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P82973 (AMPD_ENTCL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD

EC=3.5.1.28
Alternative name(s):
N-acetylmuramoyl-L-alanine amidase
Gene names
Name:ampD
OrganismEnterobacter cloacae
Taxonomic identifier550 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in both cell wall peptidoglycans recycling and beta-lactamase induction. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety By similarity.

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Cofactor

Zinc; required for amidase activity By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1871871,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
PRO_0000164412

Sites

Active site1161Proton acceptor By similarity
Metal binding341Zinc; catalytic By similarity
Metal binding1541Zinc; catalytic By similarity
Metal binding1641Zinc; catalytic By similarity
Site1621Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P82973 [UniParc].

Last modified November 2, 2001. Version 1.
Checksum: F1D23B55B84E71C8

FASTA18720,839
        10         20         30         40         50         60 
MLLENGWLVD ARHVPSPHHD CRPEDEKPTL LVVHNISLPP GEFGGPWIDA LFTGTIDPDA 

        70         80         90        100        110        120 
HPFFAEIAHL ALSADCLIRR DGEVVQYVPF DKRAWHAGVS MYQGRERCND FSIGIELEGT 

       130        140        150        160        170        180 
DTTPYTDAQY EKLVAVTQTL IGRYPAIADN ITGHSDIAPE RKTDPGPAFD WSRFHAMLTT 


SSDKEIT 

« Hide

References

[1]"Sequences of wild-type and mutant ampD genes of Citrobacter freundii and Enterobacter cloacae."
Kopp U., Wiedemann B., Lindquist S., Normark S.
Antimicrob. Agents Chemother. 37:224-228(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z14003 Genomic DNA. Translation: CAA78391.1.
PIRA48901.

3D structure databases

ProteinModelPortalP82973.
SMRP82973. Positions 1-187.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
[Graphical view]
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMPD_ENTCL
AccessionPrimary (citable) accession number: P82973
Secondary accession number(s): Q00831
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 2, 2001
Last modified: October 16, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families