CAZyme Information: MGYG000004468_00962

Basic Information

• Species: Alistipes_A sp900539755
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900539755
• CAZyme ID: MGYG000004468_00962
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
845	MGYG000004468_2|CGC3	96574.52	7.1094

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004468	2418771	MAG	Israel	Asia

• Gene Location: Start: 201740; End: 204277 Strand: -

Full Sequence      

MKSKSLHTLILGILLPVLWITATNSASGQQLIPQPNQVTRHEGTFTITSQTVLVTHEFKD
LANYLNDHIEQLCGFRLAVVTHAPDTNYISLRKNQHLTHEAYSLAITPRSIVIRGGDRGG
VFYGLQTLFQLMPSEVFAKRDSLIQDSLPNITSLQLHAVTIVDAPRFAYRGAMLDVSRTF
FTKEQVMQYLDWMSRHKLNRFHWHLTDDNGWRIEIKKYPFLTSKGAWRGPDEVLEPAYGS
GQKRYGGFYTQDDIREIVRYAAFRNIEIIPEINLPGHALALTASYPETFCSTTTATDESE
MTDITVTGNVVCVGREENFEMIRDIIHEVAALFPSHYLHLGGDEVSTRYWQKCPRCQKLM
KTHGMKSPKKLYEYFVNRVEKIAHEEGKRCVFWDEALSPELSSHTMISGWHDLATCKKAI
DQEQPVIVMPASYCYIDMKQNAFERGHTWAWLVDTRRIYSLQPDKLTSDPLKQKYVRGVE
AALWAELLDRPDRFFEYQSYPRLCALAEVGWSKPSQRNWEDFYSRLTQGHLPRLAAMGID
FYLFPPEVNYKQGMITATALPGASIYYTKDDSEPTQQSLQYTGPIFDTLQERYRFRSFYQ
GRRSPIIPISTDTAKILPARSRDTITFPLNQYIDRDGIWYLTITPSDPETVINRMNITGP
DTTYSIIRYGQKANPFAPLRLYMDPRNRNADLTLIVTNNSTAENLTVFRFRPSPYFEPQT
EISSSLTFSSRFPSQRIADYNPTTYSRSTQACQAGDFLQYNFTDSVTCRAIIVRTGIPNI
TRYIVTQGEVSYSHDGHNFVDAGVLDDNGCATIHPSMPVKAVRINITGDNGESIVAFQDL
QILPQ

Enzyme Prediction     

No EC number prediction in MGYG000004468_00962.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	162	513	9.5e-112	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	5.10e-172	167	526	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	6.17e-131	167	513	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	6.63e-121	30	624	135	726	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	1.11e-100	167	526	1	329	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.
cd06569	GH20_Sm-chitobiase-like	3.06e-81	163	544	1	441	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. 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
BCG55301.1	0.0	28	845	23	832
QGA24588.1	2.50e-305	28	845	18	828
AYN06483.1	4.35e-214	12	844	4	834
ABQ07807.1	7.80e-212	12	844	4	834
QGK72774.1	1.25e-207	12	844	4	834

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Q63_A	7.78e-102	30	585	30	588	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
6EZR_A	8.52e-100	29	541	140	637	Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZR_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZS_A Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6EZS_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6K35_A Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi],6K35_B Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi]
6EZT_A	1.14e-98	29	541	137	634	Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi],6EZT_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi]
7DUP_A	8.12e-88	31	528	6	508	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	4.28e-87	31	528	6	508	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	9.28e-99	28	585	34	585	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	2.30e-87	20	510	131	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UQG6	1.97e-77	74	565	74	544	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
B2UP57	1.15e-68	97	527	55	463	Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1
Q04786	3.89e-56	26	552	195	767	Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000249	0.999117	0.000165	0.000156	0.000141	0.000135

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004468_00962.