CAZyme Information: MGYG000003178_01947

Basic Information

• Species: Klebsiella quasivariicola
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella quasivariicola
• CAZyme ID: MGYG000003178_01947
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
368		41229.25	4.8351

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003178	3011876	MAG	United States	North America

• Gene Location: Start: 76; End: 1182 Strand: +

Full Sequence      

MDTITDSDSAQSWQFSMPRLKGSAVEGSFTLVKGDSGWRGFIDFKGKSRRAVQEIEWLDD
NQVTFRVDTWMGETRPVLTINNDTLSGYFLLGNTRYPVDGKRLDAVPQGIQPTLPDAQQQ
KNLLGGEAALWAENVAAPVIDIKLWPRAFAVAERLWSAEDVKDSDNMYQRLQAMDSWSTV
SVGLQQHAQQLEQFTRLANSSHTLALQILAEALEPAHYYTRQHLKFQANNYHQFEPLNRL
ADALPAESDTVRSLNQWAERLISDAEDAESADGLRHVFTRWQNNSGDALALTDNNYQLAA
IKPVVQQVDKLASLGLRLTDLVARQGTLDDKEYASILAQLDTAAKTQDELVIAAVYPLEK
LLRATKIK

Enzyme Prediction     

EC	3.2.1.52

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06570	GH20_chitobiase-like_1	1.13e-18	123	171	263	311	A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This subgroup lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
cd06562	GH20_HexA_HexB-like	1.05e-16	116	174	282	340	Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
cd06563	GH20_chitobiase-like	1.72e-11	112	171	297	357	The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
pfam00728	Glyco_hydro_20	1.68e-10	112	158	298	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	1.81e-07	118	157	262	303	Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASV22277.1	8.33e-261	1	368	429	796
QBL51290.1	9.95e-260	1	368	430	797
QVJ10661.1	5.03e-255	1	368	430	797
QII33357.1	2.03e-254	1	368	430	797
QHJ54117.1	5.80e-254	1	368	430	797

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YHH_A	1.84e-18	86	362	410	672	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
2GK1_N	9.94e-12	118	171	160	214	X-raycrystal structure of NGT-bound HexA [Homo sapiens],2GK1_P X-ray crystal structure of NGT-bound HexA [Homo sapiens],2GK1_R X-ray crystal structure of NGT-bound HexA [Homo sapiens],2GK1_T X-ray crystal structure of NGT-bound HexA [Homo sapiens]
1NP0_D	1.05e-11	118	171	160	214	Humanlysosomal beta-hexosaminidase isoform B in complex with intermediate analogue NAG-thiazoline [Homo sapiens],1NP0_F Human lysosomal beta-hexosaminidase isoform B in complex with intermediate analogue NAG-thiazoline [Homo sapiens]
5BRO_A	1.74e-11	30	171	355	487	Crystalstructure of modified HexB (modB) [Homo sapiens]
1NOU_A	4.09e-11	118	171	426	480	Nativehuman lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOU_B Native human lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOW_A Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],1NOW_B Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],2GJX_B Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_C Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_F Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_G Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P07686	2.39e-10	118	171	475	529	Beta-hexosaminidase subunit beta OS=Homo sapiens OX=9606 GN=HEXB PE=1 SV=4
Q29548	1.72e-09	118	171	450	503	Beta-hexosaminidase subunit beta OS=Sus scrofa OX=9823 GN=HEXB PE=1 SV=2
P49614	3.04e-09	118	171	450	503	Beta-hexosaminidase subunit beta OS=Felis catus OX=9685 GN=HEXB PE=2 SV=2
P20060	1.27e-08	117	171	453	508	Beta-hexosaminidase subunit beta OS=Mus musculus OX=10090 GN=Hexb PE=1 SV=2
Q8L7S6	1.24e-07	11	171	354	501	Beta-hexosaminidase 3 OS=Arabidopsis thaliana OX=3702 GN=HEXO3 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003178_01947.