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Database: UniProt
Entry: A0A3L6ZWH9_9MICO
LinkDB: A0A3L6ZWH9_9MICO
Original site: A0A3L6ZWH9_9MICO 
ID   A0A3L6ZWH9_9MICO        Unreviewed;       279 AA.
AC   A0A3L6ZWH9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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=D9V29_04270 {ECO:0000313|EMBL:RLP72376.1};
OS   Mycetocola manganoxydans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Mycetocola.
OX   NCBI_TaxID=699879 {ECO:0000313|EMBL:RLP72376.1, ECO:0000313|Proteomes:UP000270299};
RN   [1] {ECO:0000313|EMBL:RLP72376.1, ECO:0000313|Proteomes:UP000270299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AB209002 {ECO:0000313|EMBL:RLP72376.1,
RC   ECO:0000313|Proteomes:UP000270299};
RA   Li J.;
RL   Submitted (OCT-2018) 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:RLP72376.1}.
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DR   EMBL; RCUV01000005; RLP72376.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6ZWH9; -.
DR   OrthoDB; 2273115at2; -.
DR   Proteomes; UP000270299; 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:RLP72376.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270299};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          20..209
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   279 AA;  30352 MW;  117829152E91F674 CRC64;
     MSSWNEVADR VYQRRYDPLD VSVCVVAGSD GLLLVDTRCN PREAGELAAD VAELSSAPIR
     WVANTHAHYD HSFGNQVFPD TSIFGHHLIA RHFAEFEGPR LESWLAAPES QPHYDWRDVR
     LTPPTVPVTD VLSLDLGDRL VRFHPLPPGH TDTDLIVEIP DAATWLLGDV VEESGPPMYG
     SGSFPLGWPG VLDNIAELIA PGDVLVPGHG RPVDRAFLLE QAAVLHIVAD GIRSSFDQSE
     PIESASERVA SMSRLPLEIV ESAVLRGYTQ LAASAGASE
//
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