Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P82974 (AMPD_CITFR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismCitrobacter freundii
Taxonomic identifier546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

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.

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
   Technical term3D-structure
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_0000164411

Sites

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

Secondary structure

......................................... 187
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P82974 [UniParc].

Last modified November 2, 2001. Version 1.
Checksum: DE3B49DBA20562AB

FASTA18720,847
        10         20         30         40         50         60 
MLLDEGWLAE ARRVPSPHYD CRPDDENPSL LVVHNISLPP GEFGGPWIDA LFTGTIDPNA 

        70         80         90        100        110        120 
HPYFAGIAHL RVSAHCLIRR DGEIVQYVPF DKRAWHAGVS SYQGRERCND FSIGIELEGT 

       130        140        150        160        170        180 
DTLAYTDAQY QQLAAVTNAL ITRYPAIANN MTGHCNIAPE RKTDPGPSFD WARFRALVTP 


SSHKEMT 

« 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: OS60.
[2]"Mutational analysis of the catalytic centre of the Citrobacter freundii AmpD N-acetylmuramyl-L-alanine amidase."
Genereux C., Dehareng D., Devreese B., Van Beeumen J., Frere J.M., Joris B.
Biochem. J. 377:111-120(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains."
Liepinsh E., Genereux C., Dehareng D., Joris B., Otting G.
J. Mol. Biol. 327:833-842(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, ZINC-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z14002 Genomic DNA. Translation: CAA78390.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3GNMR-A1-187[»]
2Y28X-ray1.80A/B/C1-187[»]
2Y2BX-ray1.90A/B/C1-187[»]
2Y2CX-ray1.80A/B/C1-187[»]
2Y2DX-ray2.00A/B/C1-187[»]
2Y2EX-ray2.00A/B/C1-187[»]
ProteinModelPortalP82974.
SMRP82974. 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...

Other

EvolutionaryTraceP82974.

Entry information

Entry nameAMPD_CITFR
AccessionPrimary (citable) accession number: P82974
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 65 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references