CHIA1_EMEND
ID CHIA1_EMEND Reviewed; 961 AA.
AC Q92223; Q5ATY9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 3.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Endochitinase A;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase A;
DE Flags: Precursor;
GN Name=chiA;
OS Emericella nidulans (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=FGSC 89;
RX PubMed=9501518; DOI=10.1271/bbb.62.60;
RA Takaya N., Yamazaki D., Horiuchi H., Ohta A., Takagi M.;
RT "Cloning and characterization of a chitinase-encoding gene (chiA) from
RT Aspergillus nidulans, disruption of which decreases germination frequency
RT and hyphal growth.";
RL Biosci. Biotechnol. Biochem. 62:60-65(1998).
RN [2]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=FGSC 26 {ECO:0000303|PubMed:17455791};
RX PubMed=17455791; DOI=10.1007/bf02931619;
RA Pusztahelyi T., Molnar Z., Emri T., Klement E., Miskei M., Kerekgyarto J.,
RA Balla J., Pocsi I.;
RT "Comparative studies of differential expression of chitinolytic enzymes
RT encoded by chiA, chiB, chiC and nagA genes in Aspergillus nidulans.";
RL Folia Microbiol. (Praha) 51:547-554(2006).
CC -!- FUNCTION: GPI-anchored chitinase involved in the degradation of chitin,
CC a component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Required to reshape the cell
CC wall at the sites where cell wall remodeling and/or cell wall
CC maturation actively take place such as sites of conidia formation (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}. Cell tip
CC {ECO:0000250}. Note=Localizes at the germ tubes of conidia, at hyphal
CC branching sites and hyphal tips. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expression decreases during stationary and
CC autolytic stages. {ECO:0000269|PubMed:17455791}.
CC -!- INDUCTION: Expression is induced during conidiospore formation
CC (PubMed:9501518). Significantly up-regulated expression with colloidal
CC chitin and chito-oligomers, namely N-acetyl-D-glucosamine (GlcNAc),
CC N,N'-diacetylchitobiose (GlcNAc)2 and N,N',N''-triacetylchitotriose
CC (GlcNAc)3. Expression is not affected by changes in the levels of
CC reactive oxygen species or in the glutathione-glutathione disulfide
CC redox balance, the changes which are physiological characteristics
CC developing in aging and autolyzing fungal cultures. Down-regulated by
CC the oxidative-stress-generating agent diamide, but not by menadione or
CC hydrogen peroxide (PubMed:17455791). {ECO:0000269|PubMed:17455791,
CC ECO:0000269|PubMed:9501518}.
CC -!- PTM: O-glycosylated but not N-glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Decreases the frequency of germination.
CC {ECO:0000269|PubMed:9501518}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; D87895; BAA36223.1; -; Genomic_DNA.
DR PIR; JW0067; JW0067.
DR AlphaFoldDB; Q92223; -.
DR SMR; Q92223; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR OMA; DTVYPTD; -.
DR BRENDA; 3.2.1.14; 517.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051286; C:cell tip; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell membrane; Cell wall; Chitin degradation;
KW Chitin-binding; Glycoprotein; Glycosidase; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..936
FT /note="Endochitinase A"
FT /id="PRO_0000429820"
FT PROPEP 937..961
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000429821"
FT DOMAIN 28..339
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 338..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT LIPID 936
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 961 AA; 96840 MW; 66263B3325C533E2 CRC64;
MAPKLFTFVS ALSGLASLAS AFHAEAKSNI AVYYGQGVNQ PRLAEFCAET SYDIINIGFI
NSFPEQNPLT GLPGSDFGNQ CWADTFVVDG IASQLYSHCP NIAEDIPKCQ AAGKKVFLSL
GGATPTYWFD TIDASTKLAD FLWGAFGPVT DAWTVADKPR PFGNAVVDGF DFDIEFFGSK
GYANMIKRFR RRFGEVPDQT FYISAAPQCS IPDEQLSVAI KNAVIDFVWV QFYNTPGCSA
RDFVLGTKNG FNYDSWVEVI KAGANPNAKL YVGLPASGAA ANLGYYLTPE EVKPLVKKYM
DKYPETFGGV MLWEATQARN NQIDGVGYNE KIREILYDLD PNHPPPTTSP TPTPTPSTTT
TSTTSTTSTT SATSTTSTTS TTSTTSTTPT TSTTSTTSTT TPTPSPSPST ASSSTTETVT
PSPKPSPSES STTSETSSLP STSTPVVSET PSETKTPTSS SAPPLSSSSP VGGSSSTASS
STSTPSETPS ASSTRAVSET STHISTSTSS GPETSLTGSS TSVPATSSSV PSSAISPSST
PVISETPRPP VTSSSSSTFV SSTSTSTDCS ESSTAIGTHS SSSISETPSA STPAASPSTS
PETTKTLTVF PTPGSSVSTG TTSASTLSSS VPATSGGHTE TSTVSTSSAN QTPSASTSKP
LIPTNSASST STGSVTSTPS APGVPSSSAG SDETATTSTT DSEPTSTSSG SVTAKPTTTE
PATTTTIIVT SYTSICPTGF TTITTTITST YCPGTASATA TAIAPTTDVP GSGSGSSPAQ
PTITADIPEG WTTTVTVCTV CAATPTTVTL TLPPATTTEE STSAQPTGEV PSSDGSGSGE
VSTTTVVVVP APTGNAGDGV PAPGANVGEE YTAAPGSATT SKPLIGGGAS GAHTAYPYAS
STFHIIPSAS AHVPVPSGSG SSPSGTQGGA SPTFTGAGSR YDVVKGVPAL VALALSLLAV
L
