ID A0A315F4J3_9BURK Unreviewed; 332 AA.
AC A0A315F4J3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
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=B9Z45_00095 {ECO:0000313|EMBL:PUE63124.1};
OS Limnohabitans sp. 2KL-17.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1100704 {ECO:0000313|EMBL:PUE63124.1, ECO:0000313|Proteomes:UP000251446};
RN [1] {ECO:0000313|EMBL:PUE63124.1, ECO:0000313|Proteomes:UP000251446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2KL-17 {ECO:0000313|EMBL:PUE63124.1,
RC ECO:0000313|Proteomes:UP000251446};
RA Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA Simek K., Ghai R.;
RT "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PUE63124.1}.
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DR EMBL; NESK01000001; PUE63124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A315F4J3; -.
DR OrthoDB; 1273797at2; -.
DR Proteomes; UP000251446; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd16282; 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; 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:PUE63124.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000251446};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 68..257
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 332 AA; 36426 MW; 2482FD32958BA257 CRC64;
MKRRQWLLGG AAMCGAVLWP EARSLAQQAQ EFIEGPPVAD IPAQQLSPHV WMVYSPDGFP
TPENRGMMSN VIFVVTSAGV VVLDSGASLQ IGQMAIRMIR KVTDKPVVAV FNSHYHGDHW
LGNHAFVKAY GDQLPIYALP STIEKLKGTE GNLWRSLMER WTNQSTLGTQ VVLPNTAVQH
GQVLQFGDVT LCMHHYGTAH TPSDLCVEVV QDKLTAVGDI AMTNRIANMD EGSYPGTFKY
YKALMAATGE QLWVPGHGQA RKDLLKTYGD FMAGIWEPCL KMVEDGKSEA EAKAAVLKDP
RVAARAKTMQ GFDGNIGKYV SLAYIEAEKV AF
//
