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Protein
Submitted name:

Chitinase

Gene

chiB

Organism
Serratia marcescens
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121N-acetyl-D-glucosamine
Binding sitei191 – 1911N-acetyl-D-glucosamineCombined sources
Binding sitei220 – 2201N-acetyl-D-glucosamineCombined sources
Binding sitei316 – 3161N-acetyl-D-glucosamineCombined sources
Binding sitei403 – 4031N-acetyl-D-glucosamine
Binding sitei407 – 4071N-acetyl-D-glucosamine

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Protein family/group databases

CAZyiCBM5. Carbohydrate-Binding Module Family 5.
GH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Submitted name:
ChitinaseImported
Gene namesi
Name:chiBImported
OrganismiSerratia marcescensImported
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499chitinaseImportedPRO_5000147550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi328 ↔ 331Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E15X-ray1.90A/B1-499[»]
1E6PX-ray1.70A/B1-499[»]
1E6RX-ray2.50A/B1-499[»]
1E6ZX-ray1.99A/B2-499[»]
1GPFX-ray1.85A/B1-499[»]
1UR8X-ray1.90A/B1-499[»]
1UR9X-ray1.80A/B1-498[»]
1W1PX-ray2.10A/B1-499[»]
1W1TX-ray1.90A/B1-499[»]
1W1VX-ray1.85A/B1-499[»]
1W1YX-ray1.85A/B1-499[»]
ProteinModelPortaliQ54276.
SMRiQ54276. Positions 2-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ54276.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 982N-acetyl-D-glucosamine binding

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.UniRule annotation

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR003610. CBM_fam5/12.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02839. CBM_5_12. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q54276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTRKAVIGY YFIPTNQINN YTETDTSVVP FPVSNITPAK AKQLTHINFS
60 70 80 90 100
FLDINSNLEC AWDPATNDAK ARDVVNRLTA LKAHNPSLRI MFSIGGWYYS
110 120 130 140 150
NDLGVSHANY VNAVKTPASR AKFAQSCVRI MKDYGFDGVD IDWEYPQAAE
160 170 180 190 200
VDGFIAALQE IRTLLNQQTI TDGRQALPYQ LTIAGAGGAF FLSRYYSKLA
210 220 230 240 250
QIVAPLDYIN LMTYDLAGPW EKVTNHQAAL FGDAAGPTFY NALREANLGW
260 270 280 290 300
SWEELTRAFP SPFSLTVDAA VQQHLMMEGV PSAKIVMGVP FYGRAFKGVS
310 320 330 340 350
GGNGGQYSSH STPGEDPYPS TDYWLVGCEE CVRDKDPRIA SYRQLEQMLQ
360 370 380 390 400
GNYGYQRLWN DKTKTPYLYH AQNGLFVTYD DAESFKYKAK YIKQQQLGGV
410 420 430 440 450
MFWHLGQDNR NGDLLAALDR YFNAADYDDS QLDMGTGLRY TGVGPGNLPI
460 470 480 490
MTAPAYVPGT TYAQGALVSY QGYVWQTKWG YITSAPGSDS AWLKVGRVA
Length:499
Mass (Da):55,469
Last modified:November 1, 1996 - v1
Checksum:i58C933A9064D526B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36295 Genomic DNA. Translation: CAA85292.1.
PIRiS52422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36295 Genomic DNA. Translation: CAA85292.1.
PIRiS52422.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E15X-ray1.90A/B1-499[»]
1E6PX-ray1.70A/B1-499[»]
1E6RX-ray2.50A/B1-499[»]
1E6ZX-ray1.99A/B2-499[»]
1GPFX-ray1.85A/B1-499[»]
1UR8X-ray1.90A/B1-499[»]
1UR9X-ray1.80A/B1-498[»]
1W1PX-ray2.10A/B1-499[»]
1W1TX-ray1.90A/B1-499[»]
1W1VX-ray1.85A/B1-499[»]
1W1YX-ray1.85A/B1-499[»]
ProteinModelPortaliQ54276.
SMRiQ54276. Positions 2-499.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM5. Carbohydrate-Binding Module Family 5.
GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ54276.

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR003610. CBM_fam5/12.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02839. CBM_5_12. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Brurberg M.
    Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing."
    Brurberg M.B., Eijsink V.G., Haandrikman A.J., Venema G., Nes I.F.
    Microbiology 141:123-131(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution."
    van Aalten D.M., Synstad B., Brurberg M.B., Hough E., Riise B.W., Eijsink V.G., Wierenga R.K.
    Proc. Natl. Acad. Sci. U.S.A. 97:5842-5847(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), DISULFIDE BONDS.
  4. "Structural insights into the catalytic mechanism of a family 18 exo-chitinase."
    van Aalten D.M., Komander D., Synstad B., Gaseidnes S., Peter M.G., Eijsink V.G.
    Proc. Natl. Acad. Sci. U.S.A. 98:8979-8984(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE, DISULFIDE BONDS.
  5. "Psammaplin A, a chitinase inhibitor isolated from the Fijian marine sponge Aplysinella rhax."
    Tabudravu J.N., Eijsink V.G., Gooday G.W., Jaspars M., Komander D., Legg M., Synstad B., van Aalten D.M.
    Bioorg. Med. Chem. 10:1123-1128(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), DISULFIDE BONDS.
  6. "Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone."
    Vaaje-Kolstad G., Vasella A., Peter M.G., Netter C., Houston D.R., Westereng B., Synstad B., Eijsink V.G., van Aalten D.M.
    J. Biol. Chem. 279:3612-3619(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-498 IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE, DISULFIDE BONDS.
  7. "Structure-based exploration of cyclic dipeptide chitinase inhibitors."
    Houston D.R., Synstad B., Eijsink V.G., Stark M.J., Eggleston I.M., van Aalten D.M.
    J. Med. Chem. 47:5713-5720(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), DISULFIDE BONDS.

Entry informationi

Entry nameiQ54276_SERMA
AccessioniPrimary (citable) accession number: Q54276
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.