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P96155

- HEX1_VIBFU

UniProt

P96155 - HEX1_VIBFU

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Protein
Beta-hexosaminidase
Gene
exo I
Organism
Vibrio furnissii
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Enzyme regulationi

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

pH dependencei

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

Temperature dependencei

Optimum temperature is 35-40 degrees Celsius.

Pathwayi

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. chitin catabolic process Source: UniProtKB-UniPathway
  2. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMERMETA-16856.
UniPathwayiUPA00349.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-hexosaminidase (EC:3.2.1.52)
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
Gene namesi
Name:exo I
OrganismiVibrio furnissii
Taxonomic identifieri29494 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 611611Beta-hexosaminidase
PRO_0000215377Add
BLAST

Expressioni

Inductioni

By (GlcNAc)2.

Interactioni

Subunit structurei

Homodimer Reviewed prediction.

Structurei

3D structure databases

ProteinModelPortaliP96155.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. 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]
PfamiPF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

P96155-1 [UniParc]FASTAAdd to Basket

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MNYRIDFAVL SEHPQFCRFG LTLHNLSDQD LKAWSLHFTI DRYIQPDSIS    50
HSQIHQVGSF CSLTPEQDVI NSNSHFYCEF SIKTAPFPFH YYTDGIKAAF 100
VQINDVEPRV RHDVIVTPIA LASPYRERSE IPATDAATLS LLPKPNHIER 150
LDGEFALTAG SQISLQSSCA ETAATWLKQE LTHLYQWQPH DIGSADIVLR 200
TNPTLDEGAY LLSVDRKPIR LEASSHIGFV HASATLLQLV RPDGDNLLVP 250
HIVIKDAPRF KYRGMMLDCA RHFHPLERVK RLINQLAHYK FNTFHWHLTD 300
DEGWRIEIKS LPQLTDIGAW RGVDEVLEPQ YSLLTEKHGG FYTQEEIREV 350
IAYAAERGIT VIPEIDIPGH SRAAIKALPE WLFDEDDQSQ YRSIQYYNDN 400
VLSPALPGTY RFLDCVLEEV AALFPSHFIH IGADEVPDGV WVNSPKCQAL 450
MAEEGYTDAK ELQGHLLRYA EKKLKSLGKR MVGWEEAQHG DKVSKDTVIY 500
SWLSEQAALN CARQGFDVIL QPGQFTYLDI AQDYAPEEPG VDWAGVTPLE 550
RAYRYEPLVE VPEHDPLRKR ILGIQCALWC ELVNNQDRMD YMIYPRLTAL 600
AGSGLDTKIP A 611
Length:611
Mass (Da):69,502
Last modified:May 1, 1997 - v1
Checksum:iE04C700E88F4D8C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U41417 Genomic DNA. Translation: AAC44672.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U41417 Genomic DNA. Translation: AAC44672.1 .

3D structure databases

ProteinModelPortali P96155.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00349 .
BioCyci MetaCyc:MONOMERMETA-16856.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProi IPR025705. 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 ]
Pfami PF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view ]
PRINTSi PR00738. GLHYDRLASE20.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiHEX1_VIBFU
AccessioniPrimary (citable) accession number: P96155
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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