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CAZyme Information: MGYG000003431_01742

You are here: Home > Sequence: MGYG000003431_01742

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; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; HUN007;
CAZyme ID MGYG000003431_01742
CAZy Family GH53
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
468 52543.56 4.2785
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003431 2512610 MAG Fiji Oceania
Gene Location Start: 6;  End: 1412  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.89

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH53 1 229 1.4e-61 0.6052631578947368

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3867 GanB 8.60e-74 1 234 174 396
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
pfam07745 Glyco_hydro_53 1.04e-63 1 229 128 333
Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.
cd14256 Dockerin_I 5.03e-13 412 467 1 56
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
cd14253 Dockerin 2.68e-09 413 467 1 55
Dockerin repeat domain. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.
pfam00404 Dockerin_1 4.81e-09 413 464 1 52
Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCE04670.1 3.33e-84 1 232 184 416
BCE17102.1 3.33e-84 1 232 184 416
BCE10872.1 3.33e-84 1 232 184 416
AUZ40547.1 9.32e-84 1 232 184 416
QII51300.1 1.31e-83 1 232 184 416

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1R8L_A 1.01e-83 1 232 159 391
Thestructure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1R8L_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1UR0_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR0_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],2CCR_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2CCR_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis]
2GFT_A 7.94e-83 1 232 159 391
ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis]
7OSK_A 6.21e-32 1 245 185 407
ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230]
1HJQ_A 3.36e-15 1 232 129 332
Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Humicola insolens]
1FHL_A 8.30e-15 1 204 130 325
CrystalStructure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 293k [Aspergillus aculeatus],1FOB_A Crystal Structure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 100k [Aspergillus aculeatus],6Q3R_A ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus],6Q3R_B ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O07013 3.35e-83 1 234 188 422
Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1
Q65CX5 1.14e-82 1 232 184 416
Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1
P48843 6.33e-25 1 226 133 364
Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1
Q9Y7F8 1.53e-15 1 173 146 321
Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus tubingensis OX=5068 GN=galA PE=2 SV=1
P83691 1.84e-14 1 232 129 332
Arabinogalactan endo-beta-1,4-galactanase OS=Humicola insolens OX=34413 PE=1 SV=1

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
1.000074 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003431_01742.