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Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase type II) (Metallo-beta-lactamase NDM-1) (Metallo-beta-lactamase type II) (New Delhi metallo-beta-lactamase-1) (NDM-1)

 BLAN1_KLEPN             Reviewed;         270 AA.
C7C422;
02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 1.
22-NOV-2017, entry version 57.
RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000305};
EC=3.5.2.6 {ECO:0000269|PubMed:19770275};
AltName: Full=B2 metallo-beta-lactamase {ECO:0000305};
AltName: Full=Beta-lactamase type II {ECO:0000303|PubMed:19770275};
AltName: Full=Metallo-beta-lactamase NDM-1 {ECO:0000303|PubMed:19770275};
AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:19770275};
AltName: Full=New Delhi metallo-beta-lactamase-1 {ECO:0000303|PubMed:19770275};
Short=NDM-1 {ECO:0000303|PubMed:19770275};
Flags: Precursor;
Name=blaNDM-1 {ECO:0000303|PubMed:19770275};
Klebsiella pneumoniae.
Plasmid pKpANDM-1.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Klebsiella.
NCBI_TaxID=573;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, AND
SUBSTRATE SPECIFICITY.
STRAIN=KP-05-506;
PubMed=19770275; DOI=10.1128/AAC.00774-09;
Yong D., Toleman M.A., Giske C.G., Cho H.S., Sundman K., Lee K.,
Walsh T.R.;
"Characterization of a new metallo-beta-lactamase gene, bla(NDM-1),
and a novel erythromycin esterase gene carried on a unique genetic
structure in Klebsiella pneumoniae sequence type 14 from India.";
Antimicrob. Agents Chemother. 53:5046-5054(2009).
[2]
EPIDEMIOLOGY.
PubMed=20705517; DOI=10.1016/S1473-3099(10)70143-2;
Kumarasamy K.K., Toleman M.A., Walsh T.R., Bagaria J., Butt F.,
Balakrishnan R., Chaudhary U., Doumith M., Giske C.G., Irfan S.,
Krishnan P., Kumar A.V., Maharjan S., Mushtaq S., Noorie T.,
Paterson D.L., Pearson A., Perry C., Pike R., Rao B., Ray U.,
Sarma J.B., Sharma M., Sheridan E., Thirunarayan M.A., Turton J.,
Upadhyay S., Warner M., Welfare W., Livermore D.M., Woodford N.;
"Emergence of a new antibiotic resistance mechanism in India,
Pakistan, and the UK: a molecular, biological, and epidemiological
study.";
Lancet Infect. Dis. 10:597-602(2010).
[3]
EPIDEMIOLOGY.
PubMed=20577157;
Limbago B., Kallen A.;
"Detection of Enterobacteriaceae isolates carrying metallo-beta-
lactamase -United States, 2010.";
MMWR Morb. Mortal. Wkly. Rep. 59:750-750(2010).
[4]
X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS AND ZINC IONS, COFACTOR, AND SUBUNIT.
PubMed=22713171; DOI=10.1021/ja303579d;
King D.T., Worrall L.J., Gruninger R., Strynadka N.C.;
"New Delhi metallo-beta-lactamase: structural insights into beta-
lactam recognition and inhibition.";
J. Am. Chem. Soc. 134:11362-11365(2012).
[5]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 29-270 IN COMPLEX WITH ZINC
IONS, ENZYME REGULATION, COFACTOR, AND SUBUNIT.
PubMed=25815530; DOI=10.1021/jm501844d;
Klingler F.M., Wichelhaus T.A., Frank D., Cuesta-Bernal J.,
El-Delik J., Muller H.F., Sjuts H., Gottig S., Koenigs A., Pos K.M.,
Pogoryelov D., Proschak E.;
"Approved drugs containing thiols as inhibitors of metallo-beta-
lactamases: strategy to combat multidrug-resistant bacteria.";
J. Med. Chem. 58:3626-3630(2015).
-!- FUNCTION: Confers resistance to the different beta-lactams
antibiotics (penicillin, cephalosporin and carbapenem) via the
hydrolysis of the beta-lactam ring. Does not confer resistance to
the polymixin colistin or the fluoroquinolone ciprofloxacin.
