CAZyme Information: MGYG000000992_01293

Basic Information

• Species: UBA737 sp900547445
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA737; UBA737 sp900547445
• CAZyme ID: MGYG000000992_01293
• CAZy Family: GH2
• CAZyme Description: Evolved beta-galactosidase subunit alpha

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
324		37158.59	4.5597

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000992	1558058	MAG	Denmark	Europe

• Gene Location: Start: 975; End: 1949 Strand: +

Full Sequence      

MRRYENPLKTSENRLRPRSWYIPEGSEICPLNGEWRFVYFENGDRVGEITEWGNITVPSC
WQLEGYGKPNYTNINYPFPCDPPYVPDINPVGVYERSFQVTDGSLETYLVFEGVSSEAEV
YINGRYVGFTQGSRLMAEFDISEFVSSGTNTVRVYVRKWCCGSYLEDQDAFRFSGIFRDV
YILSRPHGHIFDLDIRTEENSIICTADTNFTAELYDGESLLSSSISDEGKLCFTVDTPKL
WTAETPNLYTVKLTAAGETITRKVGFRTIEISADYEFLINGTPVKLKGVNHHDTHPEKGW
TMSEEDYVRDLKLMKELNINTIRT

Enzyme Prediction     

No EC number prediction in MGYG000000992_01293.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	23	324	4.8e-87	0.37101063829787234

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10340	ebgA	6.90e-108	1	324	1	374	cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK09525	lacZ	1.28e-104	2	324	15	390	beta-galactosidase.
COG3250	LacZ	1.15e-78	25	324	9	340	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam02837	Glyco_hydro_2_N	9.26e-43	31	186	4	169	Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.
PRK10150	PRK10150	4.61e-28	94	324	69	332	beta-D-glucuronidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO38829.1	6.04e-115	1	324	1	325
QBF74607.1	6.17e-115	1	324	2	326
BCJ98677.1	4.63e-97	4	324	11	357
ANE45227.1	2.15e-91	4	324	8	364
BCG60948.1	5.40e-87	13	324	17	364

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6S6Z_A	4.68e-67	4	324	4	366	Structureof beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_B Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_C Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_D Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_E Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_F Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_G Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_H Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8]
6SD0_A	4.70e-67	4	324	5	367	Structureof beta-galactosidase from Thermotoga maritima. [Thermotoga maritima MSB8],6SD0_B Structure of beta-galactosidase from Thermotoga maritima. [Thermotoga maritima MSB8],6SD0_C Structure of beta-galactosidase from Thermotoga maritima. [Thermotoga maritima MSB8],6SD0_D Structure of beta-galactosidase from Thermotoga maritima. [Thermotoga maritima MSB8]
6CVM_A	8.78e-67	2	323	13	387	Atomicresolution cryo-EM structure of beta-galactosidase [Escherichia coli K-12],6CVM_B Atomic resolution cryo-EM structure of beta-galactosidase [Escherichia coli K-12],6CVM_C Atomic resolution cryo-EM structure of beta-galactosidase [Escherichia coli K-12],6CVM_D Atomic resolution cryo-EM structure of beta-galactosidase [Escherichia coli K-12],6X1Q_A 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope [Escherichia coli K-12],6X1Q_B 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope [Escherichia coli K-12],6X1Q_C 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope [Escherichia coli K-12],6X1Q_D 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope [Escherichia coli K-12]
5A1A_A	1.21e-66	2	323	13	387	2.2A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor [Escherichia coli K-12],5A1A_B 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor [Escherichia coli K-12],5A1A_C 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor [Escherichia coli K-12],5A1A_D 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor [Escherichia coli K-12]
1F4A_A	1.21e-66	2	323	12	386	E.COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC) [Escherichia coli],1F4A_B E. COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC) [Escherichia coli],1F4A_C E. COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC) [Escherichia coli],1F4A_D E. COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC) [Escherichia coli],1F4H_A E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC) [Escherichia coli],1F4H_B E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC) [Escherichia coli],1F4H_C E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC) [Escherichia coli],1F4H_D E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC) [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P06864	4.48e-75	1	324	1	374	Evolved beta-galactosidase subunit alpha OS=Escherichia coli (strain K12) OX=83333 GN=ebgA PE=1 SV=4
O33815	2.54e-69	4	324	7	356	Beta-galactosidase OS=Staphylococcus xylosus OX=1288 GN=lacZ PE=3 SV=1
Q6LL68	4.54e-69	31	324	49	384	Beta-galactosidase OS=Photobacterium profundum (strain SS9) OX=298386 GN=lacZ PE=3 SV=1
A9MQ82	1.58e-68	2	323	15	389	Beta-galactosidase OS=Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) OX=41514 GN=lacZ PE=3 SV=2
P70753	3.59e-68	4	324	7	353	Beta-galactosidase OS=Actinobacillus pleuropneumoniae OX=715 GN=lacZ PE=3 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
1.000028	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000992_01293.