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Protein
Submitted name:

Chitinase C1

Gene

chiC1

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
Metal bindingi15 – 151Calcium; via carbonyl oxygenCombined sources
Metal bindingi17 – 171Calcium; via carbonyl oxygenCombined sources
Metal bindingi93 – 931CalciumCombined sources
Metal bindingi132 – 1321Calcium; via carbonyl oxygenCombined sources
Metal bindingi134 – 1341CalciumCombined sources

GO - Molecular functioni

  • carbohydrate binding Source: InterPro
  • chitinase activity Source: CACAO
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BRENDAi3.2.1.14. 5690.

Protein family/group databases

CAZyiCBM12. Carbohydrate-Binding Module Family 12.
GH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Submitted name:
Chitinase C1Imported (EC:3.2.1.14Imported)
Gene namesi
Name:chiC1Imported
OrganismiSerratia marcescensImported
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AXNX-ray1.68A/B1-328[»]
ProteinModelPortaliQ700B8.
SMRiQ700B8. Positions 435-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.UniRule annotation
Contains 1 fibronectin type-III domain.UniRule annotation

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR003610. CBM_fam5/12.
IPR003961. FN3_dom.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF02839. CBM_5_12. 1 hit.
PF00041. fn3. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
SM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
PS50853. FN3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q700B8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNNTINAV AADDAAIMPS IANKKILMGF WHNWAAGASD GYQQGQFANM
60 70 80 90 100
NLTDIPTEYN VVAVAFMKGQ GIPTFKPYNL SDTEFRRQVG VLNSQGRAVL
110 120 130 140 150
ISLGGADAHI ELKTGDEDKL KDEIIRLVEV YGFDGLDIDL EQAAIGAANN
160 170 180 190 200
KTVLPAALKK VKDHYAAQGK NFIISMAPEF PYLRTNGTYL DYINALEGYY
210 220 230 240 250
DFIAPQYYNQ GGDGIWVDEL NAWITQNNDA MKEDFLYYLT ESLVTGTRGY
260 270 280 290 300
AKIPAAKFVI GLPSNNDAAA TGYVVNKQAV YNAFSRLDAK NLSIKGLMTW
310 320 330 340 350
SINWDNGKSK AGVAYNWEFK TRYAPLIQGG VTPPPGKPNA PTALTVAELG
360 370 380 390 400
ATSLKLSWAA ATGAFPIASY TVYRNGNPIG QTAGLSLADG GLTPATQYSY
410 420 430 440 450
FVTATDSQGN TSLPSSALAV KTANDGTPPD PGAPEWQNNH SYKAGDVVSY
460 470 480
KGKKYTCIQA HTSNAGWTPD AAFTLWQLIA
Length:480
Mass (Da):51,766
Last modified:July 5, 2004 - v1
Checksum:iDC7749619E52A6CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ630582 Genomic DNA. Translation: CAF74787.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ630582 Genomic DNA. Translation: CAF74787.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AXNX-ray1.68A/B1-328[»]
ProteinModelPortaliQ700B8.
SMRiQ700B8. Positions 435-478.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ700B8.
ChEMBLiCHEMBL5181.

Protein family/group databases

CAZyiCBM12. Carbohydrate-Binding Module Family 12.
GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.14. 5690.

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR003610. CBM_fam5/12.
IPR003961. FN3_dom.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF02839. CBM_5_12. 1 hit.
PF00041. fn3. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
SM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
PS50853. FN3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation."
    Vaaje-Kolstad G., Horn S.J., van Aalten D.M., Synstad B., Eijsink V.G.
    J. Biol. Chem. 280:28492-28497(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BJL 200Imported.
  2. "Hallmarks of processivity in glycoside hydrolases from crystallographic and computational studies of the Serratia marcescens chitinases."
    Payne C.M., Baban J., Horn S.J., Backe P.H., Arvai A.S., Dalhus B., Bjoras M., Eijsink V.G., Sorlie M., Beckham G.T., Vaaje-Kolstad G.
    J. Biol. Chem. 287:36322-36330(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1-328 IN COMPLEX WITH CALCIUM.

Entry informationi

Entry nameiQ700B8_SERMA
AccessioniPrimary (citable) accession number: Q700B8
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 66 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.