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CAZyme Information: MGYG000003523_00529

You are here: Home > Sequence: MGYG000003523_00529

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 CAG-475 sp900769205
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-917; CAG-475; CAG-475 sp900769205
CAZyme ID MGYG000003523_00529
CAZy Family GH110
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
901 MGYG000003523_90|CGC1 98317.58 4.3549
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003523 1093650 MAG Fiji Oceania
Gene Location Start: 169;  End: 2874  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003523_00529.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH110 98 636 5.2e-90 0.9981751824817519

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13229 Beta_helix 1.04e-06 495 666 2 133
Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.
cd00241 DOMON_like 3.01e-06 732 873 23 157
Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
cd09619 CBM9_like_4 1.32e-05 694 843 5 141
DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.
pfam05048 NosD 6.52e-05 478 653 49 202
Periplasmic copper-binding protein (NosD). NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain.
pfam06452 CBM9_1 6.45e-04 722 897 26 182
Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNK56674.1 2.89e-194 68 896 6 825
BBI31508.1 2.34e-45 129 616 52 537
QTH41675.1 3.74e-44 151 616 70 539
QJD86821.1 2.77e-41 143 616 64 540
AFL78386.1 1.22e-40 137 544 57 491

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7JW4_A 3.33e-33 95 638 24 597
Crystalstructure of PdGH110B in complex with D-galactose [Pseudoalteromonas distincta],7JW4_B Crystal structure of PdGH110B in complex with D-galactose [Pseudoalteromonas distincta]
7JWF_A 1.40e-32 95 638 24 597
Crystalstructure of PdGH110B D344N in complex with alpha-(1,3)-galactobiose [Pseudoalteromonas distincta],7JWF_B Crystal structure of PdGH110B D344N in complex with alpha-(1,3)-galactobiose [Pseudoalteromonas distincta],7JWF_C Crystal structure of PdGH110B D344N in complex with alpha-(1,3)-galactobiose [Pseudoalteromonas distincta],7JWF_D Crystal structure of PdGH110B D344N in complex with alpha-(1,3)-galactobiose [Pseudoalteromonas distincta]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A6LFT2 1.26e-34 102 544 29 498
Alpha-1,3-galactosidase B OS=Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152) OX=435591 GN=glaB PE=3 SV=1
A6L2M8 2.84e-33 169 544 104 495
Alpha-1,3-galactosidase B OS=Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC 11154) OX=435590 GN=glaB2 PE=3 SV=1
A6KWM0 1.45e-30 160 544 95 496
Alpha-1,3-galactosidase B OS=Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC 11154) OX=435590 GN=glaB1 PE=3 SV=1
Q64XV2 3.53e-30 96 544 24 499
Alpha-1,3-galactosidase B OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=glaB PE=3 SV=1
Q5LGZ8 1.48e-29 96 544 24 499
Alpha-1,3-galactosidase B OS=Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow) OX=272559 GN=glaB 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
0.001967 0.997095 0.000345 0.000191 0.000174 0.000171

TMHMM  Annotations      download full data without filtering help

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