UniProtKB - P29022 (CHIA_MAIZE)
Protein
Endochitinase A
Gene
CHIA
Organism
Zea mays (Maize)
Status
Functioni
Defense against chitin-containing fungal pathogens (PubMed:1551872). Hydrolyzes glycol chitin and tetra-N-acetylchitotetraose in vitro (PubMed:28328103).2 Publications
Miscellaneous
Maize chitinase B seems to be less active than chitinase A.1 Publication
Catalytic activityi
- Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.4 Publications EC:3.2.1.14
Activity regulationi
Inactivated by l-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) in the absence of exogenous nucleophiles (e.g. GlcNAc4, GlcNAc3 and GlcNAc2) (PubMed:1740436). Not inhibited by tetra-N-acetylchitopentaose or modified chitotetraose substrate TMG-chitotriomycin-pMP, containing a free, non-acetylated glucosaminyl residue or a N-trimethylamino glucosamine (TMG) residue at the non-reducing terminus, respectively (PubMed:24616181).2 Publications
Kineticsi
kcat is 56.27 s(-1) with tetra-N-acetylchitotetraose as substrate (at 37 degrees Celsius and pH 6). kcat is 55.67 s(-1) with tetra-N-acetylchitotetraose as substrate (at 37 degrees Celsius and pH 4). kcat is 69.01 s(-1) with tetra-N-acetylchitotetraose as substrate (at 50 degrees Celsius and pH 6). kcat is 53.1 s(-1) with tetra-N-acetylchitotetraose as substrate (at 70 degrees Celsius and pH 6).1 Publication
- KM=0.97 mM for tetra-N-acetylchitotetraose (at 37 degrees Celsius and pH 6)1 Publication
- KM=0.51 mM for tetra-N-acetylchitotetraose (at 37 degrees Celsius and pH 4)1 Publication
- KM=1.27 mM for tetra-N-acetylchitotetraose (at 50 degrees Celsius and pH 6)1 Publication
- KM=1.29 mM for tetra-N-acetylchitotetraose (at 70 degrees Celsius and pH 6)1 Publication
pH dependencei
Active between pH 6-3.1 Publication
Temperature dependencei
Active between 50-70 degrees Celsius.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 144 | Proton donor1 Publication | 1 |
GO - Molecular functioni
- chitinase activity Source: GO_Central
- chitin binding Source: UniProtKB-KW
- endochitinase activity Source: UniProtKB
GO - Biological processi
- amino sugar metabolic process Source: UniProtKB
- cell wall macromolecule catabolic process Source: InterPro
- chitin catabolic process Source: UniProtKB-KW
- defense response to fungus Source: UniProtKB
- polysaccharide catabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Biological process | Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation |
Ligand | Chitin-binding |
Protein family/group databases
CAZyi | CBM18, Carbohydrate-Binding Module Family 18 GH19, Glycoside Hydrolase Family 19 |
Names & Taxonomyi
Protein namesi | Recommended name: Endochitinase A1 Publication (EC:3.2.1.144 Publications)Alternative name(s): ChitA1 Publication Chitinase-A1 Publication Seed chitinase A1 Publication Allergen: Zea m 81 Publication |
Gene namesi | Name:CHIA1 Publication |
Organismi | Zea mays (Maize) |
Taxonomic identifieri | 4577 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogonodae › Andropogoneae › Tripsacinae › Zea |
Proteomesi |
|
Organism-specific databases
MaizeGDBi | 25130 |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB
Keywords - Cellular componenti
SecretedPathology & Biotechi
Allergenic propertiesi
Causes an allergic reaction in human. Food allergenic protein which binds IgE from sera of patients allergic to maize.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 144 | E → Q: Loss of catalytic activity. No effect on substrate binding or overall structure of the catalytic domain. 1 Publication | 1 |
Keywords - Diseasei
AllergenProtein family/group databases
Allergomei | 11981, Zea m 8.0101 7663, Zea m 8 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | Sequence analysisAdd BLAST | 25 | |
ChainiPRO_0000005303 | 26 – 280 | Endochitinase AAdd BLAST | 255 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 28 ↔ 36 | PROSITE-ProRule annotation | ||
Disulfide bondi | 30 ↔ 42 | PROSITE-ProRule annotation | ||
Disulfide bondi | 35 ↔ 49 | PROSITE-ProRule annotation | ||
