ID A0A2V2YGN6_9BACL Unreviewed; 340 AA.
AC A0A2V2YGN6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Glyoxylase-like metal-dependent hydrolase (Beta-lactamase superfamily II) {ECO:0000313|EMBL:PWV92057.1};
GN ORFNames=DFQ01_13744 {ECO:0000313|EMBL:PWV92057.1};
OS Paenibacillus cellulosilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=375489 {ECO:0000313|EMBL:PWV92057.1, ECO:0000313|Proteomes:UP000246635};
RN [1] {ECO:0000313|EMBL:PWV92057.1, ECO:0000313|Proteomes:UP000246635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5696 {ECO:0000313|EMBL:PWV92057.1,
RC ECO:0000313|Proteomes:UP000246635};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAY-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 -!- 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:PWV92057.1}.
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DR EMBL; QGTQ01000037; PWV92057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2YGN6; -.
DR OrthoDB; 9761531at2; -.
DR Proteomes; UP000246635; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07725; TTHA1429-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR048933; B_lactamase-like_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23131; ENDORIBONUCLEASE LACTB2; 1.
DR PANTHER; PTHR23131:SF0; ENDORIBONUCLEASE LACTB2; 1.
DR Pfam; PF21221; B_lactamase-like_C; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PWV92057.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000246635}.
FT DOMAIN 34..248
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 340 AA; 38239 MW; 6C3EA51B7E9EAAAD CRC64;
MTNEQSNTNK LEFIQQLENG WLRVKVPLPF SLKYVNAYLI PEPEGGCTVI DPGLHTPEAV
EAWESVLQSL GITFSDIARI VLTHQHPDHY GLAGLFQQRS GAPVWISRAS QRYAERMWGV
DRSLADRLVE VFRLHGMPAD LRDGIKDNLE SFVPMVSPYP AVSYMEAGEP FRFGGIDWTT
IEAHGHAEGQ ILFYDEASRI MICGDQVMPD ITPNVSVVPG EREDPLEAFL ISLEQLSKLD
VSLALPGHRD PIIDFTGRCE ALIAHHARRL DKMVAFIQEQ PESSVTGFAM CELLFSGRIT
LNMHNLRFAM AETLAHLVRL EKQGRVALLE QNGQYIYRAK
//
