CHI59_ARATH
ID CHI59_ARATH Reviewed; 264 AA.
AC O24658;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Endochitinase At2g43590 {ECO:0000305};
DE EC=3.2.1.14;
DE Flags: Precursor;
GN OrderedLocusNames=At2g43590 {ECO:0000312|EMBL:AEC10293.1};
GN ORFNames=F18O19.30 {ECO:0000312|EMBL:AEC10293.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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).
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; AAB64047.1; -; Genomic_DNA.
DR EMBL; AC002335; AAM14810.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10293.1; -; Genomic_DNA.
DR EMBL; BT009726; AAP88360.1; -; mRNA.
DR EMBL; AK228181; BAF00136.1; -; mRNA.
DR PIR; A84868; A84868.
DR RefSeq; NP_181887.1; NM_129921.6.
DR AlphaFoldDB; O24658; -.
DR SMR; O24658; -.
DR STRING; 3702.AT2G43590.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; O24658; -.
DR PRIDE; O24658; -.
DR ProteomicsDB; 246598; -.
DR EnsemblPlants; AT2G43590.1; AT2G43590.1; AT2G43590.
DR GeneID; 818961; -.
DR Gramene; AT2G43590.1; AT2G43590.1; AT2G43590.
DR KEGG; ath:AT2G43590; -.
DR Araport; AT2G43590; -.
DR TAIR; locus:2043994; AT2G43590.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_1_1; -.
DR InParanoid; O24658; -.
DR OMA; FCYVEEI; -.
DR OrthoDB; 1574413at2759; -.
DR PhylomeDB; O24658; -.
DR BioCyc; ARA:AT2G43590-MON; -.
DR PRO; PR:O24658; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O24658; baseline and differential.
DR Genevisible; O24658; AT.
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 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..264
FT /note="Endochitinase At2g43590"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433913"
FT DOMAIN 25..59
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 66..264
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT CARBOHYD 261
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 264 AA; 28353 MW; DBBD0F3FA82D19E5 CRC64;
MAFTKISLVL LLCLLGFFSE TVKSQNCGCA PNLCCSQFGY CGTDDAYCGV GCRSGPCRGS
GTPTGGSVGS IVTQGFFNNI INQAGNGCAG KRFYTRDSFV NAANTFPNFA NSVTRREIAT
MFAHFTHETG HFCYIEEING ATRNYCQSSN TQYPCAPGKG YFGRGPIQLS WNYNYGACGQ
SLGLDLLRQP ELVGSNPTVA FRTGLWFWMN SVRPVLNQGF GATIRAINGM ECNGGNSGAV
NARIGYYRDY CGQLGVDPGP NLSC
