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CAZyme Information: MGYG000002455_01662

You are here: Home > Sequence: MGYG000002455_01662

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 Bacteroides cellulosilyticus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides cellulosilyticus
CAZyme ID MGYG000002455_01662
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1106 MGYG000002455_6|CGC3 125600.32 5.8514
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002455 6974062 Isolate United States North America
Gene Location Start: 151232;  End: 154552  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002455_01662.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH35 357 668 3.9e-117 0.990228013029316
GH43 55 311 1.4e-103 0.991869918699187

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18825 GH43_CtGH43-like 5.35e-163 47 326 1 285
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 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. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. 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.
pfam01301 Glyco_hydro_35 2.37e-156 356 666 1 313
Glycosyl hydrolases family 35.
cd08985 GH43_CtGH43-like 1.25e-118 47 326 1 273
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 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. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. 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.
cd18826 GH43_CtGH43-like 7.00e-110 47 326 1 269
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 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. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. 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.
cd18822 GH43_CtGH43-like 8.78e-106 47 326 1 266
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 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. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALJ58885.1 0.0 1 1106 1 1106
QUT89998.1 0.0 1 1106 1 1106
QDO67465.1 0.0 1 1106 1 1106
QUT62346.1 0.0 2 1106 3 1106
QUT64844.1 0.0 2 1106 3 1106

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6EON_A 0.0 343 1105 21 778
GalactanaseBT0290 [Bacteroides thetaiotaomicron VPI-5482]
3D3A_A 2.46e-263 347 955 5 605
Crystalstructure of a beta-galactosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
4MAD_A 5.39e-144 356 923 23 578
ChainA, Beta-galactosidase [Niallia circulans],4MAD_B Chain B, Beta-galactosidase [Niallia circulans]
3THC_A 2.10e-123 345 907 4 581
Crystalstructure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_B Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_C Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_D Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THD_A Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_B Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_C Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_D Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens]
3WF3_A 2.13e-123 345 907 28 605
Crystalstructure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_B Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_C Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_D Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF4_A Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_B Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_C Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_D Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P16278 2.21e-122 345 907 27 604
Beta-galactosidase OS=Homo sapiens OX=9606 GN=GLB1 PE=1 SV=2
Q9TRY9 1.77e-121 357 907 42 605
Beta-galactosidase OS=Canis lupus familiaris OX=9615 GN=GLB1 PE=1 SV=3
Q5R7P4 2.29e-121 345 907 27 604
Beta-galactosidase OS=Pongo abelii OX=9601 GN=GLB1 PE=2 SV=1
P23780 7.24e-121 349 907 34 606
Beta-galactosidase OS=Mus musculus OX=10090 GN=Glb1 PE=1 SV=1
P48982 2.71e-118 354 906 33 573
Beta-galactosidase OS=Xanthomonas manihotis OX=43353 GN=bga PE=1 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
0.000444 0.998378 0.000536 0.000239 0.000192 0.000183

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002455_01662.