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Protein

Metallo-beta-lactamase type 2

Gene

blaNDM-1

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.1 Publication

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

Enzyme regulationi

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).2 Publications

Kineticsi

No activity detected against the monobactam aztreonam.1 Publication

Manual assertion based on experiment ini

  1. KM=8 µM for cefuroxime1 Publication
  2. KM=10 µM for cefotaxime1 Publication
  3. KM=10 µM for cephalothin1 Publication
  4. KM=12 µM for piperacillin1 Publication
  5. KM=16 µM for penicillin G1 Publication
  6. KM=22 µM for ampicillin1 Publication
  7. KM=49 µM for cefoxitin1 Publication
  8. KM=49 µM for meropenem1 Publication
  9. KM=77 µM for cefepime1 Publication
  10. KM=94 µM for imipenem1 Publication
  11. KM=181 µM for ceftazidime1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi120Zinc 1; via tele nitrogen2 Publications1
    Metal bindingi122Zinc 1; via pros nitrogen2 Publications1
    Metal bindingi124Zinc 22 Publications1
    Metal bindingi189Zinc 1; via tele nitrogen2 Publications1
    Metal bindingi208Zinc 22 Publications1
    Binding sitei211Substrate1 Publication1
    Binding sitei220Substrate; via amide nitrogen1 Publication1
    Metal bindingi250Zinc 2; via tele nitrogen2 Publications1

    GO - Molecular functioni

    • beta-lactamase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • antibiotic catabolic process Source: UniProtKB
    • response to antibiotic Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metallo-beta-lactamase type 2Curated (EC:3.5.2.61 Publication)
    Alternative name(s):
    B2 metallo-beta-lactamaseCurated
    Beta-lactamase type II1 Publication
    Metallo-beta-lactamase NDM-11 Publication
    Metallo-beta-lactamase type II1 Publication
    New Delhi metallo-beta-lactamase-11 Publication
    Short name:
    NDM-11 Publication
    Gene namesi
    Name:blaNDM-11 Publication
    Encoded oniPlasmid pKpANDM-10 Publication
    OrganismiKlebsiella pneumoniae
    Taxonomic identifieri573 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL1667695.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 28Sequence analysisAdd BLAST28
    ChainiPRO_000040031629 – 270Metallo-beta-lactamase type 2Add BLAST242

    Interactioni

    Subunit structurei

    Monomer.3 Publications

    Structurei

    Secondary structure

    1270
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi34 – 36Combined sources3
    Beta strandi43 – 46Combined sources4
    Beta strandi49 – 55Combined sources7
    Beta strandi58 – 67Combined sources10
    Turni68 – 70Combined sources3
    Beta strandi71 – 82Combined sources12
    Beta strandi85 – 90Combined sources6
    Helixi95 – 108Combined sources14
    Beta strandi113 – 117Combined sources5
    Beta strandi120 – 122Combined sources3
    Helixi123 – 126Combined sources4
    Helixi129 – 134Combined sources6
    Beta strandi138 – 142Combined sources5
    Helixi143 – 148Combined sources6
    Helixi149 – 151Combined sources3
    Beta strandi158 – 161Combined sources4
    Beta strandi167 – 169Combined sources3
    Helixi171 – 173Combined sources3
    Beta strandi180 – 183Combined sources4
    Beta strandi187 – 190Combined sources4
    Beta strandi195 – 198Combined sources4
    Turni199 – 202Combined sources4
    Beta strandi203 – 205Combined sources3
    Turni207 – 209Combined sources3
    Helixi221 – 223Combined sources3
    Turni226 – 228Combined sources3
    Helixi229 – 239Combined sources11
    Beta strandi245 – 247Combined sources3
    Beta strandi249 – 251Combined sources3
    Helixi257 – 267Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3PG4X-ray2.00A49-270[»]
    3Q6XX-ray1.30A/B29-270[»]
    3RKJX-ray2.00A/B39-270[»]
    3RKKX-ray2.35A/B39-270[»]
    3SBLX-ray2.31A39-270[»]
    3SFPX-ray2.27A/B/C/D39-270[»]
    3SPUX-ray2.10A/B/C/D/E27-270[»]
    3SRXX-ray2.50A/B37-270[»]
    3ZR9X-ray1.91A42-270[»]
    4EXSX-ray2.40A/B1-270[»]
    4EXYX-ray1.47A/B1-270[»]
    4EY2X-ray1.17A/B1-270[»]
    4EYBX-ray1.16A/B1-270[»]
    4EYFX-ray1.80A/B1-270[»]
    4EYLX-ray1.90A/B1-270[»]
    4GYQX-ray1.35A/B/C/D31-270[»]
    4GYUX-ray1.80A31-270[»]
    4H0DX-ray1.50A/B31-270[»]
    4HKYX-ray2.00A/B31-270[»]
    4HL1X-ray1.50A/B31-270[»]
    4HL2X-ray1.05A/B31-270[»]
    4RAMX-ray1.50A/B31-270[»]
    4RAWX-ray1.30A/B31-270[»]
    4RBSX-ray2.40A/B31-270[»]
    4RL0X-ray1.30A/B29-270[»]
    4RL2X-ray2.01A/B29-270[»]
    4RM5X-ray2.10A/B/C/D29-270[»]
    4U4LX-ray1.90A/B/C/D27-270[»]
    5A5ZX-ray2.60A/C29-270[»]
    ProteinModelPortaliC7C422.
    SMRiC7C422.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiC7C422.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KOiK18780.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001279. Metallo-B-lactamas.
    [Graphical view]
    PfamiPF00753. Lactamase_B. 1 hit.
    [Graphical view]
    SMARTiSM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    C7C422-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MELPNIMHPV AKLSTALAAA LMLSGCMPGE IRPTIGQQME TGDQRFGDLV
    60 70 80 90 100
    FRQLAPNVWQ HTSYLDMPGF GAVASNGLIV RDGGRVLVVD TAWTDDQTAQ
    110 120 130 140 150
    ILNWIKQEIN LPVALAVVTH AHQDKMGGMD ALHAAGIATY ANALSNQLAP
    160 170 180 190 200
    QEGMVAAQHS LTFAANGWVE PATAPNFGPL KVFYPGPGHT SDNITVGIDG
    210 220 230 240 250
    TDIAFGGCLI KDSKAKSLGN LGDADTEHYA ASARAFGAAF PKASMIVMSH
    260 270
    SAPDSRAAIT HTARMADKLR
    Length:270
    Mass (Da):28,499
    Last modified:September 22, 2009 - v1
    Checksum:i1B6009120B945F14
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FN396876 Genomic DNA. Translation: CAZ39946.1.
    RefSeqiWP_004201164.1. NZ_MCGW01000039.1.
    YP_005352173.1. NC_016980.1.
    YP_006958736.1. NC_019153.1.
    YP_006959150.1. NC_019158.1.
    YP_006959255.1. NC_019162.1.
    YP_006959318.1. NC_019163.1.
    YP_007195502.1. NC_019889.1.
    YP_007641427.1. NC_020811.1.
    YP_007936899.1. NC_021180.1.
    YP_008719663.1. NC_022609.1.
    YP_009023060.1. NC_023908.1.
    YP_009066437.1. NC_025105.1.
    YP_009071638.1. NC_025184.1.

