CHIA_MAIZE
ID CHIA_MAIZE Reviewed; 280 AA.
AC P29022;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Endochitinase A {ECO:0000303|PubMed:1551872};
DE EC=3.2.1.14 {ECO:0000269|PubMed:1551872, ECO:0000269|PubMed:1740436, ECO:0000269|PubMed:24616181, ECO:0000269|PubMed:28328103};
DE AltName: Full=ChitA {ECO:0000303|PubMed:24616181};
DE AltName: Full=Chitinase-A {ECO:0000303|PubMed:28328103};
DE AltName: Full=Seed chitinase A {ECO:0000303|PubMed:1551872};
DE AltName: Allergen=Zea m 8 {ECO:0000305|PubMed:28328103};
DE Flags: Precursor;
GN Name=CHIA {ECO:0000303|PubMed:28328103};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Seed;
RX PubMed=1551872; DOI=10.1016/s0021-9258(19)50474-4;
RA Huynh Q.K., Hironaka C.M., Levine E.B., Smith C.E., Borgmeyer J.R.,
RA Shah D.M.;
RT "Antifungal proteins from plants. Purification, molecular cloning, and
RT antifungal properties of chitinases from maize seed.";
RL J. Biol. Chem. 267:6635-6640(1992).
RN [2]
RP PROTEIN SEQUENCE OF 180-195, AND ACTIVITY REGULATION.
RC TISSUE=Seed;
RX PubMed=1740436; DOI=10.1016/s0021-9258(19)50609-3;
RA Verburg J.G., Smith C.E., Lisek C.A., Huynh Q.K.;
RT "Identification of an essential tyrosine residue in the catalytic site of a
RT chitinase isolated from Zea mays that is selectively modified during
RT inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide.";
RL J. Biol. Chem. 267:3886-3893(1992).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND ALLERGEN.
RX PubMed=28328103; DOI=10.1111/all.13164;
RA Volpicella M., Leoni C., Fanizza I., Distaso M., Leoni G., Farioli L.,
RA Naumann T., Pastorello E., Ceci L.R.;
RT "Characterization of maize chitinase-A, a tough allergenic molecule.";
RL Allergy 72:1423-1429(2017).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 86-278 OF MUTANT GLN-144,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, ACTIVE SITES, SITE,
RP DISULFIDE BONDS, AND MUTAGENESIS OF GLU-144.
RX PubMed=24616181; DOI=10.1002/pro.2437;
RA Chaudet M.M., Naumann T.A., Price N.P., Rose D.R.;
RT "Crystallographic structure of ChitA, a glycoside hydrolase family 19,
RT plant class IV chitinase from Zea mays.";
RL Protein Sci. 23:586-593(2014).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens
CC (PubMed:1551872). Hydrolyzes glycol chitin and tetra-N-
CC acetylchitotetraose in vitro (PubMed:28328103).
CC {ECO:0000269|PubMed:1551872, ECO:0000269|PubMed:28328103}.
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:1551872, ECO:0000269|PubMed:1740436,
CC ECO:0000269|PubMed:24616181, ECO:0000269|PubMed:28328103};
CC -!- ACTIVITY REGULATION: Inactivated by l-ethyl-3-(3-
CC dimethylaminopropyl)carbodiimide (EDC) in the absence of exogenous
CC nucleophiles (e.g. GlcNAc4, GlcNAc3 and GlcNAc2) (PubMed:1740436). Not
CC inhibited by tetra-N-acetylchitopentaose or modified chitotetraose
CC substrate TMG-chitotriomycin-pMP, containing a free, non-acetylated
CC glucosaminyl residue or a N-trimethylamino glucosamine (TMG) residue at
CC the non-reducing terminus, respectively (PubMed:24616181).
