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CAZyme Information: MGYG000001640_00955

You are here: Home > Sequence: MGYG000001640_00955

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 Duncaniella sp900549445
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp900549445
CAZyme ID MGYG000001640_00955
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1088 MGYG000001640_35|CGC1 122629.73 5.5735
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001640 2860567 MAG United States North America
Gene Location Start: 11833;  End: 15099  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001640_00955.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH35 340 651 1.2e-118 0.990228013029316
GH43 77 308 1.8e-91 0.9957081545064378

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01301 Glyco_hydro_35 5.18e-155 339 649 1 313
Glycosyl hydrolases family 35.
cd08983 GH43_Bt3655-like 1.34e-90 61 323 1 262
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. 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.
PLN03059 PLN03059 3.65e-51 337 907 34 715
beta-galactosidase; Provisional
COG1874 GanA 6.63e-42 338 908 6 593
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
cd08978 GH_F 4.25e-19 81 316 1 244
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. 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 of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 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
QCD35705.1 0.0 112 1088 87 1105
QDO67465.1 0.0 135 1088 173 1106
ALJ58885.1 0.0 148 1088 183 1106
QUT89998.1 0.0 148 1088 183 1106
QUT64844.1 0.0 148 1088 182 1106

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6EON_A 0.0 331 1087 26 778
GalactanaseBT0290 [Bacteroides thetaiotaomicron VPI-5482]
3D3A_A 4.22e-257 331 922 6 590
Crystalstructure of a beta-galactosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
4MAD_A 1.70e-140 339 905 23 578
ChainA, Beta-galactosidase [Niallia circulans],4MAD_B Chain B, Beta-galactosidase [Niallia circulans]
7KDV_A 1.49e-122 332 905 17 606
ChainA, Beta-galactosidase [Mus musculus],7KDV_C Chain C, Beta-galactosidase [Mus musculus],7KDV_E Chain E, Beta-galactosidase [Mus musculus],7KDV_G Chain G, Beta-galactosidase [Mus musculus],7KDV_I Chain I, Beta-galactosidase [Mus musculus],7KDV_K Chain K, Beta-galactosidase [Mus musculus]
3THC_A 4.31e-121 337 905 15 598
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P48982 8.31e-123 337 888 33 573
Beta-galactosidase OS=Xanthomonas manihotis OX=43353 GN=bga PE=1 SV=1
P23780 5.07e-121 332 905 34 623
Beta-galactosidase OS=Mus musculus OX=10090 GN=Glb1 PE=1 SV=1
P16278 4.51e-120 337 905 38 621
Beta-galactosidase OS=Homo sapiens OX=9606 GN=GLB1 PE=1 SV=2
Q5R7P4 4.66e-119 337 889 38 604
Beta-galactosidase OS=Pongo abelii OX=9601 GN=GLB1 PE=2 SV=1
Q9TRY9 3.75e-118 340 889 42 605
Beta-galactosidase OS=Canis lupus familiaris OX=9615 GN=GLB1 PE=1 SV=3

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
0.000239 0.999139 0.000171 0.000161 0.000143 0.000133

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001640_00955.