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Reviewed, UniProtKB/Swiss-Prot Q54468 (CHB_SERMA)

Last modified February 9, 2010. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Chitobiase
    EC=3.2.1.52
Alternative name(s):
    N-acetyl-beta-glucosaminidase
    Beta-N-acetylhexosaminidase
Gene names
Name: chb
OrganismSerratia marcescens
Taxonomic identifier615 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia

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Protein attributes

Sequence length885 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Digests the beta-1,4-glycosidic bonds in N-acetylglucosamine (GlcNAc) oligomers (mainly dimers).

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Pathway

Glycan degradation; chitin degradation.

Subunit structure

Monomer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 885858Chitobiase
PRO_0000012018

Sites

Active site5401Proton donor

Amino acid modifications

Disulfide bond56 ↔ 66
Disulfide bond400 ↔ 408
Disulfide bond505 ↔ 578

Secondary structure

1 ............................................................................................................................................. 885
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q54468-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A749CC0F507DE2E1

FASTA88598,548
        10         20         30         40         50         60 
MNAFKLSALA RLTATMGFLG GMGSAMADQQ LVDQLSQLKL NVKMLDNRAG ENGVDCAALG 

        70         80         90        100        110        120 
ADWASCNRVL FTLSNDGQAI DGKDWVIYFH SPRQTLRVDN DQFKIAHLTG DLYKLEPTAK 

       130        140        150        160        170        180 
FSGFPAGKAV EIPVVAEYWQ LFRNDFLPRW YATSGDAKPK MLANTDTENL DQFVAPFTGD 

       190        200        210        220        230        240 
QWKRTKDDKN ILMTPASRFV SNADLQTLPA GALRGKIVPT PMQVKVHAQD ADLRKGVALD 

       250        260        270        280        290        300 
LSTLVKPAAD VVSQRFALLG VPVQTNGYPI KTDIQPGKFK GAMAVSGAYE LKIGKKEAQV 

       310        320        330        340        350        360 
IGFDQAGVFY GLQSILSLVP SDGSGKIATL DASDAPRFPY RGIFLDVARN FHKKDAVLRL 

       370        380        390        400        410        420 
LDQMAAYKLN KFHFHLSDDE GWRIEIPGLP ELTEVGGQRC HDLSETTCLL PQYGQGPDVY 

       430        440        450        460        470        480 
GGFFSRQDYI DIIKYAQARQ IEVIPEIDMP AHARAAVVSM EARYKKLHAA GKEQEANEFR 

       490        500        510        520        530        540 
LVDPTDTSNT TSVQFFNRQS YLNPCLDSSQ RFVDKVIGEI AQMHKEAGQP IKTWHFGGDE 

       550        560        570        580        590        600 
AKNIRLGAGY TDKAKPEPGK GIIDQSNEDK PWAKSQVCQT MIKEGKVADM EHLPSYFGQE 

       610        620        630        640        650        660 
VSKLVKAHGI DRMQAWQDGL KDAESSKAFA TSRVGVNFWD TLYWGGFDSV NDWANKGYEV 

       670        680        690        700        710        720 
VVSNPDYVYM DFPYEVNPDE RGYYWGTRFS DERKVFSFAP DNMPQNAETS VDRDGNHFNA 

       730        740        750        760        770        780 
KSDKPWPGAY GLSAQLWSET QRTDPQMEYM IFPRALSVAE RSWHRAGWEQ DYRAGREYKG 

       790        800        810        820        830        840 
GETHFVDTQA LEKDWLRFAN ILGQRELAKL DKGGVAYRLP VPGARVAAGK LEANIALPGL 

       850        860        870        880 
GIEYSTDGGK QWQRYDAKAK PAVSGEVQVR SVSPDGKRYS RAEKV

« Hide

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References

[1]"N-acetylglucosaminidase (chitobiase) from Serratia marcescens: gene sequence, and protein production and purification in Escherichia coli."
Tews I., Vincentelli R., Vorgias C.E.
Gene 170:63-67(1996) [PubMed: 8621090] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease."
Tews I., Perrakis A., Oppenheim A., Dauter Z., Wilson K.S., Vorgias C.E.
Nat. Struct. Biol. 3:638-648(1996) [PubMed: 8673609] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L43594 Genomic DNA. Translation: AAB03808.1.
PIRJC4732.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7SX-ray1.80A28-885[»]
1C7TX-ray1.90A28-885[»]
1QBAX-ray1.85A28-885[»]
1QBBX-ray2.00A28-885[»]
ModBaseSearch...

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Enzyme and pathway databases

BRENDA3.2.1.52. 457.

Family and domain databases

InterProIPR008965. Carb_bd.
IPR004866. CB_bd_Hex_N.
IPR012291. CBD_carb_bd_dom.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR001540. Glyco_hydro_20.
IPR004867. Glyco_hydro_20_C.
IPR015883. Glyco_hydro_20_cat-core.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
IPR014756. Ig_E-set.
[Graphical view]
Gene3DG3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR22600. Glyco_hydro_20. 1 hit.
PfamPF03173. CHB_HEX. 1 hit.
PF03174. CHB_HEX_C. 1 hit.
PF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PRINTSPR00738. GLHYDRLASE20.
ProtoNetSearch...

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Entry information

Entry nameCHB_SERMA
AccessionPrimary (citable) accession number: Q54468
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents