CHI62_ARATH
ID CHI62_ARATH Reviewed; 283 AA.
AC O22841;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Endochitinase At2g43620 {ECO:0000305};
DE EC=3.2.1.14;
DE Flags: Precursor;
GN OrderedLocusNames=At2g43620 {ECO:0000312|EMBL:AEC10296.1};
GN ORFNames=F18O19.27 {ECO:0000312|EMBL:AEC10296.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY.
RX PubMed=11525512; DOI=10.1007/s004250000464;
RA Passarinho P.A., Van Hengel A.J., Fransz P.F., de Vries S.C.;
RT "Expression pattern of the Arabidopsis thaliana AtEP3/AtchitIV
RT endochitinase gene.";
RL Planta 212:556-567(2001).
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 Evidence={ECO:0000250|UniProtKB:P29022};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; AC002333; AAB64044.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10296.1; -; Genomic_DNA.
DR PIR; D84868; D84868.
DR RefSeq; NP_181890.1; NM_129924.3.
DR AlphaFoldDB; O22841; -.
DR SMR; O22841; -.
DR STRING; 3702.AT2G43620.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR MetOSite; O22841; -.
DR PaxDb; O22841; -.
DR PRIDE; O22841; -.
DR ProMEX; O22841; -.
DR ProteomicsDB; 246495; -.
DR EnsemblPlants; AT2G43620.1; AT2G43620.1; AT2G43620.
DR GeneID; 818964; -.
DR Gramene; AT2G43620.1; AT2G43620.1; AT2G43620.
DR KEGG; ath:AT2G43620; -.
DR Araport; AT2G43620; -.
DR TAIR; locus:2043919; AT2G43620.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_1_1; -.
DR InParanoid; O22841; -.
DR OMA; TTGCAAN; -.
DR OrthoDB; 1132954at2759; -.
DR PhylomeDB; O22841; -.
DR BioCyc; ARA:AT2G43620-MON; -.
DR PRO; PR:O22841; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22841; baseline and differential.
DR Genevisible; O22841; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00182; Glyco_hydro_19; 2.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Plant defense;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..283
FT /note="Endochitinase At2g43620"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433916"
FT DOMAIN 29..66
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 88..283
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 36..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 41..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 59..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 283 AA; 30378 MW; D758222971EE8404 CRC64;
MATLRAMLKN AFILFLFTLT IMAKTVFSQQ CGTTGCAANL CCSRYGYCGT TDAYCGTGCR
SGPCSSSTTP IPPTPSGGAG GLNADPRDTI ENVVTPAFFD GIMSKVGNGC PAKGFYTRQA
FIAAAQSFDA YKGTVAKREI AAMLAQFSHE SGSFCYKEEI ARGKYCSPST AYPCTPGKDY
YGRGPIQITW NYNYGAAGKF LGLPLLTDPD MVARSPQVAF QCAMWFWNLN VRPVLDQGFG
ATTRKINGGE CNGRRPAAVQ SRVNYYLEFC RTLGITPGAN LSC
