CHI2_ORYSJ
ID CHI2_ORYSJ Reviewed; 340 AA.
AC Q7DNA1; Q0DID3; Q43294;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Chitinase 2;
DE EC=3.2.1.14;
DE AltName: Full=Class I chitinase b;
DE Short=OsChia1b;
DE AltName: Full=Pathogenesis related (PR)-3 chitinase 2;
DE Flags: Precursor;
GN Name=Cht2; Synonyms=RC7; OrderedLocusNames=Os05g0399300, LOC_Os05g33130;
GN ORFNames=OsJ_18467;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=7901749; DOI=10.1007/bf00280194;
RA Nishizawa Y., Kishimoto N., Saito A., Hibi T.;
RT "Sequence variation, differential expression and chromosomal location of
RT rice chitinase genes.";
RL Mol. Gen. Genet. 241:1-10(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION.
RX PubMed=11166426; DOI=10.1016/s0168-9452(00)00413-1;
RA Datta K., Tu J., Oliva N., Ona I., Velazhahan R., Mew T.W.,
RA Muthukrishnan S., Datta S.K.;
RT "Enhanced resistance to sheath blight by constitutive expression of
RT infection-related rice chitinase in transgenic elite indica rice
RT cultivars.";
RL Plant Sci. 160:405-414(2001).
RN [7]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=16936841; DOI=10.1139/g06-020;
RA Nakazaki T., Tsukiyama T., Okumoto Y., Kageyama D., Naito K., Inouye K.,
RA Tanisaka T.;
RT "Distribution, structure, organ-specific expression, and phylogenic
RT analysis of the pathogenesis-related protein-3 chitinase gene family in
RT rice (Oryza sativa L.).";
RL Genome 49:619-630(2006).
RN [8]
RP FUNCTION.
RX PubMed=18323646; DOI=10.1271/bbb.70693;
RA Mizuno R., Itoh Y., Nishizawa Y., Kezuka Y., Suzuki K., Nonaka T.,
RA Watanabe T.;
RT "Purification and characterization of a rice class I chitinase, OsChia1b,
RT produced in Esherichia coli.";
RL Biosci. Biotechnol. Biochem. 72:893-895(2008).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF TRP-159.
RX PubMed=18211919; DOI=10.1093/jb/mvn004;
RA Mizuno R., Fukamizo T., Sugiyama S., Nishizawa Y., Kezuka Y., Nonaka T.,
RA Suzuki K., Watanabe T.;
RT "Role of the loop structure of the catalytic domain in rice class I
RT chitinase.";
RL J. Biochem. 143:487-495(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-340, AND DISULFIDE BONDS.
RX PubMed=15327374; DOI=10.2174/0929866043406968;
RA Kezuka Y., Kitazaki K., Itoh Y., Watanabe J., Takaha O., Watanabe T.,
RA Nishizawa Y., Nonaka T.;
RT "Crystallization and preliminary X-ray analysis of plant class I chitinase
RT from rice.";
RL Protein Pept. Lett. 11:401-405(2004).
CC -!- FUNCTION: Hydrolyzes chitin and plays a role in defense against fungal
CC pathogens containing chitin. Its overexpression confers enhanced
CC resistance to sheath blight pathogen (R.solani).
CC {ECO:0000269|PubMed:11166426, ECO:0000269|PubMed:18211919,
CC ECO:0000269|PubMed:18323646}.
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 -!- TISSUE SPECIFICITY: Expressed in roots, sheaths and meristems.
CC {ECO:0000269|PubMed:16936841}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF17390.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D16222; BAA03750.1; -; Genomic_DNA.
DR EMBL; X56787; CAA40107.1; -; mRNA.
DR EMBL; AP008211; BAF17390.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000142; EEE63650.1; -; Genomic_DNA.
DR PIR; S39979; S39979.
DR PIR; S40414; S40414.
DR RefSeq; XP_015640432.1; XM_015784946.1.
DR PDB; 2DKV; X-ray; 2.00 A; A=33-340.
DR PDB; 3IWR; X-ray; 2.57 A; A/B=33-340.
DR PDBsum; 2DKV; -.
DR PDBsum; 3IWR; -.
DR AlphaFoldDB; Q7DNA1; -.
DR SMR; Q7DNA1; -.
DR STRING; 4530.OS05T0399300-01; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q7DNA1; -.
DR PRIDE; Q7DNA1; -.
DR GeneID; 4338718; -.
DR KEGG; osa:4338718; -.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_4_0_1; -.
DR InParanoid; Q7DNA1; -.
DR OrthoDB; 1132954at2759; -.
DR EvolutionaryTrace; Q7DNA1; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
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:0050832; P:defense response to fungus; IDA:UniProtKB.
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; 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..340
FT /note="Chitinase 2"
FT /id="PRO_5000139669"
FT DOMAIN 33..73
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 154
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 35..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:15327374"
FT DISULFID 44..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:15327374"
FT DISULFID 47..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:15327374"
FT DISULFID 49..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:15327374"
FT DISULFID 67..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:15327374"
FT DISULFID 110..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:15327374"
FT DISULFID 184..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:15327374"
FT DISULFID 291..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:15327374"
FT MUTAGEN 159
FT /note="W->A: Increased activity."
FT /evidence="ECO:0000269|PubMed:18211919"
FT TURN 37..41
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2DKV"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:2DKV"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:2DKV"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:2DKV"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:2DKV"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 137..155
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2DKV"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2DKV"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:2DKV"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:2DKV"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:2DKV"
FT HELIX 297..312
FT /evidence="ECO:0007829|PDB:2DKV"
SQ SEQUENCE 340 AA; 35587 MW; 642F13E3928CA7BE CRC64;
MSTPRAAASL AKKAALVALA VLAAALATAA RAEQCGAQAG GARCPNCLCC SRWGWCGTTS
DFCGDGCQSQ CSGCGPTPTP TPPSPSDGVG SIVPRDLFER LLLHRNDGAC PARGFYTYEA
FLAAAAAFPA FGGTGNTETR KREVAAFLGQ TSHETTGGWP TAPDGPFSWG YCFKQEQNPP
SDYCQPSPEW PCAPGRKYYG RGPIQLSFNF NYGPAGRAIG VDLLSNPDLV ATDATVSFKT
ALWFWMTPQG NKPSSHDVIT GRWAPSPADA AAGRAPGYGV ITNIVNGGLE CGHGPDDRVA
NRIGFYQRYC GAFGIGTGGN LDCYNQRPFN SGSSVGLAEQ
