N-acetylmuramoyl-L-alanine amidase AmiB (P26365)

Identification
Name:N-acetylmuramoyl-L-alanine amidase AmiB
Synonyms:Not Available
Gene Name:amiB
Enzyme Class:
Biological Properties
General Function:Involved in N-acetylmuramoyl-L-alanine amidase activity
Specific Function:Cell-wall hydrolase probably involved in cell-wall hydrolysis, septation or recycling
Cellular Location:Secreted (Potential)
SMPDB Pathways:Not Available
KEGG Pathways:
  • Cationic antimicrobial peptide (CAMP) resistance eco01503
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylmuramoyl-Ala + 1.0Water ↔ 1.0N-Acetyl-D-muramoate + 1.0L-Alanine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide + 1.0Water → 1.0L-Alanine-D-glutamate-meso-2,6-diaminoheptanedioate-D-alanine + 1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide + 1.0Water → 1.0L-alanine-D-glutamate-meso-2,6-diaminoheptanedioate + 1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00161L-AlanineMetaboCard
ECMDB21240L-alanine-D-glutamate-meso-2,6-diaminoheptanedioateMetaboCard
ECMDB21239L-Alanine-D-glutamate-meso-2,6-diaminoheptanedioate-D-alanineMetaboCard
ECMDB21248N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramic acidMetaboCard
ECMDB21249N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptideMetaboCard
ECMDB21250N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptideMetaboCard
ECMDB20176N-Acetyl-D-muramoateMetaboCard
ECMDB20178N-Acetylmuramoyl-AlaMetaboCard
ECMDB00494WaterMetaboCard
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 linear amides
N-acetylmuramoyl-L-alanine amidase activity
Process
aminoglycan metabolic process
carbohydrate metabolic process
glycosaminoglycan metabolic process
metabolic process
peptidoglycan catabolic process
peptidoglycan metabolic process
polysaccharide metabolic process
primary metabolic process
Gene Properties
Blattner:b4169
Gene OrientationClockwise
Centisome Percentage:94.71
Left Sequence End4394088
Right Sequence End4395425
Gene Sequence:
>1338 bp
ATGCACTCTCAAATCTGGGTTGTGAGCACGCTGCTTATCAGCATCGTGTTAATTGTACTG
ACCATCGTGAAGTTCAAATTCCACCCGTTTCTGGCGCTGTTGCTGGCCAGCTTCTTCGTG
GGAACGATGATGGGCATGGGGCCACTGGATATGGTAAATGCTATTGAAAGTGGAATTGGC
GGAACGCTGGGGTTCCTCGCAGCGGTTATCGGCCTTGGCACGATACTGGGAAAAATGATG
GAAGTATCCGGGGCCGCAGAAAGAATTGGTCTGACACTTCAACGCTGCCGCTGGCTTTCA
GTTGATGTCATTATGGTGCTGGTTGGCCTGATTTGTGGCATCACGCTGTTTGTTGAAGTG
GGCGTCGTGCTATTGATTCCTCTGGCTTTTTCAATTGCCAAAAAAACCAATACCTCATTA
TTAAAGCTTGCCATTCCGCTATGTACCGCATTGATGGCAGTGCACTGCGTGGTTCCTCCA
CATCCGGCTGCTTTATATGTTGCCAATAAGCTGGGCGCAGATATCGGTTCGGTGATCGTC
TACGGTTTGCTGGTTGGGCTGATGGCATCACTGATCGGTGGCCCACTTTTCCTTAAATTT
CTGGGTCAACGACTGCCCTTTAAACCTGTACCCACAGAGTTTGCAGATCTCAAAGTTCGC
GATGAAAAAACACTACCGTCATTAGGCGCAACGTTATTCACCATACTGCTACCCATTGCG
CTGATGTTGGTTAAAACGATTGCCGAATTGAATATGGCGCGTGAGAGTGGTTTGTATATC
TTGGTTGAGTTTATTGGCAACCCTATCACTGCCATGTTTATCGCCGTGTTTGTCGCCTAT
TATGTGTTGGGTATACGCCAGCATATGAGCATGGGGACGATGCTCACACATACGGAAAAT
GGCTTCGGTTCTATTGCTAATATTTTGCTGATTATCGGGGCCGGAGGCGCATTCAACGCC
ATTTTAAAAAGCAGCAGTCTCGCTGATACGCTGGCAGTTATTCTCTCCAATATGCATATG
CACCCGATTCTTCTGGCCTGGTTAGTGGCTCTTATTCTGCATGCGGCAGTGGGCTCCGCT
ACCGTGGCAATGATGGGGGCAACGGCAATTGTTGCACCCATGCTGCCGCTGTATCCCGAC
ATCAGCCCGGAAATTATTGCGATTGCTATCGGTTCAGGTGCAATTGGCTGCACTATCGTT
ACGGACTCGCTTTTCTGGCTAGTGAAGCAATATTGCGGCGCTACGCTCAATGAAACATTT
AAATACTATACGACAGCGACATTTATCGCTTCAGTCGTCGCTCTGGCGGGCACATTCCTG
CTGTCATTTATCATCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:445
Protein Molecular Weight:47985
Protein Theoretical pI:10
Signaling Regions:
  • 1-22
Transmembrane Regions:
  • None
Protein Sequence:
>N-acetylmuramoyl-L-alanine amidase AmiB
MMYRIRNWLVATLLLLCTPVGAATLSDIQVSNGNQQARITLSFIGDPDYAFSHQSKRTVA
LDIKQTGVIQGLPLLFSGNNLVKAIRSGTPKDAQTLRLVVDLTENGKTEAVKRQNGSNYT
VVFTINADVPPPPPPPPVVAKRVETPAVVAPRVSEPARNPFKTESNRTTGVISSNTVTRP
AARATANTGDKIIIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLLNDDPMFKGVL
TRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMASWLE
QHEKQSELLGGAGDVLANSQSDPYLSQAVLDLQFGHSQRVGYDVATSMISQLQRIGEIHK
RRPEHASLGVLRSPDIPSVLVETGFISNNSEERLLASDDYQQQLAEAIYKGLRNYFLAHP
MQSAPQGATAQTASTVTTPDRTLPN
References
External Links:
ResourceLink
Uniprot ID:P26365
Uniprot Name:AMIB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1799764
Ecogene ID:EG11363
Ecocyc:EG11363
ColiBase:b4169
Kegg Gene:b4169
EchoBASE ID:EB1338
CCDB:AMIB_ECOLI
BacMap:16131991
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Tsui, H. C., Zhao, G., Feng, G., Leung, H. C., Winkler, M. E. (1994). "The mutL repair gene of Escherichia coli K-12 forms a superoperon with a gene encoding a new cell-wall amidase." Mol Microbiol 11:189-202. Pubmed: 7511774
  • Tsui, H. T., Mandavilli, B. S., Winkler, M. E. (1992). "Nonconserved segment of the MutL protein from Escherichia coli K-12 and Salmonella typhimurium." Nucleic Acids Res 20:2379. Pubmed: 1594459