Reviewed, UniProtKB/Swiss-Prot P46876 (CHI1_CANAL)

Names and origin

Protein names

Recommended name:
    Chitinase 1
    EC=3.2.1.14

Gene names

Name:

CHT1

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Subcellular location	Secreted Probable.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro 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 – 17	17	Potential
	Chain	18 – 462	445	Chitinase 1		PRO_0000011924
Regions
	Compositional bias	237 – 240	4	Poly-Ser
	Compositional bias	305 – 422	118	Thr-rich
Sites
	Active site	147	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	57	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P46876-1 [UniParc]. Last modified May 27, 2002. Version 2. Checksum: 978515D7ABECABCD	FASTA	462	48,916
	10 20 30 40 50 60 MILNLIILLA ISIVASASNI AAYWGQNAGG DQQTLGDYCS SSPASIIILS FLDGFPNLSL 70 80 90 100 110 120 NFANQCSGTF SSGLAHCSQI GSDIKSCQQQ GKTILLSLGG ATGNYGFSSD SEAVQFAGTL 130 140 150 160 170 180 WNKFGGGKDS ERPFDDAIVD GFDFDIENKD QTGYAALATQ LRKYFSTGTK SYYLSAAPQC 190 200 210 220 230 240 PYPDESVGDL MSQVDLDFAF IQFYNNYCSL NQQFNWNSWS NYARGKSIKL YLGLPGSSSS 250 260 270 280 290 300 AGSGFVGLST VQRVVASIKG DSSFGGISIW DISSAENGGY LNQLYQALSG SGSPAAPSNS 310 320 330 340 350 360 YQPNTPLTRT YGGSTATASA YISVGFTAGA THGSTTTNDL LAWIDSLFGS SQSSVQQYAT 370 380 390 400 410 420 PVQSVTATPQ PVAATTTSAP KPTASAFNWF GWFDGTTTST TLQTVYSTVP ADQTVYVTLT 430 440 450 460 TTVGSQMLQS LFDKRDVIAE AKSTNLQICW LLFIPLLALI CS

References

[1]	"Molecular cloning of a third chitinase gene (CHT1) from Candida albicans." McCreath K.J., Specht C.A., Liu Y., Robbins P.W. Yeast 12:501-504(1996) [PubMed: 8740424] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10261 / CBS 2718 / IFO 1061.
[2]	Specht C.A. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U36490 Genomic DNA. Translation: AAC49409.2.
3D structure databases
HSSP	HSSP built from PDB template 2HVM based on UniProtKB P23472.
ModBase	Search...
Protein family/group databases
CAZy	GH18. Glycoside Hydrolase Family 18.
Enzyme and pathway databases
BRENDA	3.2.1.14. 1124.
Family and domain databases
InterPro	IPR001223. Glyco_hydro18cat. IPR001579. Glyco_hydro_18_chit_AS. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00704. Glyco_hydro_18. 1 hit. [Graphical view]
PROSITE	PS01095. CHITINASE_18. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHI1_CANAL

Accession

Primary (citable) accession number: P46876

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	May 27, 2002
Last modified:	September 22, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)