CAZyme Information: MGYG000003119_00394

Basic Information

• Species: Capnocytophaga ochracea
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Flavobacteriaceae; Capnocytophaga; Capnocytophaga ochracea
• CAZyme ID: MGYG000003119_00394
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
643	MGYG000003119_6|CGC1	74414.11	7.5936

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003119	2451559	MAG	United States	North America

• Gene Location: Start: 42664; End: 44595 Strand: -

Full Sequence      

MKFYIFFIYLWCVPPCVLYAGIEHLLPAPQQVIANGQRYKVASAETRPIIIVEIVADLPE
IPVNKDEGYTLEVTKNCILIRAISGKGVYWAKQTLKQLLITKGNKAYYEGCKIIDYPAFR
VRGFMQDVGRTFMSLEELKREIALLSQYKINVFHWHLTENQGWRLQSLRYPELNAPSNYD
RMPAQYYTLQEAKELVSFCKEHNVLLIPEIDMPGHSRAFEKAFGVAMQSEKGIAILKELL
DEVVENFDVPYIHIGTDEVVFSNPQFVPEMVAYLRHKGKKVISWNPGWQYKAGEIDMTQL
WSYRGKAQKGIPAIDSKFHYINHFDAFADLVALYNSRILNVPQGDDEHAGAIIGLWNDRY
IKGERNIFIQNNFYPAMLALAERSWKGGGSEYFDGKGTMLPTDTNDPIFKQFADFERRMY
WHKTHHFTTEPFAYVPQTKVVWRITDAFPNNGNLAQSFPPEKALKESYSYEGKTYHTHKA
IGAGIYLRHTWGELVPAFYKNPQPNHTAYAYTYVYSPEEQQVGLWVSFQDYSRSEKDLPP
PQGKWDYKESKIWLNNTELSPPIWESTHRELSNEIPLTNENFQVRPPLQVTLNKGWNKVL
LKLPVGAFYTPEVRLVKWQFTCVFVTPDGKDAVKNLIYADTQR

Enzyme Prediction     

No EC number prediction in MGYG000003119_00394.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	115	386	4.6e-59	0.9673590504451038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02742	GH20_hexosaminidase	9.34e-87	122	386	2	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.
cd06563	GH20_chitobiase-like	7.96e-48	119	419	1	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	1.46e-45	119	385	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06568	GH20_SpHex_like	2.01e-40	119	321	1	231	A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. 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. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.
cd06564	GH20_DspB_LnbB-like	2.80e-39	121	387	2	326	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLF50863.1	0.0	1	643	1	643
VEI53476.1	0.0	1	643	1	643
ATA85113.1	0.0	1	643	1	643
ATA70211.1	0.0	1	643	1	643
ACU92970.1	0.0	1	643	1	643

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GH4_A	5.71e-37	66	394	121	499	Crystalstructure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]
4PYS_A	1.07e-34	67	394	78	471	Thecrystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343],4PYS_B The crystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343]
6YHH_A	1.12e-33	60	385	85	476	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
7DUP_A	1.23e-33	34	258	52	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
7DVB_A	5.51e-33	34	258	52	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49008	9.18e-33	65	385	109	503	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	4.71e-26	67	385	97	500	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
P96155	8.87e-26	66	259	206	436	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q619W7	2.04e-25	49	259	93	323	Beta-hexosaminidase A OS=Caenorhabditis briggsae OX=6238 GN=hex-1 PE=3 SV=2
Q7WUL4	1.04e-24	49	385	68	448	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 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
0.513116	0.479273	0.005147	0.000769	0.000489	0.001203

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003119_00394.