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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:08:15
Primary Accession Number DB01331
Secondary Accession Number
  • EXPT00897
Name Cefoxitin
Drug Type
  • Approved
  • Small Molecule
Description Cefoxitin is a semi-synthetic, broad-spectrum cepha antibiotic for intravenous administration. It is derived from cephamycin C, which is produced by Streptomyces lactamdurans.
Synonyms Not Available
Brand Names
  1. Mefoxin
  2. Mefoxitin
Brand Mixtures Not Available
Chemical IUPAC Name (6R,7S)-3-(carbamoyloxymethyl)-7-methoxy-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
Chemical Formula C16H17N3O7S2
Chemical Structure Structure
CAS Registry Number 35607-66-0
InChI Identifier InChI=1/C16H17N3O7S2/c1-25-16(18-10(20)5-9-3-2-4-27-9)13(23)19-11(12(21)22)8(6-26-15(17)24)7-28-14(16)19/h2-4,14H,5-7H2,1H3,(H2,17,24)(H,18,20)(H,21,22)/t14-,16+/m1/s1/f/h18,21H,17H2
InChI Key WZOZEZRFJCJXNZ-BPLXXLJGDR
KEGG Drug D02345 Link Image
KEGG Compound C06887 Link Image
PubChem Compound 441199 Link Image
PubChem Substance 10298759 Link Image
ChEBI ID Not Available
PharmGKB ID PA448856 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02128187 Link Image
RxList Link http://www.rxlist.com/cgi/generic/cefoxitin.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Cefoxitin Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 427.4520
Monoisotopic Molecular Weight 427.0508
State Solid
Melting Point Boiling Pt : 149.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.95e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.02 [SANGSTER (1993)] Source: PhysProp
Predicted LogP 0.22 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.34 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1I2W Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CO[C@]1(NC(=O)CC2=CC=CS2)[C@H]2SCC(COC(N)=O)=C(N2C1=O)C(O)=O
Canonical SMILES COC1(NC(=O)CC2=CC=CS2)C2SCC(COC(N)=O)=C(N2C1=O)C(O)=O
Drug Category
  • Anti-Bacterial Agents
  • Antibacterial Agents
  • Cephalosporins
ATC Codes
AHFS Codes
  • 08:12.07.12
Indication For the treatment of serious infections caused by susceptible strains microorganisms.
Pharmacology Cefoxitin is a cephamycin antibiotic often grouped with the second-generation cephalosporins. It is active against a broad range of gram-negative bacteria including anaerobes. The methoxy group in the 7a position provides cefoxitin with a high degree of stability in the presence of beta-lactamases, both penicillinases and cephalosporinases, of gram-negative bacteria.
Mechanism of Action The bactericidal action of cefoxitin results from inhibition of cell wall synthesis.
Absorption Not Available
Toxicity The acute intravenous LD50 in the adult female mouse and rabbit was about 8.0 g/kg and greater than 1.0 g/kg, respectively. The acute intraperitoneal LD50 in the adult rat was greater than 10.0 g/kg.
Protein Binding Not Available
Biotransformation Minimal (approximately 85 percent of cefoxitin is excreted unchanged by the kidneys over a 6-hour period).
Half Life The half-life after an intravenous dose is 41 to 59 minutes.
