CHI58_ARATH
ID CHI58_ARATH Reviewed; 265 AA.
AC O24598;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Endochitinase At2g43580 {ECO:0000305};
DE EC=3.2.1.14;
DE Flags: Precursor;
GN OrderedLocusNames=At2g43580 {ECO:0000312|EMBL:AEC10292.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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).
RN [6]
RP INDUCTION BY BOTRYTIS.
RC STRAIN=cv. Columbia;
RX PubMed=17059405; DOI=10.1111/j.1365-313x.2006.02901.x;
RA Zheng Z., Qamar S.A., Chen Z., Mengiste T.;
RT "Arabidopsis WRKY33 transcription factor is required for resistance to
RT necrotrophic fungal pathogens.";
RL Plant J. 48:592-605(2006).
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 -!- INDUCTION: Accumulates during Botrytis cinerea infection.
CC {ECO:0000269|PubMed:17059405}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; AC002333; AAB64048.1; -; Genomic_DNA.
DR EMBL; AC002335; AAM14811.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10292.1; -; Genomic_DNA.
DR EMBL; AK118596; BAC43195.1; -; mRNA.
DR EMBL; BT006229; AAP12878.1; -; mRNA.
DR PIR; H84867; H84867.
DR RefSeq; NP_181886.1; NM_129920.3.
DR AlphaFoldDB; O24598; -.
DR SMR; O24598; -.
DR STRING; 3702.AT2G43580.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; O24598; -.
DR PRIDE; O24598; -.
DR ProteomicsDB; 240614; -.
DR EnsemblPlants; AT2G43580.1; AT2G43580.1; AT2G43580.
DR GeneID; 818960; -.
DR Gramene; AT2G43580.1; AT2G43580.1; AT2G43580.
DR KEGG; ath:AT2G43580; -.
DR Araport; AT2G43580; -.
DR TAIR; locus:2044009; AT2G43580.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_1_1; -.
DR InParanoid; O24598; -.
DR OMA; AHFTYET; -.
DR OrthoDB; 1574413at2759; -.
DR PhylomeDB; O24598; -.
DR BioCyc; ARA:AT2G43580-MON; -.
DR PRO; PR:O24598; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O24598; baseline and differential.
DR Genevisible; O24598; AT.
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 GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
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; 1.
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.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Plant defense;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..265
FT /note="Endochitinase At2g43580"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433912"
FT DOMAIN 25..59
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 67..265
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 27..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 29..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 34..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 52..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 265 AA; 28781 MW; 670EDB4EB480AAD3 CRC64;
MALTKIFLIL LLSLLGLYSE TVKSQNCDCA PNLCCSQFGY CGTTADYCGS TCQSGPCRVG
GPPTGAGLVG NIVTQIFFNN IINQAGNGCA GKSFYTRDSF INATNTFPSF ANTVTRREIA
TMFAHFTYET GHFCYIEEIN GASRVMCDQN NRQYPCAPAK SYHGRGPLLL SWNFNYGACG
QSLGLDLLRQ PELVSSNPVV AFRTALWFWM KSVRPVLNQG FGATIRAISG FDCDGRNLGG
VNARIGYYRD YCGQLGLDPG ANITC
