Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P96155 (HEX1_VIBFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-hexosaminidase

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
Gene names
Name:exo I
OrganismVibrio furnissii
Taxonomic identifier29494 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes rapidly p-nitrophenyl-N-acetyl-beta-D-glucosaminide (PNP-beta-GlcNAc) and 4-methylumbelliferyl-beta-GlcNAc, and slightly active on p-nitrophenyl-beta-GalNAc. Hydrolyzes aryl-N-acetyl-beta-D-glucosaminide (aryl-beta-GlcNAc), aryl-beta-GalNAc and chitin oligosaccharides. This enzyme is not processive, i.e. when it hydrolyzes (GlcNAc)n, both products, (Glc-NAc)n-1 and the terminal GlcNAc, are released before the enzyme attacks a second molecule of (GlcNAc)n or (GlcNAc)n-1.

Catalytic activity

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

Enzyme regulation

Inhibited by mercuric ions, PNP-beta-Glc, PNP-beta-Gal, PNP-alpha-GlcNAc, and PNP-beta-S-GlcNAc.

Pathway

Glycan degradation; chitin degradation.

Subunit structure

Homodimer Potential.

Subcellular location

Periplasm.

Induction

By (GlcNAc)2.

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Biophysicochemical properties

pH dependence:

Optimum pH is between 7.0 with (Glc-NAc)n (n=3-6) as substrate, and 5.8 with (GlcNAc)2 as substrate.

Temperature dependence:

Optimum temperature is 35-40 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentPeriplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

polysaccharide 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Beta-hexosaminidase
PRO_0000215377

Sequences

Sequence LengthMass (Da)Tools
P96155 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: E04C700E88F4D8C3

FASTA61169,502
        10         20         30         40         50         60 
MNYRIDFAVL SEHPQFCRFG LTLHNLSDQD LKAWSLHFTI DRYIQPDSIS HSQIHQVGSF 

        70         80         90        100        110        120 
CSLTPEQDVI NSNSHFYCEF SIKTAPFPFH YYTDGIKAAF VQINDVEPRV RHDVIVTPIA 

       130        140        150        160        170        180 
LASPYRERSE IPATDAATLS LLPKPNHIER LDGEFALTAG SQISLQSSCA ETAATWLKQE 

       190        200        210        220        230        240 
LTHLYQWQPH DIGSADIVLR TNPTLDEGAY LLSVDRKPIR LEASSHIGFV HASATLLQLV 

       250        260        270        280        290        300 
RPDGDNLLVP HIVIKDAPRF KYRGMMLDCA RHFHPLERVK RLINQLAHYK FNTFHWHLTD 

       310        320        330        340        350        360 
DEGWRIEIKS LPQLTDIGAW RGVDEVLEPQ YSLLTEKHGG FYTQEEIREV IAYAAERGIT 

       370        380        390        400        410        420 
VIPEIDIPGH SRAAIKALPE WLFDEDDQSQ YRSIQYYNDN VLSPALPGTY RFLDCVLEEV 

       430        440        450        460        470        480 
AALFPSHFIH IGADEVPDGV WVNSPKCQAL MAEEGYTDAK ELQGHLLRYA EKKLKSLGKR 

       490        500        510        520        530        540 
MVGWEEAQHG DKVSKDTVIY SWLSEQAALN CARQGFDVIL QPGQFTYLDI AQDYAPEEPG 

       550        560        570        580        590        600 
VDWAGVTPLE RAYRYEPLVE VPEHDPLRKR ILGIQCALWC ELVNNQDRMD YMIYPRLTAL 

       610 
AGSGLDTKIP A 

« Hide

References

[1]"The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic beta-N-acetylglucosaminidase."
Keyhani N.O., Roseman S.
J. Biol. Chem. 271:33425-33432(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41417 Genomic DNA. Translation: AAC44672.1.

3D structure databases

ProteinModelPortalP96155.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMERMETA-16856.
UniPathwayUPA00349.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEX1_VIBFU
AccessionPrimary (citable) accession number: P96155
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries