CHI61_ARATH
ID CHI61_ARATH Reviewed; 281 AA.
AC O22842;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Endochitinase At2g43610 {ECO:0000305};
DE EC=3.2.1.14;
DE Flags: Precursor;
GN OrderedLocusNames=At2g43610 {ECO:0000312|EMBL:AAL62349.1};
GN ORFNames=F18O19.28 {ECO:0000312|EMBL:AEC10295.1};
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=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 [4]
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 -!- INTERACTION:
CC O22842; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-25530116, EBI-25519488;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; AC002333; AAB64045.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10295.1; -; Genomic_DNA.
DR EMBL; AY072357; AAL62349.1; -; mRNA.
DR EMBL; AY114724; AAM48043.1; -; mRNA.
DR PIR; C84868; C84868.
DR RefSeq; NP_181889.1; NM_129923.4.
DR AlphaFoldDB; O22842; -.
DR SMR; O22842; -.
DR IntAct; O22842; 1.
DR STRING; 3702.AT2G43610.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR MetOSite; O22842; -.
DR SwissPalm; O22842; -.
DR PaxDb; O22842; -.
DR PRIDE; O22842; -.
DR ProteomicsDB; 246780; -.
DR EnsemblPlants; AT2G43610.1; AT2G43610.1; AT2G43610.
DR GeneID; 818963; -.
DR Gramene; AT2G43610.1; AT2G43610.1; AT2G43610.
DR KEGG; ath:AT2G43610; -.
DR Araport; AT2G43610; -.
DR TAIR; locus:2043934; AT2G43610.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_1_1; -.
DR InParanoid; O22842; -.
DR OMA; ISSACKG; -.
DR OrthoDB; 1574413at2759; -.
DR PhylomeDB; O22842; -.
DR BioCyc; ARA:AT2G43610-MON; -.
DR PRO; PR:O22842; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22842; baseline and differential.
DR Genevisible; O22842; AT.
DR GO; GO:0005886; C:plasma membrane; 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 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 1: Evidence at protein 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..281
FT /note="Endochitinase At2g43610"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433915"
FT DOMAIN 29..66
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 86..281
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT CARBOHYD 278
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 281 AA; 29999 MW; 2E397E39A7762CCD CRC64;
MATQNAILKK ALIIFLFTLT IMTGTAFSQN CGTNGCKGNM CCSRWGYCGT TKAYCGTGCQ
SGPCNSKPKP TPTPSGSGGL NAGPRGTIAS VITPAFFNSI MSKVGSGCPA KGFYTRQAFI
AAAESFAAYK GTVAKREIAA MLAQFSHESG SFCYKEEIAR GRYCSPSTTY PCQPGKNYYG
RGPIQITWNY NYGAAGKFLG LPLLKDPDMV ARSPTVAFQC AMWFWNKNVR PVLSQGFGAT
TRRINGGECN GGRPAAVQSR VNHYLDFCKK LGVTPGTNLS C