SMART: AMP_N domain annotation

AMP_N Aminopeptidase P, N-terminal domain

SMART accession number:	SM01011
Description:	This domain is structurally very similar to the creatinase N-terminal domain. However, little or no sequence similarity exists between the two families.
Interpro abstract (IPR007865):	This entry represents the N-terminal domain of aminopeptidase P (X-Pro aminopeptidase I,II and III EC 3.4.11.9) and related sequences belonging to the peptidase M24B family. The domain is structurally very similar [(PUBMED:9520390)] to the creatinase N-terminal domain (IPR000587), however, little or no sequence similarity exists between the two domains.
GO function:	manganese ion binding (GO:0030145), aminopeptidase activity (GO:0004177)
Family alignment:	View or

There are 1167 AMP_N domains in 1167 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with AMP_N domain is also avaliable.

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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
Cellular role (predicted cellular role)
Cellular role: metabolism
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Wilce MC et al.
- Structure and mechanism of a proline-specific aminopeptidase fromEscherichia coli.
- Proc Natl Acad Sci U S A. 1998; 95: 3472-7
- Display abstract
- The structure of the proline-specific aminopeptidase (EC 3.4.11.9) fromEscherichia coli has been solved and refined for crystals of the nativeenzyme at a 2.0-A resolution, for a dipeptide-inhibited complex at 2.3-Aresolution, and for a low-pH inactive form at 2.7-A resolution. Theprotein crystallizes as a tetramer, more correctly a dimer of dimers, atboth high and low pH, consistent with observations from analyticalultracentrifuge studies that show that the protein is a tetramer underphysiological conditions. The monomer folds into two domains. The activesite, in the larger C-terminal domain, contains a dinuclear manganesecenter in which a bridging water molecule or hydroxide ion appears poisedto act as the nucleophile in the attack on the scissile peptide bond ofXaa-Pro. The metal-binding residues are located in a single subunit, butthe residues surrounding the active site are contributed by threesubunits. The fold of the protein resembles that of creatineamidinohydrolase (creatinase, not a metalloenzyme). The C-terminalcatalytic domain is also similar to the single-domain enzyme methionineaminopeptidase that has a dinuclear cobalt center.
Structure (3D structures containing this domain)

Links (links to other resources describing this domain)
PFAM AMP_N
INTERPRO IPR007865

PDB code	Main view	Title
1a16		Aminopeptidase p from e. coli with the inhibitor pro-leu
1jaw		Aminopeptidase p from e. coli low ph form
1m35		Aminopeptidase p from escherichia coli
1n51		Aminopeptidase p in complex with the inhibitor apstatin
1w2m		Ca-substituted form of e. coli aminopeptidase p
1w7v		Znmg substituted aminopeptidase p from e. coli
1wbq		Zn mg substituted aminopeptidase p from e. coli
1wl6		Mg-substituted form of e. coli aminopeptidase p
1wl9		Structure of aminopeptidase p from e. coli
1wlr		Apo aminopeptidase p from e. coli
2bh3		Zn substituted e.coli aminopeptidase p in complex with product
2bha		E. coli aminopeptidase p in complex with substrate
2bhb		Zn substituted e. coli aminopeptidase p
2bhc		Na substituted e. coli aminopeptidase p
2bhd		Mg substituted e. coli aminopeptidase p in complex with product
2bn7		Mn substituted e. coli aminopeptidase p in complex with product and zn
2bws		His243ala escherichia coli aminopeptidase p
2bwt		Asp260ala escherichia coli aminopeptidase p
2bwu		Asp271ala escherichia coli aminopeptidase p
2bwv		His361ala escherichia coli aminopeptidase p
2bww		His350ala escherichia coli aminopeptidase p
2bwx		His354ala escherichia coli aminopeptidase p
2bwy		Glu383ala escherichia coli aminopeptidase p
2iw2		Crystal structure of human prolidase
2okn		Crystal strcture of human prolidase
2v3x		His243ala escherichia coli aminopeptidase p in complex with substrate
2v3y		His361ala escherichia coli aminopeptidase p in complex with product
2v3z		Glu383ala escherichia coli aminopeptidase p in complex with substrate
3ig4		Structure of a putative aminopeptidase p from bacillus anthracis

PFAM	AMP_N
INTERPRO	IPR007865

AMP_N

3D Structures of AMP_N domains in PDB