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Database: UniProt
Entry: A0A2K9MHU5_9RHOB
LinkDB: A0A2K9MHU5_9RHOB
Original site: A0A2K9MHU5_9RHOB 
ID   A0A2K9MHU5_9RHOB        Unreviewed;       316 AA.
AC   A0A2K9MHU5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
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=CYR75_13685 {ECO:0000313|EMBL:AUM75208.1};
OS   Paracoccus jeotgali.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=2065379 {ECO:0000313|EMBL:AUM75208.1, ECO:0000313|Proteomes:UP000234882};
RN   [1] {ECO:0000313|Proteomes:UP000234882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBA4604 {ECO:0000313|Proteomes:UP000234882};
RA   Roh S.W., Kim J.Y., Kim J.S.;
RT   "Genomic analysis of Paracoccus sp. CBA4604.";
RL   Submitted (DEC-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; CP025583; AUM75208.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K9MHU5; -.
DR   KEGG; paru:CYR75_13685; -.
DR   OrthoDB; 420651at2; -.
DR   Proteomes; UP000234882; Chromosome.
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:AUM75208.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234882};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          33..219
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   316 AA;  35379 MW;  6B9DBB1E2752E028 CRC64;
     MSKQFASAGD MEEKQISFSE IGEGLWAFTA EGDPNTGVII GDDSVMIVEA QATPRLARKV
     IEKVREVTDK PISHLVMTHY HAVRVLGASA YEAPTVIMGD AARAMVVERG QEDWDSEFQR
     FPRLFQGHEE IPGLTWPTTT FNDRMTVYLG NRRIDLMHLG RAHTAGDIVV HVPDENVMFT
     GDIVEYHSAC YCGDGHLQDW PWTLEAIREY DLAAIAPGRG DALVGAEMVN AALDNTADFV
     RSTYQPAARV AARNGTLREA WDAVRAECDP KFADYAIYEH CLPFNVARAY DEARGIDTPR
     IWTAERDREM WELLQG
//
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