CHI7_ORYSI
ID CHI7_ORYSI Reviewed; 340 AA.
AC Q9SAY3; O64451;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Chitinase 7;
DE EC=3.2.1.14 {ECO:0000269|PubMed:10890535};
DE AltName: Full=Class I chitinase d;
DE Short=OsChia1d;
DE AltName: Full=Pathogenesis related (PR)-3 chitinase 7;
DE Flags: Precursor;
GN Name=Cht7; Synonyms=PC; ORFNames=OsI_19885;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. IR24, and cv. IR36; TISSUE=Pistil;
RX PubMed=10890535; DOI=10.1023/a:1006401816145;
RA Takakura Y., Ito T., Saito H., Inoue T., Komari T., Kuwata S.;
RT "Flower-predominant expression of a gene encoding a novel class I chitinase
RT in rice (Oryza sativa L.).";
RL Plant Mol. Biol. 42:883-897(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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 [3]
RP GENE FAMILY, AND NOMENCLATURE.
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:10890535}.
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:0000269|PubMed:10890535};
CC -!- TISSUE SPECIFICITY: Expressed in pistils, stamens and lodicules.
CC {ECO:0000269|PubMed:10890535}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
CC -!- CAUTION: Enzyme activity is uncertain. Was shown to have endochitinase
CC activity (in vitro) (PubMed:10890535). Lacks the conserved Glu residue
CC that is essential for catalytic activity, suggesting it lacks enzyme
CC activity. {ECO:0000269|PubMed:10890535, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25638.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB012855; BAA25638.1; ALT_INIT; mRNA.
DR EMBL; AB018248; BAA33762.1; -; mRNA.
DR EMBL; CM000130; EAY97967.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9SAY3; -.
DR SMR; Q9SAY3; -.
DR STRING; 39946.Q9SAY3; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PRIDE; Q9SAY3; -.
DR EnsemblPlants; BGIOSGA019834-TA; BGIOSGA019834-PA; BGIOSGA019834.
DR Gramene; BGIOSGA019834-TA; BGIOSGA019834-PA; BGIOSGA019834.
DR HOGENOM; CLU_045506_1_0_1; -.
DR OMA; CGRSCDH; -.
DR Proteomes; UP000007015; Chromosome 5.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
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; 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.
PE 1: Evidence at protein level;
KW 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 7"
FT /id="PRO_0000383467"
FT DOMAIN 33..73
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 35..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 44..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 49..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 67..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 118..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 185..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 293..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 340 AA; 35242 MW; 3D0A430B3E9F1515 CRC64;
MIAARAANLQ VAMKALALAV LALAYAAATA RAEQCGRQAG GARCPNRLCC SRWGWCGLTD
DYCKGGCQSQ CRVSRDGGDD DVAAVLLTAP GGGRAGVASV VTSDQFERML PHRDDAACPA
RGFYAYRAFV AAAGAFPAFA ATGDADTRKR EVAAFLAQTS HATSGGPYSW GYCYKEVKGA
TSDFCVPNAR WPCAPGKAYH ARGPMQIAYN YNYGAAGEAI GADLLGNPEL VATDPTVAFK
TALWLWMTAR SPSQPSPHAV VTGQWTPTPA DSAAGRAPGY GLTTNILTGG LQCAGGNGGA
DRVAFYKRYC DVLGVGYGPN LDCFGQAPFD GGIMSASAAK
