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Protein

Endochitinase A

Gene
N/A
Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Defense against chitin-containing fungal pathogens.1 Publication

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.2 Publications

Enzyme regulationi

Inactivated by l-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) in the absence of exogenous nucleophiles (e.g. GlcNAc4, GlcNAc3 and GlcNAc2).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1881 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase A1 Publication (EC:3.2.1.142 Publications)
Alternative name(s):
Seed chitinase A1 Publication
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi25130.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000530326 – 280Endochitinase AAdd BLAST255

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 36PROSITE-ProRule annotation
Disulfide bondi30 ↔ 42PROSITE-ProRule annotation
Disulfide bondi35 ↔ 49PROSITE-ProRule annotation
Disulfide bondi53 ↔ 58PROSITE-ProRule annotation
Disulfide bondi100 ↔ 149PROSITE-ProRule annotation
Disulfide bondi161 ↔ 170PROSITE-ProRule annotation
Disulfide bondi248 ↔ 280PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP29022.
PRIDEiP29022.

Interactioni

Protein-protein interaction databases

STRINGi4577.GRMZM2G051943_P01.

Structurei

Secondary structure

1280
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi86 – 93Combined sources8
Turni101 – 105Combined sources5
Helixi108 – 115Combined sources8
Turni119 – 122Combined sources4
Helixi127 – 145Combined sources19
Turni146 – 149Combined sources4
Beta strandi164 – 166Combined sources3
Turni180 – 183Combined sources4
Helixi187 – 197Combined sources11
Turni201 – 203Combined sources3
Helixi207 – 210Combined sources4
Helixi212 – 226Combined sources15
Helixi228 – 233Combined sources6
Helixi235 – 242Combined sources8
Beta strandi246 – 248Combined sources3
Helixi253 – 269Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MCKX-ray1.50A86-278[»]
ProteinModelPortaliP29022.
SMRiP29022.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 60Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni61 – 77Hinge region (poly-Gly)CuratedAdd BLAST17
Regioni78 – 280CatalyticCuratedAdd BLAST203

Sequence similaritiesi

Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4742. Eukaryota.
COG3979. LUCA.

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 2 hits.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29022-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:280
Mass (Da):29,125
Last modified:December 1, 1992 - v1
Checksum:i4FC5BB7D938C1CC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84164 Genomic DNA. Translation: AAA33444.1.
PIRiA42424.
UniGeneiZm.119908.
Zm.87300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84164 Genomic DNA. Translation: AAA33444.1.
PIRiA42424.
UniGeneiZm.119908.
Zm.87300.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MCKX-ray1.50A86-278[»]
ProteinModelPortaliP29022.
SMRiP29022.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G051943_P01.

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Proteomic databases

PaxDbiP29022.
PRIDEiP29022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MaizeGDBi25130.

Phylogenomic databases

eggNOGiKOG4742. Eukaryota.
COG3979. LUCA.

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 2 hits.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHIA_MAIZE
AccessioniPrimary (citable) accession number: P29022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 2, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Maize chitinase B seems to be less active than chitinase A.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.