Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-hexosaminidase

Gene

exo I

Organism
Vibrio furnissii
Status
Reviewed-Annotation score: 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.
BRENDAi3.2.1.52. 6631.
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-hexosaminidasePRO_0000215377Add
BLAST

Expressioni

Inductioni

By (GlcNAc)2.

Interactioni

Subunit structurei

Homodimer.Curated

Structurei

3D structure databases

ProteinModelPortaliP96155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

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

« Hide

        10         20         30         40         50
MNYRIDFAVL SEHPQFCRFG LTLHNLSDQD LKAWSLHFTI DRYIQPDSIS
60 70 80 90 100
HSQIHQVGSF CSLTPEQDVI NSNSHFYCEF SIKTAPFPFH YYTDGIKAAF
110 120 130 140 150
VQINDVEPRV RHDVIVTPIA LASPYRERSE IPATDAATLS LLPKPNHIER
160 170 180 190 200
LDGEFALTAG SQISLQSSCA ETAATWLKQE LTHLYQWQPH DIGSADIVLR
210 220 230 240 250
TNPTLDEGAY LLSVDRKPIR LEASSHIGFV HASATLLQLV RPDGDNLLVP
260 270 280 290 300
HIVIKDAPRF KYRGMMLDCA RHFHPLERVK RLINQLAHYK FNTFHWHLTD
310 320 330 340 350
DEGWRIEIKS LPQLTDIGAW RGVDEVLEPQ YSLLTEKHGG FYTQEEIREV
360 370 380 390 400
IAYAAERGIT VIPEIDIPGH SRAAIKALPE WLFDEDDQSQ YRSIQYYNDN
410 420 430 440 450
VLSPALPGTY RFLDCVLEEV AALFPSHFIH IGADEVPDGV WVNSPKCQAL
460 470 480 490 500
MAEEGYTDAK ELQGHLLRYA EKKLKSLGKR MVGWEEAQHG DKVSKDTVIY
510 520 530 540 550
SWLSEQAALN CARQGFDVIL QPGQFTYLDI AQDYAPEEPG VDWAGVTPLE
560 570 580 590 600
RAYRYEPLVE VPEHDPLRKR ILGIQCALWC ELVNNQDRMD YMIYPRLTAL
610
AGSGLDTKIP A
Length:611
Mass (Da):69,502
Last modified:May 1, 1997 - v1
Checksum:iE04C700E88F4D8C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41417 Genomic DNA. Translation: AAC44672.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41417 Genomic DNA. Translation: AAC44672.1.

3D structure databases

ProteinModelPortaliP96155.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00349.
BioCyciMetaCyc:MONOMERMETA-16856.
BRENDAi3.2.1.52. 6631.

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.
ProtoNetiSearch...

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(1995) [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: April 1, 2015
This is version 87 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

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.