Reviewed, UniProtKB/Swiss-Prot P29023 (CHIB_MAIZE)

Names and origin

Protein names	Recommended name:     Endochitinase B     EC=3.2.1.14 Alternative name(s):     Seed chitinase B
Organism	Zea mays (Maize)
Taxonomic identifier	4577 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	269 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Sequence similarities	Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily. Contains 1 chitin-binding type-1 domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Plant defense Polysaccharide degradation
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW defense response Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	‹1 – 20	›20	Potential
	Chain	21 – 269	249	Endochitinase B		PRO_0000005304
Regions
	Domain	21 – 55	35	Chitin-binding type-1
	Region	58 – 66	9	Hinge region (Gly-rich)
	Region	67 – 269	203	Catalytic
Amino acid modifications
	Disulfide bond	23 ↔ 31		By similarity
	Disulfide bond	25 ↔ 37		By similarity
	Disulfide bond	30 ↔ 44		By similarity
	Disulfide bond	48 ↔ 53		By similarity
	Disulfide bond	89 ↔ 138		By similarity
	Disulfide bond	150 ↔ 159		By similarity
	Disulfide bond	237 ↔ 269		By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P29023-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 3D38B1BADF75DE8F	FASTA	269	28,166
	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

References

[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: 1551872] [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: 1740436] [Abstract] Cited for: PROTEIN SEQUENCE OF 169-184. Tissue: Seed.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M84165 Genomic DNA. Translation: AAA33445.1.
PIR	B42424.
3D structure databases
HSSP	HSSP built from PDB template 1HEV based on UniProtKB P02877.
ModBase	Search...
Protein family/group databases
CAZy	CBM18. Carbohydrate-Binding Module Family 18. GH19. Glycoside Hydrolase Family 19.
Organism-specific databases
Gramene	P29023.
MaizeGDB	25130.
Enzyme and pathway databases
BRENDA	3.2.1.14. 289.
Family and domain databases
InterPro	IPR018371. Chitin-binding_1_CS. IPR001002. Chitin_bd_1. IPR016283. Glyco_hydro_19. IPR000726. Glyco_hydro_19_cat. [Graphical view]
PANTHER	PTHR22595. Glyco_hydro_19_cat. 1 hit.
Pfam	PF00187. Chitin_bind_1. 1 hit. PF00182. Glyco_hydro_19. 1 hit. [Graphical view]
PIRSF	PIRSF001060. Endochitinase. 1 hit.
PRINTS	PR00451. CHITINBINDNG.
ProDom	PD000609. Chitin_binding_1. 1 hit. PD354900. Glyco_hydro_19. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00270. ChtBD1. 1 hit. [Graphical view]
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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHIB_MAIZE

Accession

Primary (citable) accession number: P29023

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)