CHI2_HORVU
ID CHI2_HORVU Reviewed; 266 AA.
AC P23951;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=26 kDa endochitinase 2;
DE EC=3.2.1.14;
DE AltName: Full=CHI-26;
DE Flags: Precursor;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Piggy;
RX PubMed=1899089; DOI=10.1016/s0021-9258(18)52331-0;
RA Leah R., Tommerup H., Svendsen I., Mundy J.;
RT "Biochemical and molecular characterization of three barley seed proteins
RT with antifungal properties.";
RL J. Biol. Chem. 266:1564-1573(1991).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 24-77 AND 148-188.
RC TISSUE=Endosperm;
RA Leah R., Mikkelsen J.D., Mundy J., Svendsen I.;
RT "Identification of a 28,000 dalton endochitinase in barley endosperm.";
RL Carlsberg Res. Commun. 52:31-37(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC TISSUE=Seed;
RX PubMed=8421299; DOI=10.1006/jmbi.1993.1017;
RA Hart P.J., Monzingo A.F., Ready M.P., Ernst S.R., Robertus J.D.;
RT "Crystal structure of an endochitinase from Hordeum vulgare L. seeds.";
RL J. Mol. Biol. 229:189-193(1993).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; L34210; AAA56786.1; -; Genomic_DNA.
DR EMBL; M62904; AAA32941.1; -; mRNA.
DR PIR; A29104; A29104.
DR PIR; A38664; A38664.
DR PDB; 1CNS; X-ray; 1.91 A; A/B=24-266.
DR PDB; 2BAA; X-ray; 1.80 A; A=24-266.
DR PDBsum; 1CNS; -.
DR PDBsum; 2BAA; -.
DR AlphaFoldDB; P23951; -.
DR SMR; P23951; -.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PRIDE; P23951; -.
DR BRENDA; 3.2.1.14; 2687.
DR EvolutionaryTrace; P23951; -.
DR ExpressionAtlas; P23951; baseline and differential.
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 InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SUPFAM; SSF53955; SSF53955; 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;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Plant defense; Polysaccharide degradation; Signal.
FT SIGNAL 1..23
FT CHAIN 24..266
FT /note="26 kDa endochitinase 2"
FT /id="PRO_0000005297"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 46..108
FT DISULFID 120..128
FT DISULFID 227..259
FT VARIANT 205
FT /note="D -> S"
FT CONFLICT 173
FT /note="G -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="D -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:2BAA"
FT TURN 38..42
FT /evidence="ECO:0007829|PDB:2BAA"
FT TURN 47..51
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:2BAA"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:2BAA"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1CNS"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2BAA"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2BAA"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2BAA"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:2BAA"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:2BAA"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:2BAA"
SQ SEQUENCE 266 AA; 28156 MW; 0949BE88CC20B664 CRC64;
MRSLAVVVAV VATVAMAIGT ARGSVSSIVS RAQFDRMLLH RNDGACQAKG FYTYDAFVAA
AAAFPGFGTT GSADAQKREV AAFLAQTSHE TTGGWATAPD GAFAWGYCFK QERGASSDYC
TPSAQWPCAP GKRYYGRGPI QLSHNYNYGP AGRAIGVDLL ANPDLVATDA TVGFKTAIWF
WMTAQPPKPS SHAVIAGQWS PSGADRAAGR VPGFGVITNI INGGIECGHG QDSRVADRIG
FYKRYCDILG VGYGNNLDCY SQRPFA
