The domain within your query sequence starts at position 67 and ends at position 203; the E-value for the AMP_N domain shown below is 6.87e-50.

LSQVEYALRRHKLMALVHKEAQGHSGTDHTVVVLSNPTYYMSNDIPYTFHQDNNFLYLCG
FQEPDSILVLQSFSGKQLPSHKAMLFVPRRDPGRELWDGPRSGTDGAIALTGVDEAYPLE
EFQHLLPKLRGFHRDHV

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 ).

• GO function: metalloaminopeptidase activity (GO:0070006), manganese ion binding (GO:0030145)

There are 15332 AMP_N domains in 15331 proteins in SMART's nrdb database.

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

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)

3D Structures of AMP_N domains in PDB

PDB code	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	ZnMg 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 a product- like inhibitor
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
4pv4	Proline aminopeptidase P II from Yersinia pestis

Links (links to other resources describing this domain)

• PFAM: AMP_N
• INTERPRO: IPR007865