AMPP1_LACBS
ID AMPP1_LACBS Reviewed; 642 AA.
AC B0DZL3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable Xaa-Pro aminopeptidase P;
DE Short=AMPP;
DE Short=Aminopeptidase P;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN Name=AMPP; ORFNames=LACBIDRAFT_315028;
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=486041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686;
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(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; DS547156; EDQ99959.1; -; Genomic_DNA.
DR RefSeq; XP_001889370.1; XM_001889335.1.
DR AlphaFoldDB; B0DZL3; -.
DR SMR; B0DZL3; -.
DR STRING; 486041.B0DZL3; -.
DR MEROPS; M24.009; -.
DR EnsemblFungi; EDQ99959; EDQ99959; LACBIDRAFT_315028.
DR GeneID; 6085051; -.
DR KEGG; lbc:LACBIDRAFT_315028; -.
DR HOGENOM; CLU_011781_2_3_1; -.
DR InParanoid; B0DZL3; -.
DR OrthoDB; 417805at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.40.350.10; -; 2.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF53092; SSF53092; 2.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..642
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411792"
FT BINDING 439
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 548
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 562
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 562
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 642 AA; 72173 MW; AEA41CF5F61EB3A9 CRC64;
MWRAIWLRIS EKGLRRPPPP SLRTVTTSCT TMGADGVHTV NTTERLAKLR ELMKQHSVQA
FVVPSEDQHS SEYLANCDKR RAFISGFDGS AGCAIITTDK AYLFTDGRYF LQAEKQLDKN
WKLMKQGLPD VPTWQDFLYK NLGPHTQIGI DATLLAASDA ESLTKQLTPK YSKLVSLKEN
LVDVVWGEDR PSRPQNSVFH LDVKYSGQSH LDKIATLREE MKKKKAEAIV VTMLDEVAWL
LNLRGSDIEY NPVFFAYAVV TMDEVILFID SAQLDDTARH NLEHVYTMPY EAIFEHLNSL
SRTLELDRDS KVLIGDRASL AVADAIGKDN YTIVRSPIAD LKAIKNKTEL EGFRQSHIRD
GAALVRYFAW LEEQLNHGTV INESQGADKL EAFRSELDLF RGLSFDTISG TGPNGAIIHY
KPDPNDCAII KKDQVYLCDS GGQFLDGTTD VTRTWHFGTP TDEEKRAFTR VLQGHIAIDT
AVFPNGTTGY VIDAFARRAL WQDGLDYRHG TGHGVGHFLN VHEGPHGIGV RIALNNTPLK
AGMTVSNEPG YYADGKFGIR IESIVLVREV KTPNNFGDKG YLGFENVTMC PIHKNLVDVS
LLNEQEKKWL DEYHAETWDK VSPLLKGDTR ALEWLRRECS PL
