B0Y3V7 (AMPP1_ASPFC) 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
ORF Names:	AFUB_055580

Organism

Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]

Taxonomic identifier

451804 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	654 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 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_0000411779
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

Sequences

	Sequence		Length	Mass (Da)
	B0Y3V7 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: 8884D6BCE899397C	FASTA	654	72,680
	10 20 30 40 50 60 MLGFRSPIRL CKLSALGSTR LLPISRPKLF STAVARYAAD METVNTTKRL ARLRQLMQEH 70 80 90 100 110 120 KIDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAIV SMTKAALSTD GRYFNQASKQ 130 140 150 160 170 180 LDSNWELLKR GVENVPTWQE WTTEQAQGGK VVGVDPALIT ASGARSLEET LKRNGSSLVG 190 200 210 220 230 240 ISQNLVDLVW GKDRPAPPRE KVRVHPDKFS GKTFQEKIAD LRKELEKKKT AGFVISMLDE 250 260 270 280 290 300 IAWLFNLRGS DIPYNPVFFA YAIITPTKAE LYIDDDKITP EVVAHLGQDV VIKPYNSIFA 310 320 330 340 350 360 DAKALSEARR KEAGETASKF LLSNKASWAL SLSLGGEEHV EETRSPIADA KAIKNEVELA 370 380 390 400 410 420 GMRACHIRDG AALIEYFAWL ENELVNKKTV LDEVDAADKL EQIRTKHDLF AGLSFDTISS 430 440 450 460 470 480 TGPNGAVIHY KPEKGTCSII DPDAIYLCDS GAQYLDGTTD VTRTFHFGKP TELEKKAFTL 490 500 510 520 530 540 VLKGLIAIDT AVFPKGTSGF ALDALARQYL WKEGLDYLHG TGHGVGSYLN VHEGPIGIGT 550 560 570 580 590 600 RVQYTEVPIA PGNVISDEPG FYEDGKFGIR IENVIMAREV QTTHKFGDKP WLGFEHVTMA 610 620 630 640 650 PIGRNLIEPS LLSDLELKWV NDYHAEVWDK THHFFENDEF TRSWLQRETA PITK

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CEA10 / CBS 144.89 / FGSC A1163.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS499597 Genomic DNA. Translation: EDP51548.1.
3D structure databases
ProteinModelPortal	B0Y3V7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUBT00005537; CADAFUBP00005441; CADAFUBG00005537.
Phylogenomic databases
HOGENOM	HOG000255713.
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_ASPFC

Accession

Primary (citable) accession number: B0Y3V7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	April 8, 2008
Last modified:	March 6, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program