Metallo-beta-lactamase L1

Details

Name
Metallo-beta-lactamase L1
Synonyms
  • 3.5.2.6
  • Beta-lactamase type II
  • Penicillinase
Gene Name
Not Available
Organism
Pseudomonas maltophilia
Amino acid sequence
>lcl|BSEQ0012346|Metallo-beta-lactamase L1
MRSTLLAFALAVALPAAHTSAAEVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLT
ALLVQTPDGAVLLDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRR
TGAKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIVFTAHFMAG
HTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPHLIEDYRRSFATVRALPCD
VLLTPHPGASNWDYAAGARAGAKALTCKAYADAAEQKFDGQLAKETAGAR
Number of residues
290
Molecular Weight
30800.635
Theoretical pI
6.92
GO Classification
Functions
beta-lactamase activity / zinc ion binding
Processes
antibiotic catabolic process / response to antibiotic
Components
periplasmic space
General Function
Zinc ion binding
Specific Function
Has a high activity against imipenem.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0006545|873 bp
ATGCGTTCTACCCTGCTCGCCTTCGCCCTGGCCGTCGCTCTTCCGGCCGCCCACACCAGC
GCCGCCGAAGTACCACTGCCGCAGCTGCGGGCCTACACCGTGGACGCCTCGTGGCTGCAG
CCGATGGCACCGCTGCAGATCGCCGACCACACCTGGCAGATCGGCACCGAGGACCTGACC
GCGCTGCTTGTGCAGACCCCCGACGGCGCGGTGCTGCTCGACGGCGGCATGCCGCAGATG
GCCAGCCACCTGCTGGACAACATGAAGGCGCGTGGCGTGACGCCTCGGGATCTGCGGCTG
ATCCTGCTCAGCCACGCACACGCCGACCATGCCGGACCGGTGGCGGAGCTGAAGCGCCGT
ACGGGCGCCAAAGTGGCGGCCAACGCCGAATCGGCGGTGCTGCTGGCGCGTGGCGGCAGC
GATGACCTGCACTTCGGCGATGGCATCACCTACCCGCCTGCCAATGCAGACCGCATCGTC
ATGGATGGTGAAGTGATCACGGTGGGCGGCATCGTGTTCACCGCGCACTTCATGGCGGGG
CACACCCCGGGCAGCACCGCGTGGACCTGGACCGATACCCGCAATGGCAAGCCGGTGCGC
ATCGCCTACGCCGACAGCCTGAGTGCACCGGGCTACCAGCTGCAGGGAAACCCCCGTTAT
CCGCACCTGATCGAGGATTACAGGCGCAGCTTCGCGACGGTGCGGGCGCTGCCTTGCGAC
GTGTTGCTGACACCGCATCCGGGTGCCAGCAACTGGGACTACGCCGCGGGTGCCAGGGCC
GGTGCCAAGGCACTGACCTGCAAGGCCTACGCGGATGCGGCAGAACAGAAATTCGACGGG
CAGCTGGCCAAGGAAACGGCCGGGGCCCGCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP52700
UniProtKB Entry NameBLA1_STEMA
GenBank Gene IDX75074
General References
  1. Walsh TR, Hall L, Assinder SJ, Nichols WW, Cartwright SJ, MacGowan AP, Bennett PM: Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia. Biochim Biophys Acta. 1994 Jun 21;1218(2):199-201. [Article]
  2. Bicknell R, Emanuel EL, Gagnon J, Waley SG: The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275. Biochem J. 1985 Aug 1;229(3):791-7. [Article]
  3. Ullah JH, Walsh TR, Taylor IA, Emery DC, Verma CS, Gamblin SJ, Spencer J: The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution. J Mol Biol. 1998 Nov 20;284(1):125-36. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04740Moxalactam (hydrolyzed)experimentalunknownDetails
DB07939N-(3-MERCAPTOPROPANOYL)-D-ALANINEexperimentalunknownDetails
DB080694-AMINO-5-(2-METHYLPHENYL)-2,4-DIHYDRO-3H-1,2,4-TRIAZOLE-3-THIONEexperimentalunknownDetails
DB02032EpicaptoprilexperimentalunknownDetails
DB08199N-[(BENZYLOXY)CARBONYL]-L-CYSTEINYLGLYCINEexperimentalunknownDetails
DB023651,10-PhenanthrolineexperimentalunknownDetails
DB087022,5-DIPHENYLFURAN-3,4-DICARBOXYLIC ACIDexperimentalunknownDetails