ID   CSN_ASPFM               Reviewed;         238 AA.
AC   Q875I9; Q709P2; Q9Y760;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Endo-chitosanase;
DE            EC=3.2.1.132;
DE   Flags: Precursor;
GN   Name=csn;
OS   Neosartorya fumigata (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=746128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-32, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Y2K;
RX   PubMed=11115392; DOI=10.1042/ba20000063;
RA   Cheng C.Y., Li Y.K.;
RT   "An Aspergillus chitosanase with potential for large-scale preparation of
RT   chitosan oligosaccharides.";
RL   Biotechnol. Appl. Biochem. 32:197-203(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-32, VARIANTS ILE-38 AND
RP   ARG-213, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=NCPF7367;
RX   PubMed=16396247; DOI=10.1080/13693780500089216;
RA   Schwienbacher M., Weig M., Thies S., Regula J.T., Heesemann J., Ebel F.;
RT   "Analysis of the major proteins secreted by the human opportunistic
RT   pathogen Aspergillus fumigatus under in vitro conditions.";
RL   Med. Mycol. 43:623-630(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kang T.H., Chung J.Y., Chung K.C.;
RT   "The partial sequence of chitosanase cDNA from Aspergillus fumigatus using
RT   PCR.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 55-70; 73-87; 90-102 AND 119-131, SUBCELLULAR LOCATION,
RP   AND FUNCTION AS AN ALLERGEN.
RX   PubMed=17651155; DOI=10.1111/j.1365-2222.2007.02765.x;
RA   Gautam P., Sundaram C.S., Madan T., Gade W.N., Shah A., Sirdeshmukh R.,
RA   Sarma P.U.;
RT   "Identification of novel allergens of Aspergillus fumigatus using
RT   immunoproteomics approach.";
RL   Clin. Exp. Allergy 37:1239-1249(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-160 AND GLU-169.
RC   STRAIN=Y2K;
RX   PubMed=16330537; DOI=10.1074/jbc.m512506200;
RA   Cheng C.Y., Chang C.H., Wu Y.J., Li Y.K.;
RT   "Exploration of glycosyl hydrolase family 75, a chitosanase from
RT   Aspergillus fumigatus.";
RL   J. Biol. Chem. 281:3137-3144(2006).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Y2K;
RX   PubMed=22160328; DOI=10.1007/s10529-011-0816-0;
RA   Chen X., Zhai C., Kang L., Li C., Yan H., Zhou Y., Yu X., Ma L.;
RT   "High-level expression and characterization of a highly thermostable
RT   chitosanase from Aspergillus fumigatus in Pichia pastoris.";
RL   Biotechnol. Lett. 34:689-694(2012).
CC   -!- FUNCTION: Chitosanase catalyzing the endo-type cleavage of chitosan,
CC       the deacylated form of chitin. Chitosanase may be crucial in the
CC       degradation of the deacetylated portion of chitin in the fungal cell
CC       wall. Chitoolisaccharides produced by the hydrolysis of partially N-
CC       acetylated chitosan are known to have many biological activities,
CC       including antibacterial activity, immune-enhancing effects, and
CC       elicitor activity. The chitosans with higher degrees of deacetylation
CC       were shown to be the better substrates. Chitodimer, chitotrimer, and
CC       chitotetramer are the major products but monoacetyl chitodimer,
CC       monoacetyl chitotrimer, and monoacetyl chitotetramer are also produced.
CC       {ECO:0000269|PubMed:16330537, ECO:0000269|PubMed:17651155,
CC       ECO:0000269|PubMed:22160328}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of beta-(1->4)-linkages between D-glucosamine
CC         residues in a partly acetylated chitosan.; EC=3.2.1.132;
CC         Evidence={ECO:0000269|PubMed:11115392, ECO:0000269|PubMed:16330537,
CC         ECO:0000269|PubMed:22160328};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:11115392,
CC         ECO:0000269|PubMed:22160328};
CC       Temperature dependence:
CC         Optimum temperature is between 65 and 70 degrees Celsius.
CC         {ECO:0000269|PubMed:11115392, ECO:0000269|PubMed:22160328};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16396247,
CC       ECO:0000269|PubMed:17651155}.
CC   -!- INDUCTION: Expressed during human infection.
CC       {ECO:0000269|PubMed:16396247}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 75 family. {ECO:0000305}.
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DR   EMBL; AY190324; AAO41660.1; -; Genomic_DNA.
DR   EMBL; AJ607393; CAE54966.1; -; mRNA.
DR   EMBL; AF105078; AAD26111.1; -; mRNA.
DR   AlphaFoldDB; Q875I9; -.
DR   Allergome; 8985; Asp f Chitosanase.
DR   CAZy; GH75; Glycoside Hydrolase Family 75.
DR   CLAE; CSN75A_ASPFU; -.
DR   OMA; KGECAND; -.
DR   BRENDA; 3.2.1.132; 508.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016977; F:chitosanase activity; IDA:AspGD.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR009939; Chitosanase_fungal.
DR   PANTHER; PTHR42061; PTHR42061; 1.
DR   Pfam; PF07335; Glyco_hydro_75; 1.
PE   1: Evidence at protein level;
KW   Allergen; Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:11115392,
FT                   ECO:0000269|PubMed:16396247"
FT   CHAIN           18..238
FT                   /note="Endo-chitosanase"
FT                   /id="PRO_5000089367"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         38
FT                   /note="V -> I (in strain: NCPF7367)"
FT                   /evidence="ECO:0000269|PubMed:16396247"
FT   VARIANT         213
FT                   /note="W -> R (in strain: NCPF7367)"
FT                   /evidence="ECO:0000269|PubMed:16396247"
FT   MUTAGEN         160
FT                   /note="D->N: Reduces catalytic to less then 0.1 percent."
FT                   /evidence="ECO:0000269|PubMed:16330537"
FT   MUTAGEN         169
FT                   /note="E->Q: Reduces catalytic to less then 0.1 percent."
FT                   /evidence="ECO:0000269|PubMed:16330537"
SQ   SEQUENCE   238 AA;  25191 MW;  0A0A7D0118D181CB CRC64;
     MRLSEILTVA LVTGATAYNL PNNLKQIYDK HKGKCSKVLA KGFTNGDASQ GKSFSYCGDI
     PGAIFISSSK GYTNMDIDCD GANNSAGKCA NDPSGQGETA FKSDVKKFGI SDLDANIHPY
     VVFGNEDHSP KFKPQSHGMQ PLSVMAVVCN GQLHYGIWGD TNGGVSTGEA SISLADLCFP
     NEHLDGNHGH DPNDVLFIGF TSKDAVPGAT AKWKAKNAKE FEDSIKSIGD KLVAGLKA