Dosage Forms
Form Route
Powder, for solution Intramuscular
Powder, for solution Intravenous
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The cephalosporin increases the anticoagulant effect
Amikacin Increased risk of nephrotoxicity
Anisindione The cephalosporin increases the anticoagulant effect
Dicumarol The cephalosporin increases the anticoagulant effect
Gentamicin Increased risk of nephrotoxicity
Kanamycin Increased risk of nephrotoxicity
Neomycin Increased risk of nephrotoxicity
Netilmicin Increased risk of nephrotoxicity
Probenecid Probenecid increases the antibiotic's level
Streptomycin Increased risk of nephrotoxicity
Tobramycin Increased risk of nephrotoxicity
Warfarin The cephalosporin increases the anticoagulant effect
Food Interactions Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. Penicillin-binding proteins 1A/1B
  2. Beta-lactamase
  3. Beta-lactamase CTX-M-9a
Drug Target 1 [top]
Target 1 ID 633
Target 1 Name Penicillin-binding proteins 1A/1B
Target 1 Synonyms Not Available
Target 1 Gene Name pbpA
Target 1 Protein Sequence >Penicillin-binding proteins 1A/1B 
MTERKREHKDRKQNKNSPKNQSKVTKFLKWFFIGILLLGITAVTVVGIYVLSIIRSSPEL
DVQAIQSLNQPSILYDDQGNFMDNVITREQRYVVKSEEIPDNLKKAFVAIEDERFYEHKG
IDIKRIFGVIASNIKGKLSGSNTVQGASTITQQLIKNAVLTNEVSYERKIKEMYLALELE
KHLSKDEILTTYLNTIPMGGYQYGVSAAAQRFFSKNVSDLNLVECAYLGGLTQAPTSYDG
LSEANKENPSRYLNRTKSVLFKMHELGYISSEQYNDAINEIDTNGIKFTPNNKLSKTNFE
WFTRPAITQVKQDLMDKYKYTQEEVDKLIANGGLKIYTSMDRNLQNNVQKVLDDPNNYKA
ITNNPNEKNEDGVYKLQASATIIDYKTGHVKALVGGRGEQPAMSHNRAYYDLKSIGSATK
PLTVYGPAIDLGLGGAGSVVNDSPLSNKELSSTGYKDQPKNEYNSYRGPLTFREAIKISS
NLAAIKVANEVGVSNSIAYGEKLGLVYGPHSRGISTTALGQFQNDPNNPDGGNTYTLASA
FGVFGNNGVKTNAKLYTKVLDSHGNVILDTSTPEETKIFSPQASYIVYDMLKDQVESGSA
KSAKFGNIPVAGKTGTTTGDKDYLFAGLTPYYSAAIWIGYDKPREMRTSSGTVTSPIFGK
IMGLAHKDLQYKEVDNLVE
Target 1 Number of Residues 690
Target 1 Molecular Weight 75178
Target 1 Theoretical pI 9.09
Target 1 GO Classification
Function
binding
drug binding
penicillin binding
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
hydrolase activity
peptidase activity
catalytic activity
Process
cellular physiological process
cell organization and biogenesis
external encapsulating structure organization and biogenesis
cell wall organization and biogenesis
cell wall organization and biogenesis (sensu Bacteria)
cell wall biosynthesis (sensu Bacteria)
response to stimulus
response to abiotic stimulus
response to chemical stimulus
response to drug
response to antibiotic
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
cellular carbohydrate metabolism
peptidoglycan metabolism
peptidoglycan biosynthesis
Component
cell
external encapsulating structure
cell wall
cell wall (sensu Bacteria)
Target 1 General Function Cell wall/membrane/envelope biogenesis
Target 1 Specific Function Not Available
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 30-52
