P96155 (HEX1_VIBFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-hexosaminidase
EC=3.2.1.52

Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase

Gene names

Name:

exo I

Organism

Vibrio furnissii

Taxonomic identifier

29494 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Periplasm
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 611	611	Beta-hexosaminidase		PRO_0000215377

Sequences

	Sequence		Length	Mass (Da)
	P96155 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: E04C700E88F4D8C3	FASTA	611	69,502
	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

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
ProteinModelPortal	P96155.
ModBase	Search...
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMERMETA-16856.
UniPathway	UPA00349.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR025705. Beta_hexosaminidase_sua/sub. IPR015883. Glyco_hydro_20_cat-core. IPR015882. Glyco_hydro_20b. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PRINTS	PR00738. GLHYDRLASE20.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HEX1_VIBFU

Accession

Primary (citable) accession number: P96155

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program