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Protein

Endochitinase A

Gene
N/A
Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Defense against chitin containing fungal pathogens.

Catalytic activityi

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

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 A (EC:3.2.1.14)
Alternative name(s):
Seed chitinase A
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305 Componenti: Unplaced

Organism-specific databases

GrameneiP29022.
MaizeGDBi25130.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 280255Endochitinase APRO_0000005303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

PRIDEiP29022.

Interactioni

Protein-protein interaction databases

STRINGi4577.GRMZM2G051943_P01.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi86 – 938Combined sources
Turni101 – 1055Combined sources
Helixi108 – 1158Combined sources
Turni119 – 1224Combined sources
Helixi127 – 14519Combined sources
Turni146 – 1494Combined sources
Beta strandi164 – 1663Combined sources
Turni180 – 1834Combined sources
Helixi187 – 19711Combined sources
Turni201 – 2033Combined sources
Helixi207 – 2104Combined sources
Helixi212 – 22615Combined sources
Helixi228 – 2336Combined sources
Helixi235 – 2428Combined sources
Beta strandi246 – 2483Combined sources
Helixi253 – 26917Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6035Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni61 – 7717Hinge region (poly-Gly)Add
BLAST
Regioni78 – 280203CatalyticAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

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. 1 hit.
[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.

Cross-referencesi

Sequence databases

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

3D structure databases

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

PRIDEiP29022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP29022.
MaizeGDBi25130.

Family and domain databases

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. 1 hit.
[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...

Publicationsi

  1. "Antifungal proteins from plants. Purification, molecular cloning, and antifungal properties of chitinases from maize seed."
    Huynh Q.K., Hironaka C.M., Levine E.B., Smith C.E., Borgmeyer J.R., Shah D.M.
    J. Biol. Chem. 267:6635-6640(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Seed.
  2. "Identification of an essential tyrosine residue in the catalytic site of a chitinase isolated from Zea mays that is selectively modified during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide."
    Verburg J.G., Smith C.E., Lisek C.A., Huynh Q.K.
    J. Biol. Chem. 267:3886-3893(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 180-195.
    Tissue: Seed.

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: June 24, 2015
This is version 103 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.

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

External Data

Dasty 3

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 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.