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Q54276

- Q54276_SERMA

UniProt

Q54276 - Q54276_SERMA

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Protein
Submitted name: Chitinase
Gene
chiB
Organism
Serratia marcescens
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121N-acetyl-D-glucosamineImported
Binding sitei56 – 561Sulfate 5
Binding sitei89 – 891Sulfate 6
Binding sitei190 – 1901Sulfate 8; via carbonyl oxygen
Binding sitei191 – 1911N-acetyl-D-glucosamine
Binding sitei194 – 1941Sulfate 8
Binding sitei220 – 2201N-acetyl-D-glucosamine
Binding sitei264 – 2641Sulfate 9; via amide nitrogen
Binding sitei282 – 2821Sulfate 10
Binding sitei294 – 2941N-acetyl-D-glucosamine
Binding sitei316 – 3161N-acetyl-D-glucosamine
Binding sitei343 – 3431Sulfate 16
Binding sitei403 – 4031N-acetyl-D-glucosamineImported
Binding sitei407 – 4071N-acetyl-D-glucosamineImported
Binding sitei410 – 4101Sulfate 16
Binding sitei439 – 4391Sulfate 9; via carbonyl oxygen

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. chitinase activity Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. chitin catabolic process Source: InterPro
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

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499chitinaseImported
PRO_5000147550Add
BLAST

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ54276.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 982N-acetyl-D-glucosamine bindingImported
Regioni142 – 1454N-acetyl-D-glucosamine binding
Regioni214 – 2152N-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

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MSTRKAVIGY YFIPTNQINN YTETDTSVVP FPVSNITPAK AKQLTHINFS    50
FLDINSNLEC AWDPATNDAK ARDVVNRLTA LKAHNPSLRI MFSIGGWYYS 100
NDLGVSHANY VNAVKTPASR AKFAQSCVRI MKDYGFDGVD IDWEYPQAAE 150
VDGFIAALQE IRTLLNQQTI TDGRQALPYQ LTIAGAGGAF FLSRYYSKLA 200
QIVAPLDYIN LMTYDLAGPW EKVTNHQAAL FGDAAGPTFY NALREANLGW 250
SWEELTRAFP SPFSLTVDAA VQQHLMMEGV PSAKIVMGVP FYGRAFKGVS 300
GGNGGQYSSH STPGEDPYPS TDYWLVGCEE CVRDKDPRIA SYRQLEQMLQ 350
GNYGYQRLWN DKTKTPYLYH AQNGLFVTYD DAESFKYKAK YIKQQQLGGV 400
MFWHLGQDNR NGDLLAALDR YFNAADYDDS QLDMGTGLRY TGVGPGNLPI 450
MTAPAYVPGT TYAQGALVSY QGYVWQTKWG YITSAPGSDS AWLKVGRVA 499
Length:499
Mass (Da):55,469
Last modified:November 1, 1996 - v1
Checksum:i58C933A9064D526B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z36295 Genomic DNA. Translation: CAA85292.1.
PIRiS52422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z36295 Genomic DNA. Translation: CAA85292.1 .
PIRi S52422.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E15 X-ray 1.90 A/B 1-499 [» ]
1E6P X-ray 1.70 A/B 1-499 [» ]
1E6R X-ray 2.50 A/B 1-499 [» ]
1E6Z X-ray 1.99 A/B 2-499 [» ]
1GPF X-ray 1.85 A/B 1-499 [» ]
1UR8 X-ray 1.90 A/B 1-499 [» ]
1UR9 X-ray 1.80 A/B 1-498 [» ]
1W1P X-ray 2.10 A/B 1-499 [» ]
1W1T X-ray 1.90 A/B 1-499 [» ]
1W1V X-ray 1.85 A/B 1-499 [» ]
1W1Y X-ray 1.85 A/B 1-499 [» ]
ProteinModelPortali Q54276.
SMRi Q54276. Positions 2-499.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM5. Carbohydrate-Binding Module Family 5.
GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q54276.

Family and domain databases

Gene3Di 2.10.10.20. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR003610. 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 ]
Pfami PF02839. CBM_5_12. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view ]
SMARTi SM00495. ChtBD3. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view ]
SUPFAMi SSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
PROSITEi PS01095. CHITINASE_18. 1 hit.
[Graphical view ]
ProtoNeti Search...

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).
  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.
  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).
  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.
  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).

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: September 3, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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