Disulfide bondi | 53 ↔ 58 | PROSITE-ProRule annotation | ||
Disulfide bondi | 100 ↔ 149 | PROSITE-ProRule annotationCombined sources1 Publication | ||
Disulfide bondi | 161 ↔ 170 | PROSITE-ProRule annotationCombined sources1 Publication | ||
Disulfide bondi | 248 ↔ 280 | PROSITE-ProRule annotationCombined sources1 Publication |
Keywords - PTMi
Disulfide bondProteomic databases
PaxDbi | P29022 |
PRIDEi | P29022 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P29022 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 26 – 60 | Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST | 35 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 61 – 77 | Hinge region (poly-Gly)CuratedAdd BLAST | 17 | |
Regioni | 78 – 280 | CatalyticCuratedAdd BLAST | 203 |
Domaini
The N-terminal domain is not required for catalytic activity, but it is involved in substrate binding.1 Publication
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG4742, Eukaryota |
Family and domain databases
Gene3Di | 3.30.60.10, 1 hit |
InterProi | View protein in InterPro IPR001002, Chitin-bd_1 IPR018371, Chitin-binding_1_CS IPR036861, Endochitinase-like_sf IPR016283, Glyco_hydro_19 IPR000726, Glyco_hydro_19_cat IPR023346, Lysozyme-like_dom_sf |
Pfami | View protein in Pfam PF00187, Chitin_bind_1, 1 hit PF00182, Glyco_hydro_19, 2 hits |
PIRSFi | PIRSF001060, Endochitinase, 1 hit |
SMARTi | View protein in SMART SM00270, ChtBD1, 1 hit |
SUPFAMi | SSF53955, SSF53955, 1 hit SSF57016, SSF57016, 1 hit |
PROSITEi | View protein in PROSITE PS00026, CHIT_BIND_I_1, 1 hit PS50941, CHIT_BIND_I_2, 1 hit PS00773, CHITINASE_19_1, 1 hit PS00774, CHITINASE_19_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P29022-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MANAPRILAL GLLALLCAAA GPAAAQNCGC QPNFCCSKFG YCGTTDAYCG
60 70 80 90 100
DGCQSGPCRS GGGGGGGGGG GGGGSGGANV ANVVTDAFFN GIKNQAGSGC
110 120 130 140 150
EGKNFYTRSA FLSAVNAYPG FAHGGTEVEG KREIAAFFAH VTHETGHFCY
160 170 180 190 200
ISEINKSNAY CDASNRQWPC AAGQKYYGRG PLQISWNYNY GPAGRDIGFN
210 220 230 240 250
GLADPNRVAQ DAVIAFKTAL WFWMNNVHGV MPQGFGATIR AINGALECNG
260 270 280
NNPAQMNARV GYYKQYCQQL RVDPGPNLIC
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M84164 Genomic DNA Translation: AAA33444.1 |
PIRi | A42424 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M84164 Genomic DNA Translation: AAA33444.1 |
PIRi | A42424 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4MCK | X-ray | 1.50 | A | 86-278 | [»] | |
SMRi | P29022 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 4577.GRMZM2G051943_P01 |
Protein family/group databases
Allergomei | 11981, Zea m 8.0101 7663, Zea m 8 |
CAZyi | CBM18, Carbohydrate-Binding Module Family 18 GH19, Glycoside Hydrolase Family 19 |
Proteomic databases
PaxDbi | P29022 |
PRIDEi | P29022 |
Organism-specific databases
MaizeGDBi | 25130 |
Phylogenomic databases
eggNOGi | KOG4742, Eukaryota |
Gene expression databases
ExpressionAtlasi | P29022, baseline and differential |
Family and domain databases
Gene3Di | 3.30.60.10, 1 hit |
InterProi | View protein in InterPro IPR001002, Chitin-bd_1 IPR018371, Chitin-binding_1_CS IPR036861, Endochitinase-like_sf IPR016283, Glyco_hydro_19 IPR000726, Glyco_hydro_19_cat IPR023346, Lysozyme-like_dom_sf |
Pfami | View protein in Pfam PF00187, Chitin_bind_1, 1 hit PF00182, Glyco_hydro_19, 2 hits |
PIRSFi | PIRSF001060, Endochitinase, 1 hit |
SMARTi | View protein in SMART SM00270, ChtBD1, 1 hit |
SUPFAMi | SSF53955, SSF53955, 1 hit SSF57016, SSF57016, 1 hit |
PROSITEi | View protein in PROSITE PS00026, CHIT_BIND_I_1, 1 hit PS50941, CHIT_BIND_I_2, 1 hit PS00773, CHITINASE_19_1, 1 hit PS00774, CHITINASE_19_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CHIA_MAIZE | |
Accessioni | P29022Primary (citable) accession number: P29022 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 1992 |
Last sequence update: | December 1, 1992 | |
Last modified: | April 7, 2021 | |
This is version 131 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families