Chitin deacetylase precursor - Amylomyces rouxii (Filamentous fungus)

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P50325 (CDA_AMYRO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 57. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: Chitin deacetylase EC=3.5.1.41
Organism	Amylomyces rouxii (Filamentous fungus) (Mucor rouxii)
Taxonomic identifier	29923 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Fungi incertae sedis › Early diverging 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 polysaccharide 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

21

Potential

Chain

400

Chitin deacetylase

PRO_0000024832

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P50325 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F51B7F7DA9D3206B
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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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-38.
Strain: ATCC 24905 / CBS 416.77 / DSM 1191.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z19109 mRNA. Translation: CAA79525.1.
PIR	A47713.
3D structure databases
ProteinModelPortal	P50325.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.20.20.370. 1 hit.
InterPro	IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR002509. Polysac_deacetylase. [Graphical view]
Pfam	PF01522. Polysacc_deac_1. 1 hit. [Graphical view]
SUPFAM	SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CDA_AMYRO

Accession

Primary (citable) accession number: P50325

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents