ID A0A089HYV9_9BACL Unreviewed; 278 AA.
AC A0A089HYV9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000256|ARBA:ARBA00017223};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE AltName: Full=B2 metallo-beta-lactamase {ECO:0000256|ARBA:ARBA00030107};
DE AltName: Full=Metallo-beta-lactamase type II {ECO:0000256|ARBA:ARBA00033087};
GN ORFNames=H70357_01570 {ECO:0000313|EMBL:AIQ15533.1};
OS Paenibacillus sp. FSL H7-0357.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536774 {ECO:0000313|EMBL:AIQ15533.1, ECO:0000313|Proteomes:UP000029508};
RN [1] {ECO:0000313|EMBL:AIQ15533.1, ECO:0000313|Proteomes:UP000029508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0357 {ECO:0000313|EMBL:AIQ15533.1,
RC ECO:0000313|Proteomes:UP000029508};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001526};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Class-B
CC beta-lactamase family. {ECO:0000256|ARBA:ARBA00005250}.
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DR EMBL; CP009241; AIQ15533.1; -; Genomic_DNA.
DR RefSeq; WP_038584950.1; NZ_CP009241.1.
DR AlphaFoldDB; A0A089HYV9; -.
DR STRING; 1536774.H70357_01570; -.
DR KEGG; paeh:H70357_01570; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_1022825_0_0_9; -.
DR Proteomes; UP000029508; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; PTHR42951:SF20; BETA LACTAMASE; 1.
DR PANTHER; PTHR42951; METALLO-BETA-LACTAMASE DOMAIN-CONTAINING; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AIQ15533.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 18..207
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 278 AA; 31368 MW; 1790A39D52C62D8D CRC64;
MLKSKSAGVT LFQSDLYETN SLVVETVECV LVVDPCWLPR EVEEIRLYVE NILAGRRLLL
LFTHSDYDHI IGYGAFKEAE VIASRAFAGK SEEERKAIIE DLRTFDDNYY LRRPYETNYP
AVDHIIEQDG QRLVFGDMVL TGYVAPGHTD DGLFTLVEPL GLFIAGDYLS DVEFPYIYDN
SRSYEQTLGK LELILANHAI TLLVPGHGEV ADSLPEISRR KAAGLAYIDN LRTAIAEGKQ
EDIERLIDGC AFPRNMAKFH RSNRELIEKE LAETAGET
//
