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P20533 (CHIA1_BACCI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chitinase A1

EC=3.2.1.14
Gene names
Name:chiA1
OrganismBacillus circulans
Taxonomic identifier1397 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 18 family. Chitinase class II subfamily.

Contains 2 fibronectin type-III domains.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141
Chain42 – 699658Chitinase A1
PRO_0000011905

Regions

Domain467 – 55387Fibronectin type-III 1
Domain562 – 64786Fibronectin type-III 2
Region42 – 460419Catalytic

Sites

Active site2041Proton donor Probable

Experimental info

Mutagenesis2001D → E: No change in activity.
Mutagenesis2001D → N: Decrease in activity.
Mutagenesis2041E → D or Q: Loss of activity.

Secondary structure

..................................................................................................... 699
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20533 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: AC7C9B22E2987643

FASTA69973,678
        10         20         30         40         50         60 
MINLNKHTAF KKTAKFFLGL SLLLSVIVPS FALQPATAEA ADSYKIVGYY PSWAAYGRNY 

        70         80         90        100        110        120 
NVADIDPTKV THINYAFADI CWNGIHGNPD PSGPNPVTWT CQNEKSQTIN VPNGTIVLGD 

       130        140        150        160        170        180 
PWIDTGKTFA GDTWDQPIAG NINQLNKLKQ TNPNLKTIIS VGGWTWSNRF SDVAATAATR 

       190        200        210        220        230        240 
EVFANSAVDF LRKYNFDGVD LDWEYPVSGG LDGNSKRPED KQNYTLLLSK IREKLDAAGA 

       250        260        270        280        290        300 
VDGKKYLLTI ASGASATYAA NTELAKIAAI VDWINIMTYD FNGAWQKISA HNAPLNYDPA 

       310        320        330        340        350        360 
ASAAGVPDAN TFNVAAGAQG HLDAGVPAAK LVLGVPFYGR GWDGCAQAGN GQYQTCTGGS 

       370        380        390        400        410        420 
SVGTWEAGSF DFYDLEANYI NKNGYTRYWN DTAKVPYLYN ASNKRFISYD DAESVGYKTA 

       430        440        450        460        470        480 
YIKSKGLGGA MFWELSGDRN KTLQNKLKAD LPTGGTVPPV DTTAPSVPGN ARSTGVTANS 

       490        500        510        520        530        540 
VTLAWNASTD NVGVTGYNVY NGANLATSVT GTTATISGLT AGTSYTFTIK AKDAAGNLSA 

       550        560        570        580        590        600 
ASNAVTVSTT AQPGGDTQAP TAPTNLASTA QTTSSITLSW TASTDNVGVT GYDVYNGTAL 

       610        620        630        640        650        660 
ATTVTGTTAT ISGLAADTSY TFTVKAKDAA GNVSAASNAV SVKTAAETTN PGVSAWQVNT 

       670        680        690 
AYTAGQLVTY NGKTYKCLQP HTSLAGWEPS NVPALWQLQ 

« Hide

References

[1]"Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin."
Watanabe T., Suzuki K., Oyanagi W., Ohnishi K., Tanaka H.
J. Biol. Chem. 265:15659-15665(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: WL-12.
[2]"Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity."
Watanabe T., Kohori K., Miyashita K., Fujii T., Sakai H., Uchida M., Tanaka H.
J. Biol. Chem. 268:18567-18572(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
Strain: WL-12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57601 Genomic DNA. Translation: AAA81528.1.
PIRA38368.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ED7NMR-A655-699[»]
1ITXX-ray1.10A33-451[»]
1K85NMR-A559-644[»]
ProteinModelPortalP20533.
SMRP20533. Positions 33-451, 464-549, 559-644, 655-698.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM12. Carbohydrate-Binding Module Family 12.
GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.10.20. 1 hit.
2.60.40.10. 2 hits.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProIPR003610. CBM_fam5/12.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR003961. Fibronectin_type3.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF02839. CBM_5_12. 1 hit.
PF00041. fn3. 2 hits.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTSM00495. ChtBD3. 1 hit.
SM00060. FN3. 2 hits.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
PROSITEPS01095. CHITINASE_18. 1 hit.
PS50853. FN3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20533.

Entry information

Entry nameCHIA1_BACCI
AccessionPrimary (citable) accession number: P20533
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries