CHIA_SOLCI
ID CHIA_SOLCI Reviewed; 253 AA.
AC Q40114; Q40113;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Acidic endochitinase pcht28;
DE EC=3.2.1.14;
DE Flags: Precursor;
OS Solanum chilense (Tomato) (Lycopersicon chilense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4083;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. LA1930; TISSUE=Leaf;
RX PubMed=7816027; DOI=10.1007/bf00283267;
RA Chen R.D., Yu L.X., Greer A.F., Cheriti H., Tabaeizadeh Z.;
RT "Isolation of an osmotic stress- and abscisic acid-induced gene encoding an
RT acidic endochitinase from Lycopersicon chilense.";
RL Mol. Gen. Genet. 245:195-202(1994).
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- INDUCTION: By osmotic stress and abscisic acid (ABA).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; L19342; AAA64999.1; -; mRNA.
DR EMBL; M97210; AAA64998.1; -; mRNA.
DR PIR; S51588; S51588.
DR PIR; S51589; S51589.
DR AlphaFoldDB; Q40114; -.
DR SMR; Q40114; -.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycosidase;
KW Hydrolase; Plant defense; Polysaccharide degradation; Secreted; Signal;
KW Stress response.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..253
FT /note="Acidic endochitinase pcht28"
FT /id="PRO_0000005298"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 212..244
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="K -> N (in Ref. 1; AAA64998)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="R -> K (in Ref. 1; AAA64998)"
FT /evidence="ECO:0000305"
FT CONFLICT 170..171
FT /note="QD -> HH (in Ref. 1; AAA64998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 27569 MW; D48C269D5A794E60 CRC64;
MKFNIVSPVA LSCLFFLFLT GTLAQNAGSI VTRELFEQML SFRNNDACPA KGFYTYDAFI
AAANSFPGFG TTGDDTARKK EIAAFFGQTS HETKGGSAGT FTGGYCFVRQ IDQSDRYYGR
GPIQLTHQSN YERAGQGIGV GQDLVNNPDL VATDPIISFR TAIWFWMTAQ DNKPSCHNVI
IGQWTPSPAD TAANRVPGYG VITNIINGGL ECNMGPNTAV ESRIGFYRRY CGMLNVPTGE
NLDCNNQKNF AQG