AMPP3_NEOFI
ID AMPP3_NEOFI Reviewed; 467 AA.
AC A1DG66;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=NFIA_083240;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(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; DS027696; EAW18373.1; -; Genomic_DNA.
DR RefSeq; XP_001260270.1; XM_001260269.1.
DR AlphaFoldDB; A1DG66; -.
DR SMR; A1DG66; -.
DR STRING; 36630.CADNFIAP00007184; -.
DR EnsemblFungi; EAW18373; EAW18373; NFIA_083240.
DR GeneID; 4586827; -.
DR KEGG; nfi:NFIA_083240; -.
DR VEuPathDB; FungiDB:NFIA_083240; -.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_017266_1_2_1; -.
DR OMA; DQKFIYN; -.
DR OrthoDB; 352329at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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..467
FT /note="Probable Xaa-Pro aminopeptidase pepP"
FT /id="PRO_0000411878"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 51850 MW; EB791F98387A7570 CRC64;
MAAVDAILAG KYPAKAHARR VAESLQSHRN GCPGIVYLEA QKTRLIEDND EPVPFRQRRP
FFYLSGCPLS DSCLVYDLSE DQLTLFIPPV DPEDVIWSGL PMSTEQAQNQ YDVDRVLVTT
ELNSTLASIA SSHGGKAIAF TIADQVSEST QFHGFSEVNQ SVLKGVIEQS RVVKDEYEVA
LLRKANDISA KAHIAAIKAS QTAVNEREIE GAFIATCIAN GAREQSYHPI VACGENGAIL
HYGKNDDTLI DPVTNQKKRN VLIDAGGEYR TYCADITRVI PVGGKFTAET RQIYDIVLQM
QTECIAMLKE GVQWEDVHAH AHRVAIRGLL RLGILRGAED EIFEKRVSVA FFPHGLGHYL
GMDTHDTGGN PNYTDKDTMF RYLRVRGRLP AGSVITVEPG VYFCRFIIEP YIKSPESNKY
IDTNVLDRYW RVGGVRIEDN VVVTKNGYDN LTTAPKAVDE IERLAVS