CC {ECO:0000269|PubMed:1740436, ECO:0000269|PubMed:24616181}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.97 mM for tetra-N-acetylchitotetraose (at 37 degrees Celsius and
CC pH 6) {ECO:0000269|PubMed:28328103};
CC KM=0.51 mM for tetra-N-acetylchitotetraose (at 37 degrees Celsius and
CC pH 4) {ECO:0000269|PubMed:28328103};
CC KM=1.27 mM for tetra-N-acetylchitotetraose (at 50 degrees Celsius and
CC pH 6) {ECO:0000269|PubMed:28328103};
CC KM=1.29 mM for tetra-N-acetylchitotetraose (at 70 degrees Celsius and
CC pH 6) {ECO:0000269|PubMed:28328103};
CC Note=kcat is 56.27 sec(-1) with tetra-N-acetylchitotetraose as
CC substrate (at 37 degrees Celsius and pH 6). kcat is 55.67 sec(-1)
CC with tetra-N-acetylchitotetraose as substrate (at 37 degrees Celsius
CC and pH 4). kcat is 69.01 sec(-1) with tetra-N-acetylchitotetraose as
CC substrate (at 50 degrees Celsius and pH 6). kcat is 53.1 sec(-1) with
CC tetra-N-acetylchitotetraose as substrate (at 70 degrees Celsius and
CC pH 6). {ECO:0000269|PubMed:28328103};
CC pH dependence:
CC Active between pH 6-3. {ECO:0000269|PubMed:28328103};
CC Temperature dependence:
CC Active between 50-70 degrees Celsius. {ECO:0000269|PubMed:28328103};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28328103}.
CC -!- DOMAIN: The N-terminal domain is not required for catalytic activity,
CC but it is involved in substrate binding. {ECO:0000269|PubMed:24616181}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Food allergenic protein
CC which binds IgE from sera of patients allergic to maize.
CC {ECO:0000269|PubMed:28328103}.
CC -!- MISCELLANEOUS: Maize chitinase B seems to be less active than chitinase
CC A. {ECO:0000269|PubMed:1551872}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class IV subfamily. {ECO:0000305}.
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DR EMBL; M84164; AAA33444.1; -; Genomic_DNA.
DR PIR; A42424; A42424.
DR PDB; 4MCK; X-ray; 1.50 A; A=86-278.
DR PDBsum; 4MCK; -.
DR AlphaFoldDB; P29022; -.
DR SMR; P29022; -.
DR STRING; 4577.GRMZM2G051943_P01; -.
DR Allergome; 11981; Zea m 8.0101.
DR Allergome; 7663; Zea m 8.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; P29022; -.
DR PRIDE; P29022; -.
DR MaizeGDB; 25130; -.
DR eggNOG; KOG4742; Eukaryota.
DR BRENDA; 3.2.1.14; 6752.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P29022; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0008843; F:endochitinase activity; IDA:UniProtKB.
DR GO; GO:0006040; P:amino sugar metabolic process; 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; IDA: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; 2.
DR PIRSF; PIRSF001060; Endochitinase; 1.
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 1: Evidence at protein level;
KW 3D-structure; Allergen; Carbohydrate metabolism; Chitin degradation;
KW Chitin-binding; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Plant defense; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..280
FT /note="Endochitinase A"
FT /id="PRO_0000005303"
FT DOMAIN 26..60
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 61..77
FT /note="Hinge region (poly-Gly)"
FT /evidence="ECO:0000305"
FT REGION 78..280
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:24616181"
FT DISULFID 28..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 30..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 35..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 53..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 100..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:24616181, ECO:0007744|PDB:4MCK"
FT DISULFID 161..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:24616181, ECO:0007744|PDB:4MCK"
FT DISULFID 248..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:24616181, ECO:0007744|PDB:4MCK"
FT MUTAGEN 144
FT /note="E->Q: Loss of catalytic activity. No effect on
FT substrate binding or overall structure of the catalytic
FT domain."
FT /evidence="ECO:0000269|PubMed:24616181"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:4MCK"
FT TURN 101..105
FT /evidence="ECO:0007829|PDB:4MCK"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:4MCK"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:4MCK"
FT HELIX 127..145
FT /evidence="ECO:0007829|PDB:4MCK"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:4MCK"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4MCK"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:4MCK"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:4MCK"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:4MCK"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:4MCK"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:4MCK"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:4MCK"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:4MCK"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:4MCK"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:4MCK"
SQ SEQUENCE 280 AA; 29125 MW; 4FC5BB7D938C1CC1 CRC64;
MANAPRILAL GLLALLCAAA GPAAAQNCGC QPNFCCSKFG YCGTTDAYCG DGCQSGPCRS
GGGGGGGGGG GGGGSGGANV ANVVTDAFFN GIKNQAGSGC EGKNFYTRSA FLSAVNAYPG
FAHGGTEVEG KREIAAFFAH VTHETGHFCY ISEINKSNAY CDASNRQWPC AAGQKYYGRG
PLQISWNYNY GPAGRDIGFN GLADPNRVAQ DAVIAFKTAL WFWMNNVHGV MPQGFGATIR
AINGALECNG NNPAQMNARV GYYKQYCQQL RVDPGPNLIC