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 18145626 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q8XJ01 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name Q8XJ01_CLOPE Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >2040 bp 
ATGACTGAAAGAAAAAGAGAGCATAAAGATAGAAAGCAGAATAAAAATTCACCTAAAAAT
CAATCGAAAGTAACAAAATTTTTGAAATGGTTCTTTATAGGGATTCTGCTTCTAGGGATA
ACTGCCGTAACAGTAGTTGGAATTTACGTTCTTTCTATTATACGTTCATCTCCAGAGTTA
GATGTTCAGGCAATTCAATCTCTAAATCAGCCATCCATTCTTTACGATGATCAGGGAAAC
TTTATGGATAATGTTATAACTCGTGAACAACGTTATGTAGTTAAATCTGAAGAGATACCT
GATAACTTAAAAAAGGCTTTTGTAGCTATTGAAGACGAAAGATTTTATGAGCATAAAGGA
ATAGACATTAAAAGAATTTTTGGGGTAATAGCTTCTAATATTAAAGGTAAACTTTCAGGA
AGTAATACAGTTCAAGGGGCTTCAACCATAACTCAGCAACTTATAAAAAATGCCGTACTT
ACTAATGAAGTTAGTTATGAAAGAAAAATTAAAGAAATGTACTTAGCTTTGGAATTAGAA
AAGCACCTTTCAAAAGATGAAATCCTTACTACGTATTTAAATACAATTCCTATGGGTGGA
TACCAATATGGGGTTAGCGCAGCTGCTCAAAGATTTTTTAGTAAGAATGTTTCAGATTTG
AATTTAGTTGAGTGCGCTTATTTAGGAGGACTTACTCAAGCACCAACTTCTTATGATGGT
CTTTCAGAAGCAAATAAAGAAAATCCAAGTAGATATTTAAATAGAACTAAATCTGTACTA
TTTAAAATGCATGAACTTGGATATATTTCAAGTGAACAATATAATGACGCAATAAATGAA
ATTGACACAAATGGTATAAAATTCACACCAAATAATAAATTAAGTAAAACTAACTTTGAG
TGGTTCACAAGACCAGCTATAACTCAAGTTAAACAAGACTTAATGGATAAATATAAATAT
ACACAAGAGGAAGTTGACAAACTTATAGCTAATGGTGGATTAAAAATCTATACTTCAATG
GATAGAAATCTTCAAAATAATGTTCAAAAAGTTTTAGATGATCCAAATAACTATAAAGCT
ATAACTAATAATCCTAATGAAAAAAATGAAGATGGTGTTTATAAATTACAAGCATCTGCC
ACAATAATAGACTATAAAACAGGCCATGTTAAGGCTTTAGTTGGAGGAAGAGGGGAACAA
CCTGCTATGTCTCACAATAGAGCTTATTATGATTTAAAATCTATAGGTTCTGCAACAAAA
CCATTAACAGTTTATGGTCCTGCTATTGATTTAGGACTTGGTGGCGCTGGCTCTGTAGTA
AATGATTCTCCATTAAGTAATAAAGAGTTATCTTCTACAGGATATAAAGATCAACCTAAG
AATGAATACAATAGTTATAGAGGCCCTTTAACTTTTAGAGAAGCAATTAAAATCTCTAGT
AACTTAGCAGCCATAAAAGTTGCTAATGAAGTAGGTGTTTCAAACTCTATAGCTTATGGA
GAAAAATTAGGTCTTGTTTATGGACCTCATTCTAGAGGTATTTCCACAACAGCCTTAGGT
CAATTCCAAAATGACCCTAATAATCCTGATGGAGGAAATACTTATACTCTAGCTTCAGCC
TTCGGTGTTTTTGGTAATAACGGTGTTAAAACAAATGCTAAATTATATACAAAGGTATTA
GATTCTCATGGAAATGTAATTCTTGATACAAGTACTCCAGAAGAAACTAAAATATTTAGT
CCTCAAGCGTCTTATATAGTTTATGATATGCTTAAGGATCAAGTAGAAAGTGGCTCTGCA
AAATCTGCTAAATTTGGTAATATTCCTGTGGCGGGTAAAACAGGAACTACTACTGGAGAT
AAAGACTATTTATTTGCAGGATTAACTCCATATTATTCTGCGGCTATTTGGATTGGATAT
GATAAGCCTAGAGAAATGAGAACTAGTAGTGGTACTGTTACCTCTCCTATTTTCGGAAAA
ATAATGGGCTTAGCTCATAAAGACTTACAGTACAAAGAGGTTGACAACCTAGTGGAATAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Shimizu T, Ohtani K, Hirakawa H, Ohshima K, Yamashita A, Shiba T, Ogasawara N, Hattori M, Kuhara S, Hayashi H: Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):996-1001. Epub 2002 Jan 15. [PubMed Link Image]
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 2700
Target 2 Name Beta-lactamase
Target 2 Synonyms
  1. Beta-lactamase precursor
  2. EC 3.5.2.6
  3. Penicillinase
Target 2 Gene Name penP
Target 2 Protein Sequence >Beta-lactamase precursor 
