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P44624 (AMPD_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. 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
Ordered Locus Names:HI_0300
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length184 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
   Technical termComplete proteome
Reference proteome
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 – 1841841,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
PRO_0000164414

Sites

Active site1201Proton acceptor By similarity
Metal binding381Zinc; catalytic By similarity
Metal binding1591Zinc; catalytic By similarity
Metal binding1691Zinc; catalytic By similarity
Site1671Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P44624 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B7A035527E328401

FASTA18421,448
        10         20         30         40         50         60 
MRKIKDIEKG LLTDCRQIQS PHFDKRPNPQ DISLLVIHYI SLPPEQFGGG YVDDFFQGKL 

        70         80         90        100        110        120 
DPKIHPYFAE IYQMRVSAHC LIERNGRITQ YVNFNDRAWH AGVSNFQGRE KCNDFAIGIE 

       130        140        150        160        170        180 
LEGSNEQPFT DAQYFSLQEL TNVIMKSYPK ITKDRIVGHC DISPKRKIDP GQYFDWERYL 


SSVK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC21965.1.
PIRF64060.
RefSeqNP_438467.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44624.
SMRP44624. Positions 6-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC21965; AAC21965; HI_0300.
GeneID949420.
KEGGhin:HI0300.
PATRIC20189141. VBIHaeInf48452_0317.

Phylogenomic databases

eggNOGCOG3023.
KOK03806.
OMACEDRAWH.
OrthoDBEOG60GRR5.
PhylomeDBP44624.

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_HAEIN
AccessionPrimary (citable) accession number: P44624
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 85 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names