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Aspergillopepsin-1 (EC 3.4.23.18) (Aspartic protease pepA) (Aspergillopepsin I) (Aspergillopeptidase A)

 PEPA_ASPPE              Reviewed;         390 AA.
A0A146F0J0;
18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
08-JUN-2016, sequence version 1.
22-NOV-2017, entry version 10.
RecName: Full=Aspergillopepsin-1 {ECO:0000305};
EC=3.4.23.18 {ECO:0000269|PubMed:23044751};
AltName: Full=Aspartic protease pepA;
AltName: Full=Aspergillopepsin I;
AltName: Full=Aspergillopeptidase A;
Flags: Precursor;
Name=pepA;
Aspergillus pseudoglaucus (Eurotium repens).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=1405805;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 68-73;
133-145 AND 175-184.
STRAIN=MK82;
PubMed=26919469; DOI=10.1002/jsfa.7688;
Takenaka S., Umeda M., Senba H., Koyama D., Tanaka K., Yoshida K.I.,
Doi M.;
"Heterologous expression and characterization of the Aspergillus
aspartic protease involved in the hydrolysis and decolorization of
red-pigmented proteins.";
J. Sci. Food Agric. 97:95-101(2017).
[2]
PROTEIN SEQUENCE OF 68-73; 133-145 AND 175-184, FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
STRAIN=MK82;
PubMed=23044751; DOI=10.1002/jsfa.5896;
Aoki K., Matsubara S., Umeda M., Tachibana S., Doi M., Takenaka S.;
"Aspartic protease from Aspergillus (Eurotium) repens strain MK82 is
involved in the hydrolysis and decolourisation of dried bonito
(Katsuobushi).";
J. Sci. Food Agric. 93:1349-1355(2013).
-!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation
of proteinaceous substrates. The scissile peptide bond is attacked
by a nucleophilic water molecule activated by two aspartic
residues in the active site. Shows a broad primary substrate
specificity. Favors hydrophobic residues at the P1 and P1'
positions, but also accepts a lysine residue in the P1 position,
leading to the activation of trypsinogen and chymotrypsinogen A
(By similarity). Hydrolyzes myoglobin, hemoglobin and other
natural proteins. Hydrolyzes equine myoglobin between positions
'Met-1' and 'Gly-2', 'Lys-43' and 'Phe-44', and 'Leu-70' and 'Thr-
71' (PubMed:23044751). {ECO:0000250|UniProtKB:Q12567,
ECO:0000269|PubMed:23044751}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity.
Generally favors hydrophobic residues in P1 and P1', but also
accepts Lys in P1, which leads to activation of trypsinogen. Does
not clot milk. {ECO:0000269|PubMed:23044751}.
-!- ENZYME REGULATION: Inhibited by the microbial peptide pepstatin A.
{ECO:0000269|PubMed:23044751}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=28 uM for equine myoglobin {ECO:0000269|PubMed:23044751};
KM=7.9 uM for bovine hemoglobin {ECO:0000269|PubMed:23044751};
Note=kcat is 0.05 min(-1) with equine myoglobin as substrate and
0.0646 min(-1) with bovine hemoglobin as substrate.
{ECO:0000269|PubMed:23044751};
pH dependence:
Optimum pH is 2-4. Stable from pH 2 to pH 6.
{ECO:0000269|PubMed:23044751};
Temperature dependence:
Optimum temperature is 60 degrees Celsius.
{ECO:0000269|PubMed:23044751};
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
-!- MISCELLANEOUS: Used in Japanese cuisine. During the fermentation
process of Katsuobushi - dried, smoked and fermented meat of the
skipjack tuna (bonito) Katsuwonus pelamis - aspartic protease
plays a role in the decolorisation of Katsuobushi from a dark
reddish-brown to pale pink by the hydrolysis of heme proteins. The
change in color gives Katsuobushi a higher ranking and price.
{ECO:0000305|PubMed:23044751}.
-!- SIMILARITY: Belongs to the peptidase A1 family.
{ECO:0000255|PROSITE-ProRule:PRU01103}.
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EMBL; LC101500; BAU68268.1; -; Genomic_DNA.
SMR; A0A146F0J0; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
CDD; cd06097; Aspergillopepsin_like; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR13683; PTHR13683; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Aspartyl protease; Direct protein sequencing; Hydrolase; Protease;
Secreted; Signal; Zymogen.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 67 Activation peptide.
{ECO:0000269|PubMed:26919469}.
/FTId=PRO_0000438797.
CHAIN 68 390 Aspergillopepsin-1.
/FTId=PRO_5007523443.
DOMAIN 84 387 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
COMPBIAS 8 69 Ala-rich. {ECO:0000255|PROSITE-
ProRule:PRU00001}.
ACT_SITE 100 100 {ECO:0000255|PROSITE-ProRule:PRU01103}.
ACT_SITE 281 281 {ECO:0000255|PROSITE-ProRule:PRU01103}.
CONFLICT 70 72 TGS -> AAA (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 137 138 TW -> YP (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 390 AA; 40623 MW; 1BC7F9AF77ADAC71 CRC64;
MVNTSLLAAL TAYAVAVAAA PTAPQVKGFS VNQVAVPKGV YRHPAAQLAK AYGKYHATVP
TQVAAAAAAT GSVTTNPTSN DEEYITQVTV GDDTLGLDFD TGSADLWVFS SQTPSSERSG
HDYYTPGSSA QKIDGATWSI SYGDGSSASG DVYKDKVTVG GVSYDSQAVE SAEKVSSEFT
QDTENDGLLG LAFSSINTVQ PTPQKTFFDN VKSSLSEPIF AVALKHNAPG VYDFGYTDSS
KYTGSITYTD VDNSQGFWSF TADGYSIGSD SSSDSITGIA DTGTTLLLLD DSIVDAYYEQ
VNGASYDSSQ GGYVFPSSAS LPDFSVTIGD YTATVPGEYI SFADVGNGQT FGGIQSNSGI
GFSIFGDVFL KSQYVVFDAS GPRLGFAAQA


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