MKLWFSTLKLKKAAAVLLFSCVALAGCANNQTNASQPAEKNEKTEMKDDFAKLEEQFDAK
LGIFALDTGTNRTVAYRPDERFAFASTIKALTVGVLLQQKSIEDLNQRITYTRDDLVNYN
PITEKHVDTGMTLKELADASLRYSDNAAQNLILKQIGGPESLKKELRKIGDEVTNPERFE
PELNEVNPGETQDTSTARALVTSLRAFALEDKLPSEKRELLIDWMKRNTTGDALIRAGVP
DGWEVADKTGAASYGTRNDIAIIWPPKGDPVVLAVLSSRDKKDAKYDDKLIAEATKVVMK
ALNMNGK
Target 2 Number of Residues 312
Target 2 Molecular Weight 33996
Target 2 Theoretical pI 5.61
Target 2 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
beta-lactamase activity
Process
physiological process
metabolism
cellular metabolism
drug metabolism
antibiotic metabolism
antibiotic catabolism
beta-lactam antibiotic catabolism
response to stimulus
response to abiotic stimulus
response to chemical stimulus
response to drug
response to antibiotic
Component
Not Available
Target 2 General Function Defense mechanisms and antibiotic degradation
Target 2 Specific Function A beta-lactam + H(2)O = a substituted beta- amino acid
Target 2 Pathways
Name SMPDB Link KEGG Link
Penicillins and cephalosporins biosynthesis map00311 Link Image
Target 2 Reactions
  • a beta-lactam + H2O = a substituted beta-amino acid
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-26
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 39575 Link Image
Target 2 UniProtKB/Swiss-Prot ID P00808 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name BLAC_BACLI Link Image
Target 2 PDB ID 1I2W Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cell membrane
  • lipid-anchor (Probable)
Target 2 Gene Sequence >924 bp 
ATGAAATTATGGTTCAGTACTTTAAAACTGAAAAAGGCTGCAGCAGTGTTGCTTTTCTCT
TGCGTCGCGCTTGCAGGATGCGCTAACAATCAAACGAATGCCTCGCAACCTGCCGAGAAG
AATGAAAAGACGGAGATGAAAGATGATTTTGCAAAACTTGAGGAACAATTTGATGCAAAA
CTCGGGATCTTTGCATTGGATACAGGTACAAACCGGACGGTAGCGTATCGGCCGGATGAG
CGTTTTGCTTTTGCTTCGACGATTAAGGCTTTAACTGTAGGCGTGCTTTTGCAACAGAAA
TCAATAGAAGATCTGAACCAGAGAATAACATATACACGTGATGATCTTGTAAACTACAAC
CCGATTACGGAAAAGCACGTTGATACGGGAATGACGCTCAAAGAGCTTGCGGATGCTTCG
CTTCGATATAGTGACAATGCGGCACAGAATCTCATTCTTAAACAAATTGGCGGACCTGAA
AGTTTGAAAAAGGAACTGAGGAAGATTGGTGATGAGGTTACAAATCCCGAACGATTCGAA
CCAGAGTTAAATGAAGTGAATCCGGGTGAAACTCAGGATACCAGTACAGCAAGAGCACTT
GTCACAAGCCTTCGAGCCTTTGCTCTTGAAGATAAACTTCCAAGTGAAAAACGCGAGCTT
TTAATCGATTGGATGAAACGAAATACCACTGGAGACGCCTTAATCCGTGCCGGTGTGCCG
GACGGTTGGGAAGTGGCTGATAAAACTGGAGCGGCATCATATGGAACCCGGAATGACATT
GCCATCATTTGGCCGCCAAAAGGAGATCCTGTCGTTCTTGCAGTATTATCCAGCAGGGAT
AAAAAGGACGCCAAGTATGATGATAAACTTATTGCAGAGGCAACAAAGGTGGTAATGAAA
GCCTTAAACATGAACGGCAAATAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Fonze E, Vanhove M, Dive G, Sauvage E, Frere JM, Charlier P: Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin. Biochemistry. 2002 Feb 12;41(6):1877-85. [PubMed Link Image]
  2. Knox JR, Moews PC: Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration. J Mol Biol. 1991 Jul 20;220(2):435-55. [PubMed Link Image]
