A2QAW7 (AMPP2_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase An01g13040
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

ORF Names:

An01g13040

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	491 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 – 491	491	Probable Xaa-Pro aminopeptidase An01g13040		PRO_0000411827
Sites
	Metal binding	276	1	Manganese 2 By similarity
	Metal binding	287	1	Manganese 1 By similarity
	Metal binding	287	1	Manganese 2 By similarity
	Metal binding	420	1	Manganese 1 By similarity
	Metal binding	459	1	Manganese 1 By similarity
	Metal binding	459	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2QAW7 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: E44B2BDF7387C28D	FASTA	491	54,950
	10 20 30 40 50 60 MRVSIPPELV SSLGACDLRV TVRGEGIDKY PGGPGAAKQH ARKVAMKLGV SSGLIYLVGK 70 80 90 100 110 120 PTINWGDSDQ PQPFRQRRYF YYLSGADEPD CYLTYDINND LLVLYVPDFD LHRAIWMGPT 130 140 150 160 170 180 LTTDEAERRF DVDKVRYYAS LQSDIQSWVG KYNDAAPVYI LHSSQQPQFS VQQLHIDDQR 190 200 210 220 230 240 LLPAMDAARV VKDDYELRMI RHANKISGLA HRKVLEQIHK MSNEAQIEGL FLDTCVSHGA 250 260 270 280 290 300 KNQAYEIIAG SGPNAATLHY VKNNEPLKGR QLVCLDAGAE WECYASDVTR TFPLAADWPS 310 320 330 340 350 360 SHARDVYQIV EEMQEQCIKR IKPGVRFRDL QVLAHDIAIR GLQKLGVLKP GTVEEIRVSG 370 380 390 400 410 420 ASAIFFPHGL GHHVGLEVHD VSEKPITGMG LPNRPCRPDF IPAMSQSVPL LEEGMVVTIE 430 440 450 460 470 480 PGVYFSKLAL ANSRKLPQAR YINFDEAEKY IPIGGVRIED DILVTRTGYE NLTTAPKGDE 490 MLEIIRRGID N

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	AM269986 Genomic DNA. Translation: CAK37351.1.
3D structure databases
ProteinModelPortal	A2QAW7.
ModBase	Search...
Protein family/group databases
MEROPS	M24.A09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00001303; CADANGAP00001257; CADANGAG00001303.
Phylogenomic databases
HOGENOM	HOG000008763.
OrthoDB	EOG4897VR.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR007865. Aminopep_P_N. IPR000994. Pept_M24_structural-domain. IPR001131. Peptidase_M24B_aminopep-P_CS. [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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPP2_ASPNC

Accession

Primary (citable) accession number: A2QAW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	March 6, 2007
Last modified:	March 6, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program