A2QKF6 (AMPP3_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase pepP
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

Name:	pepP
ORF Names:	An05g00050

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides By similarity.
Catalytic activity	Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Sequence similarities	Belongs to the peptidase M24B family.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: InterPro metallopeptidase activity 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 – 466	466	Probable Xaa-Pro aminopeptidase pepP		PRO_0000411866
Sites
	Metal binding	264	1	Manganese 2 By similarity
	Metal binding	275	1	Manganese 1 By similarity
	Metal binding	275	1	Manganese 2 By similarity
	Metal binding	398	1	Manganese 1 By similarity
	Metal binding	438	1	Manganese 1 By similarity
	Metal binding	438	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2QKF6 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: 162A26E9A5A823F8	FASTA	466	51,472
	10 20 30 40 50 60 MTTLDSILAG RYPAKAHARR VAERLQVGGS GRNGIIYLEA QKTRLIEDND EAMHFRQRRP 70 80 90 100 110 120 FFYLSGCPLP DSSLIYNIAS DKLTLFIPPI DPEDVIWSGL PMSVAEALRL YDVDQVLHTT 130 140 150 160 170 180 DVNATLASIA SDGNGKSVAF AIEGQITEGI KFDGFLETNT SVLKGAIDST RVVKDEYEIA 190 200 210 220 230 240 LLRKANDISA KAHIAAIEAS KTATNEREIE AAFLATCIAN GARDQAYHPI VACGQNGATL 250 260 270 280 290 300 HYGRNDDDLV DPVTKAGKSS VLIDAGAEYR TYCADITRVF PLGGRFTSET QEIYKIVLQM 310 320 330 340 350 360 QLEAIAMLKE NVQWEDVHAH AHRIAIKGLL KLGILRGSED ELFEKRISVA FFPHGLGHYL 370 380 390 400 410 420 GMDTHDTGGN PNYADKDTMF KYLRVRGRLP AGSVITVEPG IYFCRFIIEP YLTSPETSKY 430 440 450 460 IDTNVLEKYW NVGGVRIEDN VHVTQQGYEN LTTAPKAIEE VEVLAT

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270101 Genomic DNA. Translation: CAK44825.1.
RefSeq	XP_001390579.1. XM_001390542.2.
3D structure databases
ProteinModelPortal	A2QKF6.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00004657.
Protein family/group databases
MEROPS	M24.A09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00004753; CADANGAP00004657; CADANGAG00004753.
GeneID	4980742.
KEGG	ang:ANI_1_6044.
Phylogenomic databases
HOGENOM	HOG000008763.
KO	K14213.
OrthoDB	EOG4J40RD.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR007865. Aminopep_P_N. IPR000994. Pept_M24_structural-domain. [Graphical view]
Pfam	PF05195. AMP_N. 1 hit. PF00557. Peptidase_M24. 1 hit. [Graphical view]
SMART	SM01011. AMP_N. 1 hit. [Graphical view]
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITE	PS00491. PROLINE_PEPTIDASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPP3_ASPNC

Accession

Primary (citable) accession number: A2QKF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	March 6, 2007
Last modified:	April 3, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program