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CAZyme Information: MGYG000003444_00117

You are here: Home > Sequence: MGYG000003444_00117

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9;
CAZyme ID MGYG000003444_00117
CAZy Family CBM38
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
835 MGYG000003444_30|CGC1 93449.74 4.8764
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003444 1503598 MAG Fiji Oceania
Gene Location Start: 5375;  End: 7882  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003444_00117.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH116 445 721 3.5e-64 0.7272727272727273
CBM38 76 198 6.8e-32 0.9612403100775194

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam04685 DUF608 4.90e-45 446 721 99 362
Glycosyl-hydrolase family 116, catalytic region. This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.
COG4354 COG4354 3.52e-37 272 728 248 720
Uncharacterized protein, contains GBA2_N and DUF608 domains [Function unknown].
pfam12215 Glyco_hydr_116N 5.10e-09 170 339 159 309
beta-glucosidase 2, glycosyl-hydrolase family 116 N-term. This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 320 to 354 amino acids in length. This domain is found associated with pfam04685. It is found just after the extreme N-terminus. The N-terminal is thought to be the luminal domain while the C terminal is the cytosolic domain. The catalytic domain of GBA-2 is unknown. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335 in the downstream family pfam04685.
TIGR01577 oligosac_amyl 0.005 430 565 329 469
oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT37401.1 0.0 1 832 196 1030
QBJ18459.1 0.0 1 832 196 1030
QDO68264.1 0.0 1 835 196 1033
ASV73565.1 3.84e-228 1 788 168 959
QDV74336.1 4.63e-203 1 806 226 1030

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FJS_A 2.10e-24 446 703 514 753
Bacterialbeta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5FJS_B Bacterial beta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5O0S_A Crystal structure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with unreacted beta Cyclophellitol Cyclosulfate probe ME711 [Thermoanaerobacterium xylanolyticum LX-11]
5BVU_A 2.14e-24 446 703 518 757
Crystalstructure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],5BX2_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with 2-deoxy-2-fluoroglucoside [Thermoanaerobacterium xylanolyticum LX-11],5BX3_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with deoxynojirimycin [Thermoanaerobacterium xylanolyticum LX-11],5BX4_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with Glucoimidazole [Thermoanaerobacterium xylanolyticum LX-11],5BX5_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with glucose [Thermoanaerobacterium xylanolyticum LX-11],5NCX_A Crystal structure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase with an covalent inhibitor [Thermoanaerobacterium xylanolyticum LX-11],5OST_A Beta-glucosidase from Thermoanaerobacterium xylolyticum GH116 in complex with Gluco-1H-imidazole [Thermoanaerobacterium xylanolyticum LX-11]
5NPF_A 2.14e-24 446 703 517 756
Crystalstructure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with beta Cyclophellitol Cyclosulfate probe ME594 [Thermoanaerobacterium xylanolyticum]
7DKS_A 2.14e-24 446 703 518 757
ChainA, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKT_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKU_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKV_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11]
7DKW_A 2.14e-24 446 703 518 757
ChainA, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKW_B Chain B, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKX_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKY_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
K0E4E1 1.35e-24 74 216 319 461
Putative glycosyl hydrolase ecdE OS=Aspergillus rugulosus OX=41736 GN=ecdE PE=3 SV=1
Q7KT91 3.41e-13 491 691 710 898
Non-lysosomal glucosylceramidase OS=Drosophila melanogaster OX=7227 GN=CG33090 PE=1 SV=1
Q69ZF3 3.93e-12 446 690 610 838
Non-lysosomal glucosylceramidase OS=Mus musculus OX=10090 GN=Gba2 PE=1 SV=2
Q9HCG7 6.83e-12 446 690 619 847
Non-lysosomal glucosylceramidase OS=Homo sapiens OX=9606 GN=GBA2 PE=1 SV=2
Q5M868 6.04e-11 446 690 610 838
Non-lysosomal glucosylceramidase OS=Rattus norvegicus OX=10116 GN=Gba2 PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000061 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003444_00117.