Q2U7S5 (AMPP1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase P
Short name=AMPP
Short name=Aminopeptidase P
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

Name:	ampp
Synonyms:	app
ORF Names:	AO090701000720

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	654 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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.
Sequence caution	The sequence BAE62390.1 differs from that shown. Reason: Erroneous gene model prediction.

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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 654	654	Probable Xaa-Pro aminopeptidase P		PRO_0000411783
Sites
	Metal binding	449	1	Manganese 2 By similarity
	Metal binding	460	1	Manganese 1 By similarity
	Metal binding	460	1	Manganese 2 By similarity
	Metal binding	558	1	Manganese 1 By similarity
	Metal binding	572	1	Manganese 1 By similarity
	Metal binding	572	1	Manganese 2 By similarity
Experimental info
	Sequence conflict	640	1	Y → C in BAD00702. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q2U7S5 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: BBF674FFF5A43198	FASTA	654	72,826
	10 20 30 40 50 60 MLFSRPPIRS PWISAFRSAS QLPLSRPRFF SISLSRYSVD METVNTSERL SRLRELMQEH 70 80 90 100 110 120 KVDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAIV SLSKAALSTD GRYFNQASKQ 130 140 150 160 170 180 LDNNWQLLKR GVEGFPTWQE WTTEQAEGGK VVGVDPALIT ASGARSLSET LKKNGSTLVG 190 200 210 220 230 240 VQQNLVDLVW GKDRPAPPRE KVRVHPEKYA GKSFQEKISE LRKELESRKS AGFIVSMLDE 250 260 270 280 290 300 IAWLFNLRGS DIPYNPVFFS FATITPTTTE LYVDADKLTP EVTAHLGQDV VIKPYDAIYA 310 320 330 340 350 360 DAKALSETRK QEAGETASKF LLSNKASWAL SLSLGGEGQV EEVRSPIGDA KAVKNDVELA 370 380 390 400 410 420 GMRACHIRDG AALTEYFAWL ENELVNKKST LDEVDAADKL EQIRSKHDLF VGLSFDTISS 430 440 450 460 470 480 TGPNGAVIHY KPEKGSCSII DPNAIYLCDS GAQYLDGTTD VTRTFHFGQP TELEKKAFTL 490 500 510 520 530 540 VLKGVIGLDT AVFPKGTSGF ALDVLARQYL WKEGLDYLHG TGHGIGSYLN VHEGPIGVGT 550 560 570 580 590 600 RVQYTEVPIA PGNVISDEPG FYEDGKFGIR IENVIMAREV QTTHKFGDKP WLGFEHVTMA 610 620 630 640 650 PIGRNLIEPS LLSDAELKWV NDYHREIWEK THHFFENDEY TRSWLQRETQ PISK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of aminopeptidase-P from Aspergillus oryzae." Matsushima K., Koyama Y., Takahashi T., Matsuda T., Ito K., Nakahara T., Umitsuki G. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 42149 / RIB 40.
[2]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB078875 mRNA. Translation: BAD00702.1. AP007164 Genomic DNA. Translation: BAE62390.1. Sequence problems.
RefSeq	XP_001823523.2. XM_001823471.2.
3D structure databases
ProteinModelPortal	Q2U7S5.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00010793.
Protein family/group databases
MEROPS	M24.009.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00011018; CADAORAP00010793; CADAORAG00011018.
GeneID	5995580.
KEGG	aor:AOR_1_1270114.
Phylogenomic databases
eggNOG	COG0006.
HOGENOM	HOG000255713.
KO	K01262.
OrthoDB	EOG45F0XX.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR000587. Creatinase. IPR000994. Pept_M24_structural-domain. IPR001131. Peptidase_M24B_aminopep-P_CS. [Graphical view]
Pfam	PF01321. Creatinase_N. 1 hit. PF00557. Peptidase_M24. 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

AMPP1_ASPOR

Accession

Primary (citable) accession number: Q2U7S5
Secondary accession number(s): Q76LL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program