ID A0A1Z4VPI3_9GAMM Unreviewed; 373 AA.
AC A0A1Z4VPI3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=FOKN1_1147 {ECO:0000313|EMBL:BAZ93546.1};
OS Thiohalobacter thiocyanaticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalobacterales;
OC Thiohalobacteraceae; Thiohalobacter.
OX NCBI_TaxID=585455 {ECO:0000313|EMBL:BAZ93546.1, ECO:0000313|Proteomes:UP000218765};
RN [1] {ECO:0000313|EMBL:BAZ93546.1, ECO:0000313|Proteomes:UP000218765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOKN1 {ECO:0000313|EMBL:BAZ93546.1,
RC ECO:0000313|Proteomes:UP000218765};
RA Oshiki M., Fukushima T., Kawano S., Nakagawa J.;
RT "Thiocyanate degradation by Thiohalobacter thiocyanaticus FOKN1.";
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}.
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DR EMBL; AP018052; BAZ93546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4VPI3; -.
DR KEGG; ttc:FOKN1_1147; -.
DR Proteomes; UP000218765; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000218765};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 106..300
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 35..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 41399 MW; 5AD03E9075FC47F7 CRC64;
MIVNVEMDMP GYQVLVRLSQ ALILSGALAA PALAEPDGSL QNPGSAERHP DNRLPPNAID
TDTLPRIVID ADAPDDRPLP YYQLAPDTYF LYGNIAQVNE RNRGFNGNAG FVVTTEGVVV
IDSLGTPELG HRLIATIRSV TDRPIRYLIL THSHPDHAYG AAAFRELDAE VTVIGHPGIL
DYLGTPVLQE SADYRRDILG ADMRGFEGVA PDVLIDRPRL GIPYSLELGD ERFDIYNAGK
HHSYGDLVVH QSGEDILWIS DLAFNQRTTF MGDGNSIQAL EAQDWLLQTF PHARLMVPGH
GSAQTPPFPM VEKTRAYIQR LRDEMAAAID DGLTLSEAVE QSHFTDWADV PLYEENHRRN
ANFVYLEMEM ALF
//
