P44624 (AMPD_HAEIN) 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
Ordered Locus Names:	HI_0300

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	184 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
Technical term	Complete proteome Reference proteome
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 – 184	184	1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD		PRO_0000164414
Sites
	Active site	120	1	Proton acceptor By similarity
	Metal binding	38	1	Zinc; catalytic By similarity
	Metal binding	159	1	Zinc; catalytic By similarity
	Metal binding	169	1	Zinc; catalytic By similarity
	Site	167	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44624 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: B7A035527E328401	FASTA	184	21,448
	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

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC21965.1.
PIR	F64060.
RefSeq	NP_438467.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44624.
SMR	P44624. Positions 6-183.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0300.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC21965; AAC21965; HI_0300.
GeneID	949420.
KEGG	hin:HI0300.
PATRIC	20189141. VBIHaeInf48452_0317.
Phylogenomic databases
eggNOG	COG3023.
KO	K03806.
OMA	LFQGCLD.
ProtClustDB	PRK11789.
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_HAEIN

Accession

Primary (citable) accession number: P44624

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program