AMPP3_PENRW
ID AMPP3_PENRW Reviewed; 465 AA.
AC B6H2M0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Probable Xaa-Pro aminopeptidase pepP;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN Name=pepP; ORFNames=Pc13g05440;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; AM920428; CAP91613.1; -; Genomic_DNA.
DR RefSeq; XP_002558978.1; XM_002558932.1.
DR AlphaFoldDB; B6H2M0; -.
DR SMR; B6H2M0; -.
DR STRING; 1108849.XP_002558978.1; -.
DR EnsemblFungi; CAP91613; CAP91613; PCH_Pc13g05440.
DR GeneID; 8317336; -.
DR KEGG; pcs:Pc13g05440; -.
DR VEuPathDB; FungiDB:PCH_Pc13g05440; -.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_017266_1_2_1; -.
DR OMA; DQKFIYN; -.
DR OrthoDB; 352329at2759; -.
DR BioCyc; PCHR:PC13G05440-MON; -.
DR Proteomes; UP000000724; Contig Pc00c13.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..465
FT /note="Probable Xaa-Pro aminopeptidase pepP"
FT /id="PRO_0000411882"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 51201 MW; 857DC553C4CADBDF CRC64;
MTTVDTILAA KYPAKAHALR VSESLKARHG GAGVIYLEAQ KTRLIEDSDE DMPFRQRRPF
FYLTGCLLPD AAVVYDAVKD ELTLFIPPIN PESVIWSGLP LSPEEAAKLY DVDRVLFTTD
VNSTLASIAS SHNGQTAAFA IAEQVSEGTS FQGFAETNTT SLKTAIEETR VIKDAYEVAL
LRKANDISTK AHVAAIHASK TATNERQIEA AIIGACIANG CREQSYHPIV AGGEGGATLH
YVRNDVDLVD PVTKQRKNNV LIDAGGEYQT YCADITRVIP LNGRFAPETR QIYEIVLQMQ
TECIAMLKEG VCWDDVHALA HRIAIRGLLK LGILRGSEDE LFEKRVSVAF FPHGLGHYLG
MDTHDTGGNP NYEDKDTMFR YLRVRANLPA GSVVTVEPGI YFCRFIIDPI LKAPETGKYI
DTEVLERYWS VGGVRIEDNI HITKDGSENL TTAPKSIEEV ESLAL