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CAZyme Information: MGYG000004164_01036

You are here: Home > Sequence: MGYG000004164_01036

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 UMGS1494 sp900552305
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; UMGS1494; UMGS1494 sp900552305
CAZyme ID MGYG000004164_01036
CAZy Family CBM9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1324 MGYG000004164_43|CGC1 146247 4.7034
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004164 2287505 MAG United Kingdom Europe
Gene Location Start: 4956;  End: 8930  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004164_01036.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM9 1178 1322 7.2e-25 0.8571428571428571

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09619 CBM9_like_4 1.09e-20 1157 1314 3 183
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.
pfam06452 CBM9_1 1.61e-20 1163 1323 7 182
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.
cd00005 CBM9_like_1 4.84e-17 1187 1323 43 185
DOMON-like type 9 carbohydrate binding module of xylanases. 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. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
cd09621 CBM9_like_5 7.11e-09 1177 1320 24 188
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 functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
cd00241 DOMON_like 7.86e-08 1171 1284 8 142
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ANE48490.1 1.91e-140 188 1311 37 1170
ANE48489.1 3.00e-101 183 1322 32 1112
QJC51548.1 2.52e-74 189 1322 40 1353
QWG03218.1 3.32e-63 189 898 26 739
AFY32698.1 3.51e-63 184 876 49 752

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6P2M_A 2.28e-58 183 874 4 690
ChainA, Type 3a cellulose-binding domain protein [Caldicellulosiruptor lactoaceticus 6A]
4LGN_A 2.62e-53 183 874 1 732
Thestructure of Acidothermus cellulolyticus family 74 glycoside hydrolase [Acidothermus cellulolyticus 11B]
2CN2_A 1.38e-50 197 874 20 728
ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_C Chain C, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_D Chain D, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]
2CN3_A 1.85e-50 197 874 20 728
ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN3_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]
2EBS_A 1.87e-48 189 879 4 764
ChainA, Oligoxyloglucan reducing end-specific cellobiohydrolase [Geotrichum sp. M128],2EBS_B Chain B, Oligoxyloglucan reducing end-specific cellobiohydrolase [Geotrichum sp. M128]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A3DFA0 5.34e-51 178 887 27 770
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xghA PE=3 SV=1
Q70DK5 5.34e-51 178 887 27 770
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
Q8J0D2 9.47e-48 178 879 15 787
Oligoxyloglucan reducing end-specific cellobiohydrolase OS=Geotrichum sp. (strain M128) OX=203496 PE=1 SV=1
Q3MUH7 1.51e-47 200 937 50 830
Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
Q5BD38 1.29e-38 189 874 35 805
Oligoxyloglucan-reducing end-specific xyloglucanase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xgcA 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
0.000276 0.998943 0.000271 0.000184 0.000174 0.000151

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004164_01036.