    Genome annotation databases

    GeneIDi11934636.
    13913959.
    13914060.
    13914125.
    13914405.
    14258327.
    14858116.
    15414734.
    17373266.
    18983573.
    20471925.
    20494087.
    KEGGiag:CAZ39946.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FN396876 Genomic DNA. Translation: CAZ39946.1.
    RefSeqiWP_004201164.1. NZ_MCGW01000039.1.
    YP_005352173.1. NC_016980.1.
    YP_006958736.1. NC_019153.1.
    YP_006959150.1. NC_019158.1.
    YP_006959255.1. NC_019162.1.
    YP_006959318.1. NC_019163.1.
    YP_007195502.1. NC_019889.1.
    YP_007641427.1. NC_020811.1.
    YP_007936899.1. NC_021180.1.
    YP_008719663.1. NC_022609.1.
    YP_009023060.1. NC_023908.1.
    YP_009066437.1. NC_025105.1.
    YP_009071638.1. NC_025184.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3PG4X-ray2.00A49-270[»]
    3Q6XX-ray1.30A/B29-270[»]
    3RKJX-ray2.00A/B39-270[»]
    3RKKX-ray2.35A/B39-270[»]
    3SBLX-ray2.31A39-270[»]
    3SFPX-ray2.27A/B/C/D39-270[»]
    3SPUX-ray2.10A/B/C/D/E27-270[»]
    3SRXX-ray2.50A/B37-270[»]
    3ZR9X-ray1.91A42-270[»]
    4EXSX-ray2.40A/B1-270[»]
    4EXYX-ray1.47A/B1-270[»]
    4EY2X-ray1.17A/B1-270[»]
    4EYBX-ray1.16A/B1-270[»]
    4EYFX-ray1.80A/B1-270[»]
    4EYLX-ray1.90A/B1-270[»]
    4GYQX-ray1.35A/B/C/D31-270[»]
    4GYUX-ray1.80A31-270[»]
    4H0DX-ray1.50A/B31-270[»]
    4HKYX-ray2.00A/B31-270[»]
    4HL1X-ray1.50A/B31-270[»]
    4HL2X-ray1.05A/B31-270[»]
    4RAMX-ray1.50A/B31-270[»]
    4RAWX-ray1.30A/B31-270[»]
    4RBSX-ray2.40A/B31-270[»]
    4RL0X-ray1.30A/B29-270[»]
    4RL2X-ray2.01A/B29-270[»]
    4RM5X-ray2.10A/B/C/D29-270[»]
    4U4LX-ray1.90A/B/C/D27-270[»]
    5A5ZX-ray2.60A/C29-270[»]
    ProteinModelPortaliC7C422.
    SMRiC7C422.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    ChEMBLiCHEMBL1667695.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi11934636.
    13913959.
    13914060.
    13914125.
    13914405.
    14258327.
    14858116.
    15414734.
    17373266.
    18983573.
    20471925.
    20494087.
    KEGGiag:CAZ39946.

    Phylogenomic databases

    KOiK18780.

    Miscellaneous databases

    EvolutionaryTraceiC7C422.
    PROiC7C422.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001279. Metallo-B-lactamas.
    [Graphical view]
    PfamiPF00753. Lactamase_B. 1 hit.
    [Graphical view]
    SMARTiSM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiBLAN1_KLEPN
    AccessioniPrimary (citable) accession number: C7C422
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: September 22, 2009
    Last modified: November 30, 2016
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.2 Publications

    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.Curated

    Keywords - Technical termi

    3D-structure, Plasmid

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.