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CAZyme Information: MGYG000000583_02193

You are here: Home > Sequence: MGYG000000583_02193

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 Acetatifactor sp900766575
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900766575
CAZyme ID MGYG000000583_02193
CAZy Family CBM61
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1430 152518.97 4.1673
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000583 2865631 MAG Madagascar Africa
Gene Location Start: 3709;  End: 8001  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.89

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH53 443 822 9.1e-119 0.9970760233918129
CBM61 914 1053 4.3e-28 0.9858156028368794
CBM61 201 339 9.6e-17 0.9858156028368794

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3867 GanB 4.63e-131 426 834 23 403
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
pfam07745 Glyco_hydro_53 4.73e-119 443 822 1 333
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.
cd00118 LysM 2.74e-07 1386 1429 3 45
Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
pfam07532 Big_4 4.59e-06 838 895 1 56
Bacterial Ig-like domain (group 4). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
TIGR02899 spore_safA 6.65e-06 1388 1429 1 42
spore coat assembly protein SafA. SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNM03783.1 0.0 4 1430 3 1357
CBK73963.1 7.17e-250 198 1062 41 852
ADL34775.1 1.20e-222 426 1055 245 874
SQI62631.1 2.33e-195 243 1062 82 815
QGH37103.1 7.11e-195 363 1060 100 795

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1R8L_A 5.65e-143 419 828 1 394
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 4.17e-142 419 828 1 394
ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis]
7OSK_A 7.46e-73 430 834 38 403
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 1.76e-40 445 751 6 301
Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Humicola insolens]
1HJS_A 1.26e-38 445 751 6 301
Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_A Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O07013 5.85e-144 411 828 21 423
Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1
Q65CX5 1.93e-142 418 828 25 419
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 4.66e-47 440 752 4 314
Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1
P48841 2.54e-42 442 751 27 330
Arabinogalactan endo-beta-1,4-galactanase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=ganB PE=1 SV=1
A1D3T4 2.43e-41 445 751 27 324
Probable arabinogalactan endo-beta-1,4-galactanase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=galA PE=3 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
0.003204 0.887381 0.108156 0.000595 0.000342 0.000282

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000583_02193.