CAZyme Information: MGYG000004538_01409

Basic Information

• Species: CAG-313 sp900760745
• Lineage: Bacteria; Firmicutes; Bacilli; ML615J-28; CAG-313; CAG-313; CAG-313 sp900760745
• CAZyme ID: MGYG000004538_01409
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
601	MGYG000004538_27|CGC1	70108.28	5.4737

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004538	1759821	MAG	Israel	Asia

• Gene Location: Start: 1730; End: 3535 Strand: +

Full Sequence      

MKIYPIPQKIDIKKSILVDKKIKHISNDFSEKLLEIGKQIVQIDAASQTLLFIKKDLSVV
NDEGYHLEITSNCIEIKAKTEQGAFYGLMTLQQLYREENISQVYIEDYPDLKIRGVMLDI
SRSKVPTVATLKSLIDFFASLKYNHLELYVEGFSFEYRSFPNVLKDHNYLSLDEYLEIEA
YAKEKYIDFVPNQNGFGHMSDWLQKEEYKSLAECPEGFYIWGCHRIPSTLDPTNPESVQL
VEKMYKDMLPYTSSKYFNMNFDEPYELGSGKSKEKCEQTSKEDVYIEFFNQLAAVVKSYH
KTPMIWGDVLIKNRDKVNLLPKDVIFIDWGYNKDYPFKEHASMLKEKNINYLTAPGTSSW
STITGRLMDMQETIENSTTSAKKYNGLGAIITDWGDMGHLQYLPSSYLGFIYGALLCWSK
ATLDDARIVLKDKLADDKLEEVIVDLSTYHLLEGPYRDYGSRLFSTIMWAEHAQRQTDPK
TFFLEKMQSNYIEEENQKKLKQLFSLNKEKLKEAKDTLEKAEMKNAIDLLETLLAINDKL
YSYSQSCIVSFDNEIKQLETYLNKHLELWCARNKKEGYEFSANRIHWLIEMLMCLDRKER
V

Enzyme Prediction     

No EC number prediction in MGYG000004538_01409.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	112	398	1.9e-45	0.884272997032641

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	3.65e-82	113	419	1	301	Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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.
cd06564	GH20_DspB_LnbB-like	2.87e-23	112	398	1	299	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.
cd02742	GH20_hexosaminidase	5.07e-23	113	396	1	278	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.
pfam00728	Glyco_hydro_20	1.67e-19	114	329	4	239	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06570	GH20_chitobiase-like_1	4.64e-18	114	329	4	223	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVK17427.1	7.59e-154	40	593	44	611
AYQ72904.1	8.44e-110	60	592	86	628
QNK59368.1	2.31e-108	63	590	83	621
ABV34402.1	2.38e-107	5	432	3	443
CEP77548.1	9.94e-106	3	591	14	602

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4H04_A	2.44e-13	60	329	107	375	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
3GH4_A	8.04e-13	58	306	117	375	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]
7DUP_A	6.66e-10	22	329	38	389	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	2.68e-09	22	329	38	389	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]
5A6B_D	6.38e-08	93	405	80	410	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49009	1.06e-15	57	425	123	523	Beta-hexosaminidase subunit alpha OS=Entamoeba histolytica OX=5759 GN=HEXA PE=1 SV=2
Q54SC9	2.33e-15	62	310	108	366	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 SV=1
P43077	7.58e-15	56	386	105	447	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
E9DFH0	1.76e-13	56	330	115	415	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
Q86M34	8.34e-12	41	320	111	414	Beta-hexosaminidase subunit beta OS=Entamoeba histolytica OX=5759 GN=HEXB 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
1.000065	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004538_01409.