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CAZyme Information: MGYG000001514_02476

You are here: Home > Sequence: MGYG000001514_02476

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 Paenibacillus_A ihumii
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
CAZyme ID MGYG000001514_02476
CAZy Family CBM9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
692 MGYG000001514_12|CGC17 76580.63 5.9046
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001514 5923787 Isolate not provided not provided
Gene Location Start: 997691;  End: 999769  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001514_02476.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM9 154 323 9.8e-46 0.9945054945054945
CE1 442 689 8.4e-32 0.9515418502202643

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00005 CBM9_like_1 1.87e-81 144 324 1 185
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.
pfam06452 CBM9_1 5.11e-58 154 324 1 182
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.
cd09619 CBM9_like_4 1.21e-23 152 319 2 187
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.
cd09618 CBM9_like_2 6.06e-14 150 298 9 177
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 subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints.
COG2382 Fes 1.06e-13 399 691 42 297
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ACL77751.1 0.0 2 691 3 691
AEY68182.1 0.0 4 691 2 686
QSF48012.1 0.0 62 691 2 630
QLG42560.1 6.74e-314 115 691 27 603
AFH62884.1 1.24e-311 124 692 52 619

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1GKL_A 5.70e-81 409 691 24 288
ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],1GKL_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],1WB4_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1WB4_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1WB5_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1WB5_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1WB6_A Chain A, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],1WB6_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus]
6FJ4_A 3.36e-77 409 691 10 274
ChainA, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus]
1GKK_A 5.23e-77 409 691 24 288
ChainA, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1GKK_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],3ZI7_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus YS],3ZI7_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus YS],4BAG_A Chain A, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],4BAG_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],4H35_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],4H35_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],5FXM_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],6Y8G_AAA Chain AAA, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],6Y8G_BBB Chain BBB, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus]
7NWN_AAA 1.14e-59 139 336 17 215
ChainAAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWO_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWP_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWQ_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B]
1I82_A 5.62e-39 147 323 5 187
Family9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Cellobiose [Thermotoga maritima],1I8A_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Glucose [Thermotoga maritima],1I8U_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P51584 1.06e-72 409 691 812 1076
Endo-1,4-beta-xylanase Y OS=Acetivibrio thermocellus OX=1515 GN=xynY PE=1 SV=1
P38535 1.00e-37 147 329 714 900
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
P36917 1.06e-37 147 329 862 1048
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
Q60042 1.24e-34 143 323 865 1053
Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1
Q60037 3.88e-34 143 323 869 1057
Endo-1,4-beta-xylanase A OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=xynA 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
0.000256 0.998951 0.000286 0.000175 0.000167 0.000143

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001514_02476.