CAZyme Information: MGYG000000312_02249

Basic Information

• Species: Eisenbergiella sp900539715
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900539715
• CAZyme ID: MGYG000000312_02249
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
652	MGYG000000312_30|CGC2	73807.88	4.639

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000312	2782709	MAG	Sweden	Europe

• Gene Location: Start: 12052; End: 14010 Strand: +

Full Sequence      

MIFTCKSIPEGYEAGIRELLAPRGHEICREGCAAGSVALTFRAVEGDSIRGVYTVGEDGN
GGEAVLTAGHKTFFFRALMRLVRELENRGAAEDFAWEEPVFLDRNGTMLDCSRNSVLTVE
TIKKYIRMQAAVGMNTLMLYTEDTYEVPEYPYFGYMRGRYTKEELREMTDYAELFGIEMI
PCIQALAHLKNALRWAAMAGMQDTDDILMSGDEKVYDFVKACIKNATEPFHTKRVHLGMD
EAWALGLGKYLHKNGYHDKSEIMAAHLERVDKICKELGLEPMIWSDMYLRMVSEHNEYYD
IPLDADLSGAVKPPKGVTLVYWDYYHEDEEFYKEYLRMHRQLSEQVIFAGGGWVWNGVSP
NLELAKNTTEPAMKACKKAGVREAVCTMWQDNGAETPMLSGLPSIVRFAEHGFAEEVSEE
TIDTQLEFLTGCSAEALNLLGSLDHVNSSCTYDNPSKFLLYQDVLTGLFDAQTKGWDADA
YYAGLRDRLNRICEDWRLSNAEKTVDESVHASACLMLEMYGALADALSVKADLGKKIYEA
YHADDKEELRRLAQQDISLCMEKIEAYRELREKVWDDESKIFGWEVIDIRFGGLFARLKS
TQKRLNAYLDGKLAAVSELEEERLLFQPAAEGKEPGLLNCNQWAQIVSASPM

Enzyme Prediction     

No EC number prediction in MGYG000000312_02249.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	106	412	1.4e-42	0.9376854599406528

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	1.68e-105	106	412	3	299	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.
pfam18088	Glyco_H_20C_C	1.87e-60	453	639	23	194	Glycoside Hydrolase 20C C-terminal domain. This is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. The C-terminal domain is commonly known as Domain III is important in dimerization as it forms the primary interface of the dimer. However, there is presently no evidence supporting dimerization as being necessary for catalysis. Domain III is unusual among structurally characterized GH20 enzymes but in GH20 enzymes possessing domain III, dimerization seems to be a conserved feature.
cd02742	GH20_hexosaminidase	3.36e-44	106	399	3	286	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	9.27e-21	106	323	5	240	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06562	GH20_HexA_HexB-like	3.77e-16	106	289	5	213	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUG40135.1	2.89e-164	62	626	50	599
AIQ64921.1	1.19e-161	60	650	52	635
ALC91381.1	2.08e-161	71	625	59	599
ASM70625.1	1.27e-157	61	648	57	631
SDS03697.1	1.97e-157	62	651	53	630

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2EPL_X	9.66e-116	75	650	59	622	N-acetyl-B-D-glucosaminidase(GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPM_X N-acetyl-B-D-glucoasminidase (GCNA) from Stretococcus gordonii [Streptococcus gordonii],2EPN_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPN_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii]
5A69_A	1.94e-114	58	650	65	644	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-PUGNAc [Streptococcus pneumoniae TIGR4],5A6A_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6A_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6J_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_D GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6K_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5A6K_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5AC5_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4],5AC5_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4]
5A6B_A	1.94e-114	58	650	65	644	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5A6B_D	5.25e-114	58	650	65	643	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5AC4_A	5.39e-114	58	650	65	644	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4],5AC4_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A6QNR0	7.21e-10	131	355	27	242	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q8WVB3	4.68e-08	119	324	23	225	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
P49008	1.89e-07	97	287	166	387	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P49009	8.38e-07	75	296	154	407	Beta-hexosaminidase subunit alpha OS=Entamoeba histolytica OX=5759 GN=HEXA PE=1 SV=2

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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000312_02249.