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O83008 (O83008_SERMA) Unreviewed, UniProtKB/TrEMBL

Last modified May 31, 2011. Version 57. Feed History...

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

Names and origin

Protein names
Gene names
Name:chiA EMBL BAA31567.1
OrganismSerratia marcescens EMBL BAA31567.1
Taxonomic identifier615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. RuleBase RU004453

Ontologies

Keywords
   DomainSignal EMBL BAA31567.1
   Molecular functionGlycosidase RuleBase RU000489
Hydrolase
   Technical term3D-structure PDB 1EDQ
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

chitinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential EMBL BAA31567.1
Chain24 – 563540chitinase A EMBL BAA31567.1
PRO_5000049238

Sequences

Sequence LengthMass (Da)Tools
O83008 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: CF0B130905AF6E8B

FASTA56361,111
        10         20         30         40         50         60 
MRKFNKPLLA LLIGSTLCSA AQAAAPGKPT IAWGNTKFAI VEVDQAATAY NNLVKVKNAA 

        70         80         90        100        110        120 
DVSVSWNLWN GDTGTTAKVL LNGKEAWSGP STGSSGTANF KVNKGGRYQM QVALCNADGC 

       130        140        150        160        170        180 
TASDATEIVV ADTDGSHLAP LKEPLLEKNK PYKQNSGKVV GSYFVEWGVY GRNFTVDKIP 

       190        200        210        220        230        240 
AQNLTHLLYG FIPICGGNGI NDSLKEIEGS FQALQRSCQG REDFKVSIHD PFAALQKAQK 

       250        260        270        280        290        300 
GVTAWDDPYK GNFGQLMALK QAHPDLKILP SIGGWTLSDP FFFMGDKVKR DRFVGSVKEF 

       310        320        330        340        350        360 
LQTWKFFDGV DIDWEFPGGK GANPNLGSPQ DGETYVLLMK ELRAMLDQLS VETGRKYELT 

       370        380        390        400        410        420 
SAISAGKDKI DKVAYNVAQN SMDHIFLMSY DFYGAFDLKN LGHQTALNAP AWKPDTAYTT 

       430        440        450        460        470        480 
VNGVNALLAQ GVKPGKIVVG TAMYGRGWTG VNGYQNNIPF TGTATGPVKG TWENRIVDYR 

       490        500        510        520        530        540 
QIAGQFMSGE WQYTYDATAE APYVFKPSTG DLITFDDARS VQAKGKYVLD KQLGGLFSWE 

       550        560 
IDADNGDILN SMNASLGNSA GVQ 

« Hide

References

[1]"Genetic analysis of the chitinase system of Serratia marcescens 2170."
Watanabe T., Kimura K., Sumiya T., Nikaidou N., Suzuki K., Suzuki M., Taiyoji M., Ferrer S., Regue M.
J. Bacteriol. 179:7111-7117(1997) [PubMed: 9371460] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 2170 EMBL BAA31567.1.
[2]Suzuki K., Nikaidou N., Watanabe T.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 2170 EMBL BAA31567.1.
[3]"De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin."
Papanikolau Y., Tavlas G., Vorgias C.E., Petratos K.
Acta Crystallogr. D Biol. Crystallogr. 59:400-403(2003) [PubMed: 12554965] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 24-563.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015996 Genomic DNA. Translation: BAA31567.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EDQX-ray1.55A24-563[»]
ProteinModelPortalO83008.
SMRO83008. Positions 24-563.
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011583. Chitinase_II.
IPR013540. ChitinaseA_N.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR022409. PKD/Chitinase_dom.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF08329. ChitinaseA_N. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTSM00636. Glyco_18. 1 hit.
SM00089. PKD. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameO83008_SERMA
AccessionPrimary (citable) accession number: O83008
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: May 31, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)