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Protein

Endochitinase

Gene
N/A
Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed-Annotation score: Annotation score: 4 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

  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
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 (EC:3.2.1.14)
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Subcellular locationi

Vacuole By similarity
Note: Vacuolar and protoplast.By similarity

GO - Cellular componenti

  1. vacuole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 317290EndochitinasePRO_0000005311Add
BLAST
Propeptidei318 – 32811Removed in mature formCuratedPRO_0000005312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 45PROSITE-ProRule annotation
Disulfide bondi39 ↔ 51PROSITE-ProRule annotation
Disulfide bondi44 ↔ 58PROSITE-ProRule annotation
Disulfide bondi62 ↔ 66PROSITE-ProRule annotation
Disulfide bondi97 ↔ 159PROSITE-ProRule annotation
Disulfide bondi170 ↔ 178PROSITE-ProRule annotation
Disulfide bondi277 ↔ 309PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

ProMEXiP06215.

Expressioni

Inductioni

By ethylene.

Structurei

3D structure databases

ProteinModelPortaliP06215.
SMRiP06215. Positions 28-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6841Chitin-binding type-1PROSITE-ProRule annotationAdd
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.
PRINTSiPR00451. CHITINBINDNG.
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.

P06215-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKNRMMMMI WSVGVVWMLL LVGGSYGEQC GRQAGGALCP GGNCCSQFGW
60 70 80 90 100
CGSTTDYCGP GCQSQCGGPS PAPTDLSALI SRSTFDQMLK HRNDGACPAK
110 120 130 140 150
GFYTYDAFIA AAKAYPSFGN TGDTATRKRE IAAFLGQTSH ETTGGWATAP
160 170 180 190 200
DGPYAWGYCF VRERNPSTYC SATPQFPCAP GQQYYGRGPI QISWNYNYGQ
210 220 230 240 250
CGRAIGVDLL NKPDLVATDS VISFKSALWF WMTAQSPKPS SHDVITSRWT
260 270 280 290 300
PSSADVAARR LPGYGTVTNI INGGLECGRG QDSRVQDRIG FFKRYCDLLG
310 320
VGYGNNLDCY SQTPFGNSLL LSDLVTSQ
Length:328
Mass (Da):35,444
Last modified:December 31, 1987 - v1
Checksum:i0B5A73626C776C8A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401P → L in AAA33757 (PubMed:16665863).Curated
Sequence conflicti54 – 541T → S AA sequence (Ref. 2) Curated
Sequence conflicti56 – 561D → E AA sequence (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881M → V.
Natural varianti168 – 1681T → A.
Natural varianti210 – 2101L → F.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13968 mRNA. Translation: AAA33756.1.
M19052 mRNA. Translation: AAA33757.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13968 mRNA. Translation: AAA33756.1.
M19052 mRNA. Translation: AAA33757.1.

3D structure databases

ProteinModelPortaliP06215.
SMRiP06215. Positions 28-316.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Proteomic databases

ProMEXiP06215.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
PRINTSiPR00451. CHITINBINDNG.
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. "Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris."
    Broglie K.E., Gaynor J.J., Broglie R.M.
    Proc. Natl. Acad. Sci. U.S.A. 83:6820-6824(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Saxa.
  2. "Amino-terminal sequence of ethylene-induced bean leaf chitinase reveals similarities to sugar-binding domains of wheat germ agglutinin."
    Lucas J., Henschen A., Lottspeich F., Voegeli U., Boller T.
    FEBS Lett. 193:208-210(1984)
    Cited for: PROTEIN SEQUENCE OF 28-57.
  3. "Chitinase cDNA cloning and mRNA induction by fungal elicitor, wounding, and infection."
    Hedrick S.A., Bell J.N., Boller T., Lamb C.J.
    Plant Physiol. 86:182-186(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-51.

Entry informationi

Entry nameiCHIT_PHAVU
AccessioniPrimary (citable) accession number: P06215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 31, 1987
Last sequence update: December 31, 1987
Last modified: January 6, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.