CAZyme Information: MGYG000000014_03243

Basic Information

• Species: Clostridium butyricum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium butyricum
• CAZyme ID: MGYG000000014_03243
• CAZy Family: GH4
• CAZyme Description: putative 6-phospho-beta-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
437	MGYG000000014_17|CGC1	48736.47	5.4045

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000014	4564499	Isolate	United Kingdom	Europe

• Gene Location: Start: 11076; End: 12389 Strand: +

Full Sequence      

MDKKIKIVTIGGGSSYTPELIEGFIKRYHELPVGEIWLVDIESGKEKLEIVGNLAKRMVK
KAGVPIDIHLTLDRREALKDADFVTTQIRVGQLDARNKDERIPLSHGVIGQETNGAGGMF
KAFRTIPVILDIDKDMSQLCPNAWLINFSNPAGMVTEALLKYGINKKVIGLCNVPIGMEK
AVAGMLDVDFNRITMTFAGLNHMVFGKEIYLDGENVTDKVINSIAEGKMGSIVKNIKDFE
WSPHFIKALNMMPCPYHKYYYQTSEMLEDELKEFSKGETRAEIVQKLEKDLFELYKDETL
DIKPPQLEKRGGAYYSDAACRLINSIYNDKKDIQPVDVRNNGAIEGIDDNSAVEVSCIIT
KDGPKPLSIGKLPVAVNGLVQTIKSFEKLVVDAAVEGDYNKALLALTINPLIPSEKMAKV
LLDELLEAHKEYLPQFN

Enzyme Prediction     

EC	3.2.1.86

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH4	6	185	2.2e-77	0.9888268156424581

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd05296	GH4_P_beta_glucosidase	0.0	5	433	1	419	Glycoside Hydrolases Family 4; Phospho-beta-glucosidase. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the phospho-beta-glucosidases. Other organisms (such as archaea and Thermotoga maritima ) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. The 6-phospho-beta-glucosidase from Thermotoga maritima hydrolylzes cellobiose 6-phosphate (6P) into glucose-6P and glucose, in an NAD+ and Mn2+ dependent fashion. The Escherichia coli 6-phospho-beta-glucosidase (also called celF) hydrolyzes a variety of phospho-beta-glucosides including cellobiose-6P, salicin-6P, arbutin-6P, and gentobiose-6P. Phospho-beta-glucosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.
COG1486	CelF	0.0	3	436	2	439	Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism].
cd05197	GH4_glycoside_hydrolases	1.09e-173	5	428	1	425	Glycoside Hydrases Family 4. Glycoside hydrolases cleave glycosidic bonds to release smaller sugars from oligo- or polysaccharides. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by GH4 glycoside hydrolases. Other organisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. GH4 family members include 6-phospho-beta-glucosidases, 6-phospho-alpha-glucosidases, alpha-glucosidases/alpha-glucuronidases (only from Thermotoga), and alpha-galactosidases. They require two cofactors, NAD+ and a divalent metal (Mn2+, Ni2+, Mg2+), for activity. Some also require reducing conditions. GH4 glycoside hydrolases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.
cd05298	GH4_GlvA_pagL_like	6.25e-115	6	437	2	437	Glycoside Hydrolases Family 4; GlvA- and pagL-like glycosidases. Bacillus subtilis GlvA and Clostridium acetobutylicum pagL are 6-phospho-alpha-glucosidase, catalyzing the hydrolysis of alpha-glucopyranoside bonds to release glucose from oligosaccharides. The substrate specificities of other members of this subgroup are unknown. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP_PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases, which include 6-phospho-beta-glucosidases, 6-phospho-alpha-glucosidases, alpha-glucosidases/alpha-glucuronidases (only from Thermotoga), and alpha-galactosidases. Members of this subfamily are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.
pfam02056	Glyco_hydro_4	1.43e-80	6	188	1	183	Family 4 glycosyl hydrolase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXB83769.1	0.0	1	437	1	437
QGH27631.1	0.0	1	437	1	437
QGH23586.1	0.0	1	437	1	437
QCJ05878.1	0.0	1	437	1	437
QSX02431.1	0.0	1	437	1	437

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5C3M_A	1.59e-223	1	436	1	437	Crystalstructure of Gan4C, a GH4 6-phospho-glucosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5C3M_B Crystal structure of Gan4C, a GH4 6-phospho-glucosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5C3M_C Crystal structure of Gan4C, a GH4 6-phospho-glucosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5C3M_D Crystal structure of Gan4C, a GH4 6-phospho-glucosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
1S6Y_A	5.30e-218	2	436	5	440	2.3Acrystal structure of phospho-beta-glucosidase [Geobacillus stearothermophilus]
1UP7_A	3.61e-80	3	433	1	414	Structureof the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_B Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_C Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_D Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_E Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_F Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_G Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_H Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8]
1UP4_A	8.23e-78	6	433	2	412	Structureof the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_B Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_C Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_D Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_E Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_F Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_G Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_H Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8]
1UP6_A	8.47e-78	6	433	3	413	Structureof the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_B Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_C Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_D Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_E Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_F Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_G Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_H Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P46320	5.95e-222	1	436	1	436	Probable 6-phospho-beta-glucosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=licH PE=2 SV=1
P17411	1.44e-164	1	436	1	439	6-phospho-beta-glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=chbF PE=1 SV=4
Q9X108	2.63e-79	5	433	1	412	6-phospho-beta-glucosidase BglT OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bglT PE=1 SV=1
Q97LM4	6.69e-73	3	437	2	441	Maltose-6'-phosphate glucosidase MalH OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=malH PE=1 SV=1
C7NB67	3.83e-67	3	434	2	437	6-phospho-alpha-glucosidase OS=Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b) OX=523794 GN=pagL 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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000014_03243.