  3. Moews PC, Knox JR, Dideberg O, Charlier P, Frere JM: Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution. Proteins. 1990;7(2):156-71. [PubMed Link Image]
  4. Wittman V, Wong HC: Regulation of the penicillinase genes of Bacillus licheniformis: interaction of the pen repressor with its operators. J Bacteriol. 1988 Jul;170(7):3206-12. [PubMed Link Image]
  5. Meadway RJ: The amino acid sequence of penicillinase from Bacillus licheniformis. Biochem J. 1969 Nov;115(3):12P-13P. [PubMed Link Image]
  6. Neugebauer K, Sprengel R, Schaller H: Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium. Nucleic Acids Res. 1981 Jun 11;9(11):2577-88. [PubMed Link Image]
  7. Izui K, Nielsen JB, Caulfield MP, Lampen JO: Large exopenicillinase, initial extracellular form detected in cultures of Bacillus licheniformis. Biochemistry. 1980 Apr 29;19(9):1882-6. [PubMed Link Image]
  8. Kroyer J, Chang S: The promoter-proximal region of the Bacillus licheniformis penicillinase gene: Nucleotide sequence and predicted leader peptide sequence. Gene. 1981 Dec;15(4):343-7. [PubMed Link Image]
Target 2 Drug References
  1. d'Azevedo PA, Goncalves AL, Musskopf MI, Ramos CG, Dias CA: Laboratory tests in the detection of extended spectrum beta-lactamase production: National Committee for Clinical Laboratory Standards (NCCLS) screening test, the E-test, the double disk confirmatory test, and cefoxitin susceptibility testing. Braz J Infect Dis. 2004 Oct;8(5):372-7. Epub 2005 Mar 17. [PubMed Link Image]
  2. Ke YY, Lin TH: A theoretical study on the activation of Ser70 in the acylation mechanism of cephalosporin antibiotics. Biophys Chem. 2005 Apr 22;114(2-3):103-13. Epub 2004 Nov 30. [PubMed Link Image]
  3. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  4. Song W, Lee KM, Kim HS, Kim JS, Kim J, Jeong SH, Roh KH: Clonal spread of both oxyimino-cephalosporin- and cefoxitin-resistant Klebsiella pneumoniae isolates co-producing SHV-2a and DHA-1 beta-lactamase at a burns intensive care unit. Int J Antimicrob Agents. 2006 Dec;28(6):520-4. Epub 2006 Nov 13. [PubMed Link Image]
  5. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 4629
Target 3 Name Beta-lactamase CTX-M-9a
Target 3 Synonyms
  1. Beta-lactamase
  2. Betalactamase CTX-M-9
  3. CTX-M-9 beta-lactamase
Target 3 Gene Name blaCTX-M-9a
Target 3 Protein Sequence >Beta-lactamase CTX-M-9a 
MVTKRVQRMMFAAAACIPLLLGSAPLYAQTSAVQQKLAALEKSSGGRLGVALIDTADNTQ
VLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTM
TLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDP
RDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTAGDKTGS
GDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLASAARIIAEGL
Target 3 Number of Residues 295
Target 3 Molecular Weight 30952
Target 3 Theoretical pI 9.38
Target 3 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
