CHI9_ORYSJ
ID CHI9_ORYSJ Reviewed; 334 AA.
AC Q688M5; A0A0P0WM33;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Chitinase 9;
DE EC=3.2.1.14;
DE AltName: Full=Pathogenesis related (PR)-3 chitinase 9;
DE Flags: Precursor;
GN Name=Cht9; Synonyms=Cht1; OrderedLocusNames=Os05g0399400, LOC_Os05g33140;
GN ORFNames=P0605G01.14;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
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 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: May play a role in defense against fungal pathogens
CC containing chitin.
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 at high levels in roots, sheaths and
CC meristems. {ECO:0000269|PubMed:16936841}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; AC132492; AAU10806.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17391.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS93904.1; -; Genomic_DNA.
DR RefSeq; XP_015640433.1; XM_015784947.1.
DR AlphaFoldDB; Q688M5; -.
DR SMR; Q688M5; -.
DR STRING; 4530.OS05T0399400-00; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q688M5; -.
DR PRIDE; Q688M5; -.
DR EnsemblPlants; Os05t0399400-00; Os05t0399400-00; Os05g0399400.
DR GeneID; 4338719; -.
DR Gramene; Os05t0399400-00; Os05t0399400-00; Os05g0399400.
DR KEGG; osa:4338719; -.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_0_1; -.
DR InParanoid; Q688M5; -.
DR OMA; GYGTITN; -.
DR OrthoDB; 1132954at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
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:0050832; P:defense response to fungus; IBA:GO_Central.
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; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..334
FT /note="Chitinase 9"
FT /id="PRO_0000383469"
FT DOMAIN 24..64
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 26..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 35..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 38..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 40..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 58..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 107..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 181..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 288..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 334 AA; 34401 MW; B147004C31999D14 CRC64;
MKATTTAVAL LVAAAAMAAQ VVAEQCGSQA GGALCPNCLC CSSYGWCGST SDYCGDGCQS
QCDGCGGGGG GGGGGGGGGG GGGGAVEAVV SKELFEQLLL HRNDAACPAR GFYTYDALVT
AAAAFPDFAA TGDDEARKRE VAAFLGQTSH ETTGGWATAP DGPYSWGYCF KEEIGATASY
CVPSAEWPCA PDKKYFGRGP IQLSYNYNYG PAGEAIGEDL LNNPELVASD PVVSFKTALW
FWMTPQSPKP SCHDVITGQW TPSSGDIAAG RVPGYGVITN IINGGLECGF GPDDRVANRI
GFYQRYCDVL GIGYGSNLDC YDQRPFNSGL TAAQ
