ID A0A1Y2R1V8_9BURK Unreviewed; 326 AA.
AC A0A1Y2R1V8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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=CAP37_01250 {ECO:0000313|EMBL:OSZ74131.1};
OS Hydrogenophaga sp. IBVHS1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1985169 {ECO:0000313|EMBL:OSZ74131.1, ECO:0000313|Proteomes:UP000194358};
RN [1] {ECO:0000313|EMBL:OSZ74131.1, ECO:0000313|Proteomes:UP000194358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVHS1 {ECO:0000313|EMBL:OSZ74131.1,
RC ECO:0000313|Proteomes:UP000194358};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-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:OSZ74131.1}.
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DR EMBL; NFUU01000001; OSZ74131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2R1V8; -.
DR STRING; 1985169.CAP37_01250; -.
DR OrthoDB; 5290005at2; -.
DR Proteomes; UP000194358; 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:OSZ74131.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194358};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..229
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 326 AA; 35911 MW; 168F7BFF86348131 CRC64;
MSKAFASQAD LADKKITFEQ LSPHCWAYTA EGDPNSGVII GEKFIMVSDA TATPAMARDL
IQQIRTVSDK PIKYVLLTHY HAVRVLGASA YVAEGATEII ASRGTYELIV ERGAEDMQSE
MERFPRLFRG ADSVPGLTWP TLVVGDGKPG RQGSLEVDLG GVKVQIWHPG PGHTRGDTIA
WVEEEKVLFS GDLVEYEAGV YTGDAQLEEW PTTLEALRAL KAEYIVPGRG EAMKGNADVN
KALDYTQRWV TTLFQAGKEA AAAGMDLKSA MAHTRKSMDP VFGHVFIYEH CLPFDVSRAY
DEAKGIKNPR IWTAERDKEM WSALQA
//