{ECO:0000269|PubMed:19770275}.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000269|PubMed:19770275}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:22713171,
ECO:0000269|PubMed:25815530};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530};
-!- ENZYME REGULATION: Inhibits by captopril, thiorphan, dimercaprol
and tiopronin (PubMed:25815530). This enzyme is not susceptible to
inactivation by the beta-lactamase-blocking agents clavulanic acid
(PubMed:19770275). {ECO:0000269|PubMed:19770275,
ECO:0000269|PubMed:25815530}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8 uM for cefuroxime {ECO:0000269|PubMed:19770275};
KM=10 uM for cefotaxime {ECO:0000269|PubMed:19770275};
KM=10 uM for cephalothin {ECO:0000269|PubMed:19770275};
KM=12 uM for piperacillin {ECO:0000269|PubMed:19770275};
KM=16 uM for penicillin G {ECO:0000269|PubMed:19770275};
KM=22 uM for ampicillin {ECO:0000269|PubMed:19770275};
KM=49 uM for cefoxitin {ECO:0000269|PubMed:19770275};
KM=49 uM for meropenem {ECO:0000269|PubMed:19770275};
KM=77 uM for cefepime {ECO:0000269|PubMed:19770275};
KM=94 uM for imipenem {ECO:0000269|PubMed:19770275};
KM=181 uM for ceftazidime {ECO:0000269|PubMed:19770275};
Note=No activity detected against the monobactam aztreonam.
{ECO:0000269|PubMed:19770275};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19770275,
ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
-!- MISCELLANEOUS: Enterobacteriaceae carrying this gene (identified
by PCR) have been isolated in Sweden, India, Pakistan, Bangladesh,
England, Scotland, Northern Ireland, Australia and the USA. The
organisms they were identified in were K.pneumoniae, Enterobacter
cloacae, E.coli, Proteus spp, Citrobacter freundii, Morganella
morganii, Providencia spp and Klebsille oxytoca. In India most
isolates were from community-acquired infections rather than
hospital-acquired infections, indicating the gene is widespread in
the environment. {ECO:0000269|PubMed:20577157,
ECO:0000269|PubMed:20705517}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
Class-B beta-lactamase family. {ECO:0000305}.
-!- CAUTION: Transfer of a plasmid encoding this gene has been
detected between bacteria within a patient (between K.pneumoniae
and E.coli). Additionally the gene may be encoded within a
transposon. {ECO:0000305}.
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EMBL; FN396876; CAZ39946.1; -; Genomic_DNA.
RefSeq; WP_004201164.1; NZ_NPII01000041.1.
RefSeq; YP_005352173.1; NC_016980.1.
RefSeq; YP_006958736.1; NC_019153.1.
RefSeq; YP_006959150.1; NC_019158.1.
RefSeq; YP_006959255.1; NC_019162.1.
RefSeq; YP_006959318.1; NC_019163.1.
RefSeq; YP_007195502.1; NC_019889.1.
RefSeq; YP_007641427.1; NC_020811.1.
RefSeq; YP_007936899.1; NC_021180.1.
RefSeq; YP_008719663.1; NC_022609.1.
RefSeq; YP_009023060.1; NC_023908.1.
RefSeq; YP_009071638.1; NC_025184.1.
PDB; 3PG4; X-ray; 2.00 A; A=49-270.
PDB; 3Q6X; X-ray; 1.30 A; A/B=29-270.
PDB; 3RKJ; X-ray; 2.00 A; A/B=39-270.
PDB; 3RKK; X-ray; 2.35 A; A/B=39-270.
PDB; 3SBL; X-ray; 2.31 A; A=39-270.
PDB; 3SFP; X-ray; 2.27 A; A/B/C/D=39-270.
PDB; 3SPU; X-ray; 2.10 A; A/B/C/D/E=27-270.
PDB; 3SRX; X-ray; 2.50 A; A/B=37-270.
PDB; 3ZR9; X-ray; 1.91 A; A=42-270.
