:0000313|EMBL:EOL44016.1,
RC ECO:0000313|Proteomes:UP000013785};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus phoeniculicola BAA-412.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:EOL44016.1}.
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DR EMBL; AJAT01000014; EOL44016.1; -; Genomic_DNA.
DR RefSeq; WP_010768309.1; NZ_KB946327.1.
DR AlphaFoldDB; R3W8A0; -.
DR STRING; 154621.RV11_GL000271; -.
DR PATRIC; fig|1158610.3.peg.1633; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_4_4_9; -.
DR OrthoDB; 9801679at2; -.
DR Proteomes; UP000013785; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000013785}.
FT DOMAIN 3..233
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 321..477
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 515 AA; 57431 MW; 8AD7A0E124AE0433 CRC64;
MEIRILATSD MHGYIEPTNY AEKNSDLPFG TEKIATLIKK IREQATGPVL LIENGDFIQG
SPFSYYLAKS KRVAELTQVI NTLDYDLGVL GNHEFNYGLA YLNSAIKSYN HPVLAANILN
KDGQPAFGKA YEIFEKEGVK IAVLGLVTQY IPHWEQPATV KDLTFKSIVE TAKEYIPQLK
EQADIVVVAY HGGFERDLVT GEPTELLTGE NEGYQLLQEV SGIDALVTGH QHREIATHIH
GVPVIQPGYR GSHLGEIILE VENTQEGWHV VSSQAEIHAT AGVVADEEIK ELIAPIGEEV
EKWLDQPVGK VEGSMKINDP MGVRLHEHPY IEFINRVQMD ASGAKISGTS LFNNEGKGFG
EIITMRDVIT NYIYPNTLAV LKVTGADLRA ALEQTANYLA VKDGKIIFNP EFIEPKPQYY
NYDMYEGIDY VIDMSKPAFS RITTLTFEGK PVEPTDELEM VINQYRAVGG GNYTMFEAGK
IVREIQIDMT ELIANYLKKN PVIQAETNQN FTVIL
//
