ID F4CUR8_PSEUX Unreviewed; 319 AA.
AC F4CUR8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 OrderedLocusNames=Psed_4219 {ECO:0000313|EMBL:AEA26382.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA26382.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA26382.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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; CP002593; AEA26382.1; -; Genomic_DNA.
DR RefSeq; WP_013676297.1; NC_015312.1.
DR AlphaFoldDB; F4CUR8; -.
DR STRING; 675635.Psed_4219; -.
DR KEGG; pdx:Psed_4219; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_056342_4_0_11; -.
DR OrthoDB; 420651at2; -.
DR Proteomes; UP000007809; 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:UP000007809};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 33..222
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 319 AA; 35125 MW; EF977ACC9A0C7C90 CRC64;
MAKPFASSAD VEAKEQTLEL LADGVYALTA EGDPNIGAIE GEDFLVCFEA LATPVVAARW
LAILREHTDK PVRYLVLSHY HAVRVLGASA FDAEAIVAHE ITRELVAERG AQDWESEFAR
MPRLAEGADS VPGLTWPTLT FADRMTIDLG GDRGELVLQY HGRGHTEGDI TAWLPRHRIL
FAGDLVEAQA ALYTGDASHR DWATTTLDRI EALGADQLVG GRGGVSRGPA EVSAAIAQTR
RFLQVMIDRV GAVQQRGGTL KEAFETTHAA LVDDYGRWPI FEHCLPFDVS RLWDELSGVE
RPIIWTSERD QEVWAQLQD
//
