Reviewed, UniProtKB/Swiss-Prot P50325 (CDA_MUCRO)

Names and origin

Protein names	Recommended name:     Chitin deacetylase     EC=3.5.1.41
Organism	Mucor rouxii
Taxonomic identifier	29923 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Fungi incertae sedis › Basal fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Amylomyces

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin. This enzyme specifically acts on beta-1-4-linked N-acetylglucosamine homopolymers and requires at least 4 residues for catalysis.
Catalytic activity	Chitin + H2O = chitosan + acetate.
Sequence similarities	Belongs to the polysaccharide deacetylase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chitin deacetylase 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 – 21	21	Potential
	Chain	22 – 421	400	Chitin deacetylase		PRO_0000024832
Amino acid modifications
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Glycosylation	70	1	N-linked (GlcNAc...) Potential
	Glycosylation	87	1	N-linked (GlcNAc...) Potential
	Glycosylation	106	1	N-linked (GlcNAc...) Potential
	Glycosylation	168	1	N-linked (GlcNAc...) Potential
	Glycosylation	307	1	N-linked (GlcNAc...) Potential
	Glycosylation	323	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	367	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P50325-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: F51B7F7DA9D3206B	FASTA	421	45,972
	10 20 30 40 50 60 MQIKTFALSA AIAQVATLAL ADTSANYWQS FTSQINPKNI SIPSIEQTSS IDPTQECAYY 70 80 90 100 110 120 TPDASLFTFN ASEWPSIWEV ATTNGMNESA EFLSVYNSID WTKAPNISVR TLDANGNLDT 130 140 150 160 170 180 TGYNTATDPD CWWTATTCTS PKISDINDDI SKCPEPETWG LTYDDGPNCS HNAFYDYLQE 190 200 210 220 230 240 QKLKASMFYI GSNVVDWPYG AMRGVVDGHH IASHTWSHPQ MTTKTNQEVL AEFYYTQKAI 250 260 270 280 290 300 KLATGLTPRY WRPPYGDIDD RVRWIASQLG LTAVIWNLDT DDWSAGVTTT VEAVEQSYSD 310 320 330 340 350 360 YIAMGTNGTF ANSGNIVLTH EINTTMSLAV ENLPKIISAY KQVIDVATCY NISHPYFEDY 370 380 390 400 410 420 EWTNVLNGTK SSATASGSAT SASASGGATT AAAHIQASTS GAMSVLPNLA LISAFIATLL F

References

[1]

"The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products." Kafetzopoulos D., Thireos G., Vournakis J.N., Bouriotis V. Proc. Natl. Acad. Sci. U.S.A. 90:8005-8008(1993) [PubMed: 8367456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-38. Strain: ATCC 24905 / CBS 416.77 / DSM 1191.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z19109 mRNA. Translation: CAA79525.1.
PIR	A47713.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.1.41. 21529.
Family and domain databases
InterPro	IPR002509. Polysac_deacetylase. [Graphical view]
Gene3D	G3DSA:3.20.20.370. Polysac_deacetylase. 1 hit.
Pfam	PF01522. Polysacc_deac_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDA_MUCRO

Accession

Primary (citable) accession number: P50325

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	September 22, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)