PDB; 4EXS; X-ray; 2.40 A; A/B=1-270.
PDB; 4EXY; X-ray; 1.47 A; A/B=1-270.
PDB; 4EY2; X-ray; 1.17 A; A/B=1-270.
PDB; 4EYB; X-ray; 1.16 A; A/B=1-270.
PDB; 4EYF; X-ray; 1.80 A; A/B=1-270.
PDB; 4EYL; X-ray; 1.90 A; A/B=1-270.
PDB; 4GYQ; X-ray; 1.35 A; A/B/C/D=31-270.
PDB; 4GYU; X-ray; 1.80 A; A=31-270.
PDB; 4H0D; X-ray; 1.50 A; A/B=31-270.
PDB; 4HKY; X-ray; 2.00 A; A/B=31-270.
PDB; 4HL1; X-ray; 1.50 A; A/B=31-270.
PDB; 4HL2; X-ray; 1.05 A; A/B=31-270.
PDB; 4RAM; X-ray; 1.50 A; A/B=31-270.
PDB; 4RAW; X-ray; 1.30 A; A/B=31-270.
PDB; 4RBS; X-ray; 2.40 A; A/B=31-270.
PDB; 4RL0; X-ray; 1.30 A; A/B=29-270.
PDB; 4RL2; X-ray; 2.01 A; A/B=29-270.
PDB; 4RM5; X-ray; 2.10 A; A/B/C/D=29-270.
PDB; 4U4L; X-ray; 1.90 A; A/B/C/D=27-270.
PDB; 5A5Z; X-ray; 2.60 A; A/C=29-270.
PDB; 5JQJ; X-ray; 1.67 A; A=29-270.
PDB; 5K4K; X-ray; 1.76 A; A/K=29-270.
PDB; 5K4M; X-ray; 1.98 A; A=29-270.
PDB; 5K4N; X-ray; 1.68 A; A=29-270.
PDB; 5N0H; X-ray; 1.90 A; A/B=29-270.
PDB; 5N0I; X-ray; 1.47 A; A/B=29-270.
PDBsum; 3PG4; -.
PDBsum; 3Q6X; -.
PDBsum; 3RKJ; -.
PDBsum; 3RKK; -.
PDBsum; 3SBL; -.
PDBsum; 3SFP; -.
PDBsum; 3SPU; -.
PDBsum; 3SRX; -.
PDBsum; 3ZR9; -.
PDBsum; 4EXS; -.
PDBsum; 4EXY; -.
PDBsum; 4EY2; -.
PDBsum; 4EYB; -.
PDBsum; 4EYF; -.
PDBsum; 4EYL; -.
PDBsum; 4GYQ; -.
PDBsum; 4GYU; -.
PDBsum; 4H0D; -.
PDBsum; 4HKY; -.
PDBsum; 4HL1; -.
PDBsum; 4HL2; -.
PDBsum; 4RAM; -.
PDBsum; 4RAW; -.
PDBsum; 4RBS; -.
PDBsum; 4RL0; -.
PDBsum; 4RL2; -.
PDBsum; 4RM5; -.
PDBsum; 4U4L; -.
PDBsum; 5A5Z; -.
PDBsum; 5JQJ; -.
PDBsum; 5K4K; -.
PDBsum; 5K4M; -.
PDBsum; 5K4N; -.
PDBsum; 5N0H; -.
PDBsum; 5N0I; -.
ProteinModelPortal; C7C422; -.
SMR; C7C422; -.
ChEMBL; CHEMBL1667695; -.
GeneID; 11934636; -.
GeneID; 13913959; -.
GeneID; 13914060; -.
GeneID; 13914125; -.
GeneID; 13914405; -.
GeneID; 14258327; -.
GeneID; 14858116; -.
GeneID; 15414734; -.
GeneID; 17373266; -.
GeneID; 18983573; -.
GeneID; 20494087; -.
KEGG; ag:CAZ39946; -.
KO; K18780; -.
EvolutionaryTrace; C7C422; -.
