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CAZyme Information: MGYG000004456_00784

You are here: Home > Sequence: MGYG000004456_00784

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Prevotella sp900556795
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556795
CAZyme ID MGYG000004456_00784
CAZy Family GH43
CAZyme Description Beta-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1540 MGYG000004456_6|CGC2 175892.79 7.1727
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004456 3541309 MAG Israel Asia
Gene Location Start: 58617;  End: 63239  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004456_00784.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH2 539 1415 1.2e-205 0.9654255319148937
GH43 18 286 2.1e-111 0.9889705882352942

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10340 ebgA 0.0 505 1538 4 1000
cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK09525 lacZ 0.0 505 1526 17 1020
beta-galactosidase.
cd09002 GH43_XYL-like 1.10e-147 15 288 1 271
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
COG3250 LacZ 7.48e-147 543 1414 9 802
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
smart01038 Bgal_small_N 5.06e-86 1260 1535 1 272
Beta galactosidase small chain. This domain comprises the small chain of dimeric beta-galactosidases EC:3.2.1.23. This domain is also found in single chain beta-galactosidase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNT67030.1 0.0 486 1540 25 1089
BCS85008.1 0.0 499 1535 23 1050
ALO49591.1 0.0 499 1538 24 1050
QUB81015.1 0.0 500 1538 27 1054
QUB84549.1 0.0 493 1540 16 1052

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6S6Z_A 1.89e-192 546 1536 38 980
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 1.95e-192 546 1536 39 981
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]
3DEC_A 5.31e-184 504 1538 6 997
ChainA, Beta-galactosidase [Bacteroides thetaiotaomicron VPI-5482]
3BGA_A 7.91e-181 497 1538 2 1001
Crystalstructure of beta-galactosidase from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],3BGA_B Crystal structure of beta-galactosidase from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482]
4V41_A 1.99e-138 504 1534 15 1019
E.COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_B E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_C E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_D E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_E E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_F E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_G E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_H E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_I E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_J E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_K E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_L E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_M E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_N E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_O E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V41_P E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC) [Escherichia coli BL21],4V44_A E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_B E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_C E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_D E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_E E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_F E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_G E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_H E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_I E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_J E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_K E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_L E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_M E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_N E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_O E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V44_P E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE [Escherichia coli],4V45_A E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_B E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_C E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_D E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_E E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_F E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_G E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_H E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_I E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_J E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_K E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_L E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_M E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_N E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_O E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli],4V45_P E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O52847 2.37e-194 502 1538 17 1034
Beta-galactosidase OS=Priestia megaterium (strain DSM 319 / IMG 1521) OX=592022 GN=bgaM PE=3 SV=1
Q56307 1.07e-191 546 1536 39 981
Beta-galactosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=lacZ PE=1 SV=2
Q9K9C6 2.11e-175 506 1534 11 1008
Beta-galactosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=lacZ PE=3 SV=1
Q6LL68 5.65e-166 504 1537 11 1027
Beta-galactosidase OS=Photobacterium profundum (strain SS9) OX=298386 GN=lacZ PE=3 SV=1
Q7MG04 1.67e-160 504 1537 12 1028
Beta-galactosidase OS=Vibrio vulnificus (strain YJ016) OX=196600 GN=lacZ PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.489914 0.509055 0.000270 0.000391 0.000188 0.000188

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004456_00784.