P82973 (AMPD_ENTCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Enterobacter cloacae

Taxonomic identifier

550 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter › Enterobacter cloacae complex

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Cell wall biogenesis/degradation
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Gene Ontology (GO)
Biological_process	peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 187	187	1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD		PRO_0000164412
Sites
	Active site	116	1	Proton acceptor By similarity
	Metal binding	34	1	Zinc; catalytic By similarity
	Metal binding	154	1	Zinc; catalytic By similarity
	Metal binding	164	1	Zinc; catalytic By similarity
	Site	162	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P82973 [UniParc]. Last modified November 2, 2001. Version 1. Checksum: F1D23B55B84E71C8	FASTA	187	20,839
	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

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.
PIR	A48901.
3D structure databases
ProteinModelPortal	P82973.
SMR	P82973. Positions 1-187.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.80.10. 1 hit.
InterPro	IPR002502. Amidase_domain. [Graphical view]
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
SUPFAM	SSF55846. Amidase_2. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMPD_ENTCL

Accession

Primary (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:	April 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program