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CAZyme Information: MGYG000001000_00650

You are here: Home > Sequence: MGYG000001000_00650

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 UBA4716 sp900556575
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; UBA4716; UBA4716 sp900556575
CAZyme ID MGYG000001000_00650
CAZy Family GH53
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
869 MGYG000001000_61|CGC1 95399.92 4.533
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001000 2124642 MAG China Asia
Gene Location Start: 3253;  End: 5862  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001000_00650.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH53 328 689 1.7e-78 0.9824561403508771

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07745 Glyco_hydro_53 7.72e-69 328 693 2 333
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.
COG3867 GanB 1.97e-66 326 700 39 398
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
NF033679 DNRLRE_dom 2.73e-04 58 185 28 163
DNRLRE domain. The DNRLRE domain, with a length of about 160 amino acids, appears typically in large, repetitive surface proteins of bacteria and archaea, sometimes repeated several times. It occurs, notably, three times in the C-terminal region of the enzyme disaggregatase from the archaeal species Methanosarcina mazei, each time with the motif DNRLRE, for which the domain is named. Archaeal proteins within this family are described particularly well by the currently more narrowly defined Pfam model, PF06848. Note that the catalytic region of disaggregatase, in the N-terminal portion of the protein, is modeled by a different HMM, PF08480.
cd19608 GH113_mannanase-like 0.004 543 590 177 231
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNU65257.1 1.06e-126 100 697 31 650
AGI39701.1 2.22e-123 55 742 224 902
AGC68692.1 2.22e-123 55 742 224 902
ANW99026.1 3.05e-123 55 742 224 902
ANX01554.1 1.07e-122 55 742 224 902

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7OSK_A 2.93e-41 324 694 48 392
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]
1R8L_A 4.15e-37 314 700 12 395
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 2.55e-36 314 700 12 395
ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis]
1HJQ_A 3.87e-36 328 653 5 303
Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Humicola insolens]
1HJS_A 8.81e-32 328 653 5 303
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
Q65CX5 1.09e-36 297 700 15 420
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
P83691 2.12e-35 328 653 5 303
Arabinogalactan endo-beta-1,4-galactanase OS=Humicola insolens OX=34413 PE=1 SV=1
O07013 3.29e-35 299 695 26 419
Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1
Q0CTQ7 4.49e-32 328 648 19 314
Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=galA PE=3 SV=1
Q8X168 6.20e-32 328 681 21 348
Arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus niger OX=5061 GN=galA 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
0.002674 0.995445 0.000443 0.000530 0.000434 0.000415

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001000_00650.