ID A0A3Q8SAI1_9BACL Unreviewed; 208 AA.
AC A0A3Q8SAI1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:AZK46186.1};
GN ORFNames=EIM92_08245 {ECO:0000313|EMBL:AZK46186.1};
OS Paenibacillus lentus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1338368 {ECO:0000313|EMBL:AZK46186.1, ECO:0000313|Proteomes:UP000273145};
RN [1] {ECO:0000313|EMBL:AZK46186.1, ECO:0000313|Proteomes:UP000273145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25539 {ECO:0000313|EMBL:AZK46186.1,
RC ECO:0000313|Proteomes:UP000273145};
RA Kook J.-K., Park S.-N., Lim Y.K.;
RT "Genome sequencing of Paenibacillus lentus DSM25539(T).";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Counteracts the endogenous Pycsar antiviral defense system.
CC Phosphodiesterase that enables metal-dependent hydrolysis of host
CC cyclic nucleotide Pycsar defense signals such as cCMP and cUMP.
CC {ECO:0000256|ARBA:ARBA00034301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic CMP + H2O = CMP + H(+); Xref=Rhea:RHEA:72675,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58003,
CC ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00034221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72676;
CC Evidence={ECO:0000256|ARBA:ARBA00034221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic UMP + H2O = H(+) + UMP; Xref=Rhea:RHEA:70575,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:184387; Evidence={ECO:0000256|ARBA:ARBA00034227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70576;
CC Evidence={ECO:0000256|ARBA:ARBA00034227};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP034248; AZK46186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q8SAI1; -.
DR KEGG; plen:EIM92_08245; -.
DR OrthoDB; 9802248at2; -.
DR Proteomes; UP000273145; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd06262; metallo-hydrolase-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR46233; HYDROXYACYLGLUTATHIONE HYDROLASE GLOC; 1.
DR PANTHER; PTHR46233:SF3; HYDROXYACYLGLUTATHIONE HYDROLASE GLOC; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AZK46186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000273145}.
FT DOMAIN 13..191
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 208 AA; 22841 MW; 0BFBCDF6440F62F5 CRC64;
MLNIETFSLG PLQTNAYLIR GEDEGKAIVI DPGMNPAPLI RRIEGLEIEA ILLTHAHFDH
IGGVEEIRRL KKCPVYLHSL ESDWLTTPAL NGSLRWAEVS PPIQSGPAEY ELAEGQKLKL
IGHEFTVFHT PGHSPGSVSF LCGNHLFSGD VLFRMSVGRT DLPGGREADL FNSIRGKLFT
LSDEVIVYPG HGPKTTIGFE KANNPYVS
//
