[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Seed; PubMed=1551872 [NCBI, ExPASy, EBI, Israel, Japan] Huynh Q.K., Hironaka C.M., Levine E.B., Smith C.E., Borgmeyer J.R., Shah D.M.; "Antifungal proteins from plants. Purification, molecular cloning, and antifungal properties of chitinases from maize seed."; J. Biol. Chem. 267:6635-6640(1992).
[2]	PROTEIN SEQUENCE OF 169-184. TISSUE=Seed; PubMed=1740436 [NCBI, ExPASy, EBI, Israel, Japan] Verburg J.G., Smith C.E., Lisek C.A., Huynh Q.K.; "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."; J. Biol. Chem. 267:3886-3893(1992).

Comments

FUNCTION: Defense against chitin containing fungal pathogens.
CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
MISCELLANEOUS: Maize chitinase B seems to be less active than chitinase A.
SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily [view classification].
SIMILARITY: Contains 1 chitin-binding type-1 domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M84165; AAA33445.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B42424; B42424.

3D structure databases

HSSP

P02877; 1HEV. [HSSP ENTRY / PDB]

ModBase

P29023.

Organism-specific databases

Gramene

P29023; -.

MaizeGDB

25130; -.

Ontologies

GO:0008061;	Molecular function: chitin binding (inferred from electronic annotation from InterPro).
GO:0004568;	Molecular function: chitinase activity (inferred from electronic annotation from InterPro).
GO:0016998;	Biological process: cell wall catabolic process (inferred from electronic annotation from InterPro).
GO:0006032;	Biological process: chitin catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001002; Chitin_bd_1.
IPR016283; Glyco_hydro_19.
IPR000726; Glyco_hydro_19_cat.
Graphical view of domain structure.

PANTHER

PTHR22595; Glyco_hydro_19_cat; 1.

Pfam

PF00187; Chitin_bind_1; 1.
PF00182; Glyco_hydro_19; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001060; Endochitinase; 1.

PRINTS

PR00451; CHITINBINDNG.

ProDom

PD000609; Chitin_binding_1; 1.
PD354900; Glyco_hydro_19; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00270; ChtBD1; 1.
SMART graphical view of domain structure.

PROSITE

PS00026; CHIT_BIND_I_1; 1.
PS50941; CHIT_BIND_I_2; 1.
PS00773; CHITINASE_19_1; 1.
PS00774; CHITINASE_19_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Carbohydrate metabolism; Chitin degradation; Chitin-binding; Direct protein sequencing; Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`<1 20`	`>20`	`Potential.`
`CHAIN`	`21 269`	`249`	`Endochitinase B.`	`PRO_0000005304`
`DOMAIN`	`21 55`	`35`	`Chitin-binding type-1.`
`REGION`	`58 66`	`9`	`Hinge region (Gly-rich).`
`REGION`	`67 269`	`203`	`Catalytic.`
`DISULFID`	`23 31`		`By similarity.`
`DISULFID`	`25 37`		`By similarity.`
`DISULFID`	`30 44`		`By similarity.`
`DISULFID`	`48 53`		`By similarity.`
`DISULFID`	`89 138`		`By similarity.`
`DISULFID`	`150 159`		`By similarity.`
`DISULFID`	`237 269`		`By similarity.`
`NON_TER`	`1 1`

Sequence information

Length: 269 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 28166 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 3D38B1BADF75DE8F [This is a checksum on the sequence]

        10         20         30         40         50         60 
PQLVALGLAL LCAVAGPAAA QNCGCQPNVC CSKFGYCGTT DEYCGDGCQS GPCRSGRGGG 

        70         80         90        100        110        120 
GSGGGGANVA SVVTSSFFNG IKNQAGSGCE GKNFYTRSAF LSAVKGYPGF AHGGSQVQGK 

       130        140        150        160        170        180 
REIAAFFAHA THETGHFCYI SEINKSNAYC DPTKRQWPCA AGQKYYGRGP LQISWNYNYG 

       190        200        210        220        230        240 
PAGRAIGFDG LGDPGRVARD AVVAFKAALW FWMNSVHGVV PQGFGATTRA MQRALECGGN 

       250        260 
NPAQMNARVG YYRQYCRQLG VDPGPNLTC

P29023 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools