Reviewed, UniProtKB/Swiss-Prot P80052 (CHIT_DIOJA)

Names and origin

Protein names	Recommended name:     Acidic endochitinase     EC=3.2.1.14
Organism	Dioscorea japonica (Yam)
Taxonomic identifier	4673 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Dioscoreales › Dioscoreaceae › Dioscorea

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
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
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
	Chain	1 – 250	250	Acidic endochitinase		PRO_0000124826
Regions
	Domain	1 – 36	36	Chitin-binding type-1
Amino acid modifications
	Modified residue	1	1	Pyrrolidone carboxylic acid
	Disulfide bond	3 ↔ 12		By similarity
	Disulfide bond	5 ↔ 18		By similarity
	Disulfide bond	11 ↔ 25		By similarity
	Disulfide bond	29 ↔ 34		By similarity
	Disulfide bond	66 ↔ 115		Ref.3
	Disulfide bond	128 ↔ 136		Ref.3
	Disulfide bond	218 ↔ 250		Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P80052-1 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 958E0816553C4985	FASTA	250	27,908
	10 20 30 40 50 60 QNCQCDTTIY CCSQHGYCGN SYDYCGPGCQ AGPCWDPCEG DGTLTVSDIV TQEFWDGIAS 70 80 90 100 110 120 QAAANCPGKS FYTRSNFLEA VSAYPGFGTK CTDEDRKREI AAYFAHVTHE TGHLCYIEER 130 140 150 160 170 180 DGHANNYCQE SQQYPCNPNK EYFGRGPMQL SWNYNYIDAG KELHFDGLND PDIVGRDPII 190 200 210 220 230 240 SFKTSLWFWI RKGVQYVILD PNQGFGATIR IINGGQECDG HNTAQMMARV GYYQEYCAQL 250 GVSPGNNLPC

References

[1]	"The complete amino acid sequence of yam (Dioscorea japonica) chitinase. A newly identified acidic class I chitinase." Araki T., Funatsu J., Kuramoto M., Konno H., Torikata T. J. Biol. Chem. 267:19944-19947(1992) [PubMed: 1400311] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Aerial tuber.
[2]	"Amino acid sequence of the N-terminal domain of yam (Dioscorea japonica) aerial tuber acidic chitinase. Evidence for the presence of a wheat germ agglutinin domain in matured acidic chitinase from unstressed tuber." Araki T., Funatsu J., Kuramoto M., Torikata T. Plant Mol. Biol. 19:351-354(1992) [PubMed: 1623187] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-53. Tissue: Aerial tuber.
[3]	"Positions of disulfide bonds in yam (Dioscorea japonica) acidic class IL (class IV) chitinase." Araki T., Kuramoto M., Torikata T. Arch. Biochem. Biophys. 335:118-122(1996) [PubMed: 8914841] [Abstract] Cited for: DISULFIDE BONDS IN CATALYTIC DOMAIN.

Cross-references

Sequence databases
PIR	A44039.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	CBM18. Carbohydrate-Binding Module Family 18. GH19. Glycoside Hydrolase Family 19.
Enzyme and pathway databases
BRENDA	3.2.1.14. 306115.
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]
Gene3D	G3DSA:3.30.60.10. Chitin_bd_1. 1 hit.
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.
ProDom	PD000609. Chitin_bd_1. 1 hit. [Graphical view] [Entries sharing at least one domain]
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

CHIT_DIOJA

Accession

Primary (citable) accession number: P80052

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	February 1, 1994
Last modified:	November 24, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)