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   24-JAN-2024, entry version 114.
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;
GN   OrderedLocusNames=Os05g0399300, LOC_Os05g33130; 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; 39947.Q7DNA1; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   PaxDb; 39947-Q7DNA1; -.
DR   EnsemblPlants; Os05t0399300-01; Os05t0399300-01; Os05g0399300.
DR   GeneID; 4338718; -.
DR   Gramene; Os05t0399300-01; Os05t0399300-01; Os05g0399300.
DR   KEGG; osa:4338718; -.
DR   eggNOG; KOG4742; Eukaryota.
DR   HOGENOM; CLU_045506_4_0_1; -.
DR   InParanoid; Q7DNA1; -.
DR   OrthoDB; 997724at2759; -.
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   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd06921; ChtBD1_GH19_hevein; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 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   PANTHER; PTHR22595:SF140; CHITINASE 2; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
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; Lysozyme-like; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 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
//