CHI1_ORYSJ
ID CHI1_ORYSJ Reviewed; 323 AA.
AC Q42993; A0A0P0X1A6; Q42996; Q7DM46;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Chitinase 1;
DE EC=3.2.1.14;
DE AltName: Full=Class I chitinase a;
DE Short=OsChia1a;
DE AltName: Full=Pathogenesis related (PR)-3 chitinase 1;
DE Flags: Precursor;
GN Name=Cht1; Synonyms=CH16, RC24;
GN OrderedLocusNames=Os06g0726200, LOC_Os06g51060;
GN ORFNames=OsJ_22713, P0017G10.4, P0548E04.24;
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].
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 [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of chitinase genes in rice seeds.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [MRNA] OF 21-323.
RC STRAIN=cv. Nipponbare;
RA Nishizawa Y., Hibi T.;
RT "Isolation and characterization of a cDNA for rice chitinase.";
RL Plant Sci. 76:211-218(1991).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=8605293; DOI=10.1007/bf00049319;
RA Xu Y., Zhu Q., Panbangred W., Shirasu K., Lamb C.;
RT "Regulation, expression and function of a new basic chitinase gene in rice
RT (Oryza sativa L.).";
RL Plant Mol. Biol. 30:387-401(1996).
RN [8]
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).
CC -!- FUNCTION: Hydrolyzes chitin and may play a role in defense against
CC fungal pathogens containing chitin. {ECO:0000269|PubMed:8605293}.
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, leaves, sheaths and meristems.
CC {ECO:0000269|PubMed:16936841}.
CC -!- INDUCTION: By fungal elicitor and wounding.
CC {ECO:0000269|PubMed:8605293}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; D16221; BAA03749.1; -; Genomic_DNA.
DR EMBL; EF122477; ABL74564.1; -; mRNA.
DR EMBL; AP003685; BAD61709.1; -; Genomic_DNA.
DR EMBL; AP004685; BAD61801.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS99596.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ38338.1; -; Genomic_DNA.
DR EMBL; X56063; CAA39535.1; -; mRNA.
DR PIR; T03614; T03614.
DR AlphaFoldDB; Q42993; -.
DR SMR; Q42993; -.
DR STRING; 4530.OS06T0726200-02; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q42993; -.
DR PRIDE; Q42993; -.
DR EnsemblPlants; Os06t0726200-02; Os06t0726200-02; Os06g0726200.
DR Gramene; Os06t0726200-02; Os06t0726200-02; Os06g0726200.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_0_1; -.
DR InParanoid; Q42993; -.
DR OMA; CEPSATW; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q42993; OS.
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; IEP: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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..323
FT /note="Chitinase 1"
FT /id="PRO_5000139668"
FT DOMAIN 21..61
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 23..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 32..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 35..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 37..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 55..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 100..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 176..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 283..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 323 AA; 33765 MW; 1C85B6227A33EB06 CRC64;
MRALAVVVVA TAFAVVAVRG EQCGSQAGGA LCPNCLCCSQ YGWCGSTSAY CGSGCQSQCS
GSCGGGGPTP PSGGGGSGVA SIVSRSLFDQ MLLHRNDAAC PAKNFYTYDA FVAAANAFPS
FATTGDAATR KREVAAFLAQ TSHETTGGWA TAPDGPYSWG YCFKEENNGN VGSDYCVQSS
QWPCAAGKKY YGRGPIQISY NYNYGPAGQA IGSNLLSNPD LVASDATVSF KTAFWFWMTP
QSPKPSCHAV MTGQWTPNGN DQAAGRVPGY GVVTNIINGG VECGHGADSR VADRIGFYKR
YCDMLGVSYG ANLDCYNQRP FNS
