AMPP1_CHAGB
ID AMPP1_CHAGB Reviewed; 624 AA.
AC Q2H8T2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=CHGG_03372;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ91437.1; -; Genomic_DNA.
DR RefSeq; XP_001229888.1; XM_001229887.1.
DR AlphaFoldDB; Q2H8T2; -.
DR SMR; Q2H8T2; -.
DR STRING; 38033.XP_001229888.1; -.
DR MEROPS; M24.009; -.
DR EnsemblFungi; EAQ91437; EAQ91437; CHGG_03372.
DR GeneID; 4388486; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_2_1; -.
DR InParanoid; Q2H8T2; -.
DR OMA; YRPGKWG; -.
DR OrthoDB; 417805at2759; -.
DR Proteomes; UP000001056; 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 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..624
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411786"
FT BINDING 414
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 624 AA; 68186 MW; D3CC4ED836CB34F2 CRC64;
METVNTTARL TTLRSLMKEN GVDIYGIIVP SEDSHASEYI APCDGRRAFI SGFTGSAGTA
VVTQDKAALA TDGRYFNQAG KQLDGNWHLL KTGLQDVPTW QDWTAEASAG GKTVGVDPSL
ISSPIAEKLD ESIKKSGGAG LKAVSENLVD PVWGSDRPAR SSNPVKLLIG KYSGKDTAAK
LTELRKELEK KKAAAFVLSM LDEVAWLFNL RGSDITYNPV FYSYAIVTQD SATLYVDVSK
LDDESRSYLD QNKVTIKPYD TLFEDAKALA SAAEAKGTSE APRKYFVSNK GSWALKLALG
GDKFVEEVRS PVGDAKAVKN DTELEGMRQC HIRDGVALIQ FFAWLEDQLV NKKAVLDEVA
AADQLEALRS KQTDFVGLSF DTISSTGPNA AVIHYKPEPG ACSIIDPEAI YLCDSGAQFL
DGTTDVTRTL HFGTPTAEQK KAYTLVLKGN IALDTAIFPK GTTGYAIDCL ARQFLWASSP
FSTKQGLDYR HGTGHGVGSY LNVHEGPIGI GTRKQYAEVA LAAGNVLSIE PGFYEDGSYG
IRIENLAMVR EVKTEHSFGD KPFLGFEHVT MVPYCRKLID EALLTAEERE WLNQSNKEIR
EKMAGRFDGD QLTQAWLERE TQPF