beta-lactamase activity
Process
physiological process
metabolism
cellular metabolism
drug metabolism
antibiotic metabolism
antibiotic catabolism
beta-lactam antibiotic catabolism
response to stimulus
response to abiotic stimulus
response to chemical stimulus
response to drug
response to antibiotic
Component
Not Available
Target 3 General Function Involved in beta-lactamase activity
Target 3 Specific Function Not Available
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Essential
Target 3 GenBank ID Protein Not Available
Target 3 UniProtKB/Swiss-Prot ID Q9L5C8 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name Q9L5C8_ECOLI Link Image
Target 3 PDB ID 1YMX Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Cytoplasmic
Target 3 Gene Sequence >876 bp 
ATGGTGACAAAGAGAGTGCAACGGATGATGTTCGCGGCGGCGGCGTGCATTCCGCTGCTG
CTGGGCAGCGCGCCGCTTTATGCGCAGACGAGTGCGGTGCAGCAAAAGCTGGCGGCGCTG
GAGAAAAGCAGCGGAGGGCGGCTGGGCGTCGCGCTCATCGATACCGCAGATAATACGCAG
GTGCTTTATCGCGGTGATGAACGCTTTCCAATGTGCAGTACCAGTAAAGTTATGGCGGCC
GCGGCGGTGCTTAAGCAGAGTGAAACGCAAAAGCAGCTGCTTAATCAGCCTGTCGAGATC
AAGCCTGCCGATCTGGTTAACTACAATCCGATTGCCGAAAAACACGTCAACGGCACAATG
ACGCTGGCAGAGCTGAGCGCGGCCGCGTTGCAGTACAGCGACAATACCGCCATGAACAAA
TTGATTGCCCAGCTCGGTGGCCCGGGAGGCGTGACGGCTTTTGCCCGCGCGATCGGCGAT
GAGACGTTTCGTCTGGATCGCACTGAACCTACGCTGAATACCGCCATTCCCGGCGACCCG
AGAGACACCACCACGCCGCGGGCGATGGCACAGACGTTGCGTCAGCTTACGCTGGGTCAT
GCGCTGGGCGAAACCCAGCGGGCGCAGTTGGTGACGTGGCTCAAAGGCAATACGACCGGC
GCAGCCAGCATTCGGGCCGGCTTACCGACGTCGTGGACTGCAGGTGATAAGACCGGCAGC
GGCGACTACGGCACCACCAATGATATTGCGGTGATCTGGCCGCAGGGTCGTGCGCCGCTG
GTTCTGGTGACCTATTTTACCCAGCCGCAACAGAACGCAGAGAGCCGCCGCGATGTGCTG
GCTTCAGCGGCGAGAATCATCGCCGAAGGGCTGTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Sabate M, Tarrago R, Navarro F, Miro E, Verges C, Barbe J, Prats G: Cloning and sequence of the gene encoding a novel cefotaxime-hydrolyzing beta-lactamase (CTX-M-9) from Escherichia coli in Spain. Antimicrob Agents Chemother. 2000 Jul;44(7):1970-3. [PubMed Link Image]
  2. Chanawong A, M'Zali FH, Heritage J, Xiong JH, Hawkey PM: Three cefotaximases, CTX-M-9, CTX-M-13, and CTX-M-14, among Enterobacteriaceae in the People's Republic of China. Antimicrob Agents Chemother. 2002 Mar;46(3):630-7. [PubMed Link Image]
  3. Saladin M, Cao VT, Lambert T, Donay JL, Herrmann JL, Ould-Hocine Z, Verdet C, Delisle F, Philippon A, Arlet G: Diversity of CTX-M beta-lactamases and their promoter regions from Enterobacteriaceae isolated in three Parisian hospitals. FEMS Microbiol Lett. 2002 Apr 9;209(2):161-8. [PubMed Link Image]
  4. Sabate M, Navarro F, Miro E, Campoy S, Mirelis B, Barbe J, Prats G: Novel complex sul1-type integron in Escherichia coli carrying bla(CTX-M-9). Antimicrob Agents Chemother. 2002 Aug;46(8):2656-61. [PubMed Link Image]
Target 3 Drug References Not Available

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.