PRO; PR:C7C422; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0008800; F:beta-lactamase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0017001; P:antibiotic catabolic process; IDA:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
Pfam; PF00753; Lactamase_B; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Hydrolase; Metal-binding;
Periplasm; Plasmid; Signal; Zinc.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 270 Metallo-beta-lactamase type 2.
/FTId=PRO_0000400316.
METAL 120 120 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:22713171,
ECO:0000269|PubMed:25815530}.
METAL 122 122 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:22713171,
ECO:0000269|PubMed:25815530}.
METAL 124 124 Zinc 2. {ECO:0000269|PubMed:22713171,
ECO:0000269|PubMed:25815530}.
METAL 189 189 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:22713171,
ECO:0000269|PubMed:25815530}.
METAL 208 208 Zinc 2. {ECO:0000269|PubMed:22713171,
ECO:0000269|PubMed:25815530}.
METAL 250 250 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:22713171,
ECO:0000269|PubMed:25815530}.
BINDING 211 211 Substrate. {ECO:0000269|PubMed:22713171}.
BINDING 220 220 Substrate; via amide nitrogen.
{ECO:0000269|PubMed:22713171}.
STRAND 34 36 {ECO:0000244|PDB:4HL2}.
STRAND 43 46 {ECO:0000244|PDB:4HL2}.
STRAND 49 55 {ECO:0000244|PDB:4HL2}.
STRAND 58 67 {ECO:0000244|PDB:4HL2}.
TURN 68 70 {ECO:0000244|PDB:4HL2}.
STRAND 71 82 {ECO:0000244|PDB:4HL2}.
STRAND 85 90 {ECO:0000244|PDB:4HL2}.
HELIX 95 108 {ECO:0000244|PDB:4HL2}.
STRAND 113 117 {ECO:0000244|PDB:4HL2}.
STRAND 120 122 {ECO:0000244|PDB:4HL2}.
HELIX 123 126 {ECO:0000244|PDB:4HL2}.
HELIX 129 134 {ECO:0000244|PDB:4HL2}.
STRAND 138 142 {ECO:0000244|PDB:4HL2}.
HELIX 143 148 {ECO:0000244|PDB:4HL2}.
HELIX 149 151 {ECO:0000244|PDB:4HL2}.
STRAND 158 161 {ECO:0000244|PDB:4HL2}.
STRAND 167 169 {ECO:0000244|PDB:4HL2}.
HELIX 171 173 {ECO:0000244|PDB:4HL2}.
STRAND 180 183 {ECO:0000244|PDB:4HL2}.
STRAND 187 190 {ECO:0000244|PDB:4HL2}.
STRAND 195 198 {ECO:0000244|PDB:4HL2}.
TURN 199 202 {ECO:0000244|PDB:4HL2}.
STRAND 203 205 {ECO:0000244|PDB:4HL2}.
TURN 207 209 {ECO:0000244|PDB:4HL2}.
HELIX 221 223 {ECO:0000244|PDB:3RKK}.
TURN 226 228 {ECO:0000244|PDB:4HL2}.
HELIX 229 239 {ECO:0000244|PDB:4HL2}.
STRAND 245 247 {ECO:0000244|PDB:4HL2}.
STRAND 249 251 {ECO:0000244|PDB:4HL2}.
HELIX 257 267 {ECO:0000244|PDB:4HL2}.
SEQUENCE 270 AA; 28499 MW; 1B6009120B945F14 CRC64;
MELPNIMHPV AKLSTALAAA LMLSGCMPGE IRPTIGQQME TGDQRFGDLV FRQLAPNVWQ
HTSYLDMPGF GAVASNGLIV RDGGRVLVVD TAWTDDQTAQ ILNWIKQEIN LPVALAVVTH
AHQDKMGGMD ALHAAGIATY ANALSNQLAP QEGMVAAQHS LTFAANGWVE PATAPNFGPL
KVFYPGPGHT SDNITVGIDG TDIAFGGCLI KDSKAKSLGN LGDADTEHYA ASARAFGAAF
PKASMIVMSH SAPDSRAAIT HTARMADKLR


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