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Protein

Endochitinase A

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

Functioni

Defense against chitin-containing fungal pathogens.1 Publication

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.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

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation
LigandChitin-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

Pathology & Biotechi

Protein family/group databases

Allergomei11981 Zea m 8.0101
7663 Zea m 8

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

Expressioni

Gene expression databases

ExpressionAtlasiP29022 differential

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

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
InterProiView 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
PfamiView protein in Pfam
PF00187 Chitin_bind_1, 1 hit
PF00182 Glyco_hydro_19, 2 hits
PIRSFiPIRSF001060 Endochitinase, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000609 Chitin_bd_1, 1 hit
SMARTiView protein in SMART
SM00270 ChtBD1, 1 hit
SUPFAMiSSF53955 SSF53955, 1 hit
SSF57016 SSF57016, 1 hit
PROSITEiView 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

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

Similar proteinsi

Entry informationi

Entry nameiCHIA_MAIZE
AccessioniPrimary (citable) accession number: P29022
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 23, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

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