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P29022

- CHIA_MAIZE

UniProt

P29022 - CHIA_MAIZE

Protein

Endochitinase A

Gene
N/A
Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    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

    1. chitinase activity Source: UniProtKB-EC
    2. chitin binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. chitin catabolic process Source: UniProtKB-KW
    3. defense response Source: UniProtKB-KW
    4. polysaccharide catabolic process Source: UniProtKB-KW
    5. somatic embryogenesis Source: EnsemblPlants/Gramene

    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

    Organism-specific databases

    GrameneiP29022.
    MaizeGDBi25130.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: EnsemblPlants/Gramene
    2. plant-type cell wall Source: EnsemblPlants/Gramene
    3. plasma membrane Source: EnsemblPlants/Gramene

    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.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MANAPRILAL GLLALLCAAA GPAAAQNCGC QPNFCCSKFG YCGTTDAYCG    50
    DGCQSGPCRS GGGGGGGGGG GGGGSGGANV ANVVTDAFFN GIKNQAGSGC 100
    EGKNFYTRSA FLSAVNAYPG FAHGGTEVEG KREIAAFFAH VTHETGHFCY 150
    ISEINKSNAY CDASNRQWPC AAGQKYYGRG PLQISWNYNY GPAGRDIGFN 200
    GLADPNRVAQ DAVIAFKTAL WFWMNNVHGV MPQGFGATIR AINGALECNG 250
    NNPAQMNARV GYYKQYCQQL RVDPGPNLIC 280
    Length:280
    Mass (Da):29,125
    Last modified:December 1, 1992 - v1
    Checksum:i4FC5BB7D938C1CC1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84164 Genomic DNA. Translation: AAA33444.1.
    PIRiA42424.
    UniGeneiZm.119908.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84164 Genomic DNA. Translation: AAA33444.1 .
    PIRi A42424.
    UniGenei Zm.119908.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4MCK X-ray 1.50 A 86-278 [» ]
    ProteinModelPortali P29022.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM18. Carbohydrate-Binding Module Family 18.
    GH19. Glycoside Hydrolase Family 19.

    Proteomic databases

    PRIDEi P29022.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei P29022.
    MaizeGDBi 25130.

    Family and domain databases

    Gene3Di 3.30.60.10. 1 hit.
    InterProi IPR001002. Chitin-bd_1.
    IPR018371. Chitin-binding_1_CS.
    IPR016283. Glyco_hydro_19.
    IPR000726. Glyco_hydro_19_cat.
    IPR023346. Lysozyme-like_dom.
    [Graphical view ]
    Pfami PF00187. Chitin_bind_1. 1 hit.
    PF00182. Glyco_hydro_19. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001060. Endochitinase. 1 hit.
    ProDomi PD000609. Chitin_bd_1. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00270. ChtBD1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    SSF57016. SSF57016. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 96 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, Direct protein sequencing

    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