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CAZyme Information: MGYG000000424_01949

You are here: Home > Sequence: MGYG000000424_01949

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-353 sp900768995
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; CAG-353; CAG-353 sp900768995
CAZyme ID MGYG000000424_01949
CAZy Family GH113
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
327 37912.67 4.9923
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000424 2854163 MAG Sweden Europe
Gene Location Start: 19117;  End: 20100  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.78

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH113 3 320 1.3e-106 0.9901960784313726

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd19608 GH113_mannanase-like 2.67e-109 1 324 1 310
Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins. Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences.
cd19606 GH113-like 1.11e-87 3 324 2 303
Glycoside hydrolase family 113 beta-mannosidase and similar proteins. Family 113 glycoside hydrolases cleave (1->4)-beta-glycosidic linkages, such as endo-1,4-beta-mannanase. This family also includes TIM-barrel domains found in gene transfer agent proteins.
cd19607 GTA_TIM-barrel-like 0.001 57 283 68 366
Putative glycoside hydrolase TIM-barrel domain in gene transfer agent and similar proteins. This domain is found in the gene transfer agent protein, such as the Rhodobacter capsulatus putative gene transfer agent protein encoded by orfg15. In the purple nonsulfur bacterium Rhodobacter capsulatus, DNA transmission is mediated via an unusual system, a small bacteriophage-like particle called the gene transfer agent (GTA) that transfers random 4.5-kb segments of the producing cell's genome to recipient cells, where allelic replacement occurs.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ABX41272.1 3.90e-138 1 324 1 319
QNF27001.1 7.32e-132 3 324 6 317
AOZ92031.1 2.50e-130 3 324 7 320
AIQ18672.1 3.01e-128 3 324 6 317
AIQ53005.1 8.59e-128 3 324 6 317

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4CD6_A 1.22e-79 3 320 13 310
Thestructure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG [Alicyclobacillus acidocaldarius],4CD7_A The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose [Alicyclobacillus acidocaldarius],4CD7_B The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose [Alicyclobacillus acidocaldarius],4CD8_A The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManMIm [Alicyclobacillus acidocaldarius]
3CIV_A 2.47e-79 3 320 36 333
Crystalstructure of the endo-beta-1,4-mannanase from Alicyclobacillus acidocaldarius [Alicyclobacillus acidocaldarius]
7DV7_A 7.28e-77 3 326 38 342
ChainA, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DV7_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5]
7DVZ_A 7.28e-77 3 326 38 342
ChainA, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DVZ_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DW8_A Chain A, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DW8_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DWA_A Chain A, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DWA_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5]
7DVJ_A 5.80e-76 3 326 38 342
ChainA, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DVJ_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000044 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000424_01949.