Q10736 (AMPN_ACEPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aminopeptidase N
EC=3.4.11.2

Alternative name(s):
Alpha-aminoacylpeptide hydrolase

Gene names

Name:

pepN

Organism

Acetobacter pasteurianus (Acetobacter turbidans)

Taxonomic identifier

438 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acetobacter

Protein attributes

Sequence length	355 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation By similarity.
Catalytic activity	Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›355	›355	Aminopeptidase N		PRO_0000095067
Regions
	Region	290 – 294	5	Substrate binding By similarity
Sites
	Active site	327	1	Proton acceptor By similarity
	Metal binding	326	1	Zinc; catalytic By similarity
	Metal binding	330	1	Zinc; catalytic By similarity
	Metal binding	349	1	Zinc; catalytic By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	349	1	Substrate By similarity
Experimental info
	Non-terminal residue	355	1

Sequences

	Sequence		Length	Mass (Da)
	Q10736 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 8F214BDB2B368232	FASTA	355	38,820
	10 20 30 40 50 60 MRRLLTLTTL LAGVPLAAPV CAEQVFSFQR AAGQLPKTVV PVSYGINIST DIDNLKLTGQ 70 80 90 100 110 120 ETIQVDVRTP TEDVTLNQAG LHLAGAVLDN GVKATITQDD AAETATLHFP AKVSKGAHTL 130 140 150 160 170 180 VITYSGPILK TPNGIYVDDY TAPSGETKRM LVTQFEVADA RRMFPGWDEP AFKATFQLNV 190 200 210 220 230 240 TLPKEAVAVS NMPVTQSTPE GTSQKRVSFA TTPRMSTYLL ALVAGDMKSV QGQADGTPLA 250 260 270 280 290 300 VYAPSGLEEQ GEYALHASEK ILPYYNNYFG VKYPLPQMDM VAIPGNYQAG AMENWGLLTY 310 320 330 340 350 IDNVLLFDPP NSTPRTRELI YEVVAHEMAH QWSGDLVTMG WWDNIWLNEG FASWM

References

[1]	"Cloning and DNA sequence analysis of the 5' end of aminopeptidase N (pepN) from Acetobacter turbidans ATCC9325." Weber M. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 9325 / NCTC 6249 / NRRL B-570.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X94692 Genomic DNA. Translation: CAA64355.1.
3D structure databases
ProteinModelPortal	Q10736.
ModBase	Search...
Protein family/group databases
MEROPS	M01.005.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPN_ACEPA

Accession

Primary (citable) accession number: Q10736

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program