Reviewed, UniProtKB/Swiss-Prot P44624 (AMPD_HAEIN)

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:	HI0300

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW 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 zinc 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
	Metal binding	38	1	Zinc; catalytic By similarity
	Metal binding	159	1	Zinc; catalytic By similarity
	Metal binding	169	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44624-1 [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: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC21965.1.
PIR	F64060.
RefSeq	NP_438467.1.
3D structure databases
HSSP	HSSP built from PDB template 1J3G based on UniProtKB P82974.
ModBase	Search...
Genome annotation databases
GeneID	949420.
GenomeReviews	Gene locus HI0300 in contig L42023_GR.
KEGG	hin:HI0300.
NMPDR	fig|71421.1.peg.282.
TIGR	HI0300.
Phylogenomic databases
HOGENOM	P44624.
OMA	LFQGCLD.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0300-MON.
Family and domain databases
InterPro	IPR002502. Amidase_2. [Graphical view]
Gene3D	G3DSA:3.40.80.10. Amidase_2. 1 hit.
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
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:	November 3, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)