AMPP1_PODAN
ID AMPP1_PODAN Reviewed; 680 AA.
AC B2AWV6; A0A090CXB1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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; OrderedLocusNames=Pa_7_8470; ORFNames=PODANS_7_8470;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU633900; CAP68880.1; -; Genomic_DNA.
DR EMBL; FO904942; CDP32352.1; -; Genomic_DNA.
DR RefSeq; XP_001908207.1; XM_001908172.1.
DR AlphaFoldDB; B2AWV6; -.
DR SMR; B2AWV6; -.
DR STRING; 5145.XP_001908207.1; -.
DR MEROPS; M24.A10; -.
DR EnsemblFungi; CAP68880; CAP68880; PODANS_7_8470.
DR GeneID; 6192025; -.
DR KEGG; pan:PODANSg5242; -.
DR VEuPathDB; FungiDB:PODANS_7_8470; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_3_1; -.
DR OrthoDB; 417805at2759; -.
DR Proteomes; UP000001197; Chromosome 7.
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 InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..680
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411806"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 586
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 600
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 600
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 680 AA; 75096 MW; 37534DD2228663E8 CRC64;
MRHIWALPSL TALSLFQASA ASAVPRARQA INTSSPLAPF RTKRRFRTQA QLLSNSATKT
TLVEEMVTVD TTSRLAALRS LMKERNLHVY VVPSEDSHAS EYIADCDARR TFISGFSGSA
GTAIVTLDKA ALATDGRYFN QASKQLDSNW YLLKTGMQDV PTWQEWATQE AEGGKLIGVD
PQLISSAIAE KLDEDIKNAG GGGLVGIKEN LVDLVWGSEQ PPRPSNSVFL LGQQYAGKDT
AAKLADLRKE LDKKKAAGFV LSMLDEIAWL FNLRGSDIAY NPVFFSYAIV TQASATLYID
EAKLTDECKT YLERNKVTIK PYGALFEDSE ELARRAEADS KDAKPRKYLI SSKGSWALKL
ALGGNKFVDE VRSPVGDAKA VKNDVELNGM RNCHIRDGAA LTEFFAWLED QLVNQKAQLD
EVDAADKLEQ IRSKHKDFVG LSFDTISSTG ANAAVIHYKP EKGACKIIDP NAIYLCDSGA
QYLDGTTDTT RTLHFGTPTA KEKKAYTLVL KGNIALDSVV FPKGTSGFAI DVMARQFLWK
YGLDYRHGTG HGVGSFLNVH EGPIGIGTRK QYIDVALAAG NVLSIEPGYY EDEAFGIRIE
NLAIVKEVKT EHSFGDKPYL GFEHVTMVPY ARNLIDETLL TPDEKDWLNR ANKKILEKTL
GYFENDPLTK AWLLRETQPF
