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CAZyme Information: MGYG000000534_02145

You are here: Home > Sequence: MGYG000000534_02145

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 Prevotella sp900543975
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900543975
CAZyme ID MGYG000000534_02145
CAZy Family GH9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
845 95565.83 6.3953
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000534 3142227 MAG Fiji Oceania
Gene Location Start: 14178;  End: 16715  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000534_02145.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH9 118 591 1.3e-72 0.9880382775119617
CE4 623 755 1.4e-18 0.9230769230769231

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00759 Glyco_hydro_9 8.06e-63 126 591 7 372
Glycosyl hydrolase family 9.
cd10917 CE4_NodB_like_6s_7s 1.60e-29 627 825 1 171
Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.
cd10950 CE4_BsYlxY_like 1.84e-27 623 836 2 186
Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis putative polysaccharide deacetylase BsYlxY, encoded by the ylxY gene, which is a member of the carbohydrate esterase 4 (CE4) superfamily. Although its biological function still remains unknown, BsYlxY shows high sequence homology to the catalytic domain of Bacillus subtilis pdaB gene encoding a putative polysaccharide deacetylase (BsPdaB), which is essential for the maintenance of spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. However, disruption of the ylxY gene in B. subtilis did not cause any sporulation defect. Moreover, the Asp residue in the classical His-His-Asp zinc-binding motif of CE4 esterases is mutated to a Val residue in this family. Other catalytically relevant residues of CE4 esterases are also not conserved, which suggest that members of this family may be inactive.
cd10948 CE4_BsPdaA_like 1.00e-22 599 834 12 223
Catalytic NodB homology domain of Bacillus subtilis polysaccharide deacetylase PdaA, and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis pdaA gene encoding polysaccharide deacetylase BsPdaA, which is a member of the carbohydrate esterase 4 (CE4) superfamily. BsPdaA deacetylates peptidoglycan N-acetylmuramic acid (MurNAc) residues to facilitate the formation of muramic delta-lactam, which is required for recognition of germination lytic enzymes. BsPdaA deficiency leads to the absence of muramic delta-lactam residues in the spore cortex. Like other CE4 esterases, BsPdaA consists of a single catalytic NodB homology domain that appears to adopt a deformed (beta/alpha)8 barrel fold with a putative substrate binding groove harboring the majority of the conserved residues. It utilizes a general acid/base catalytic mechanism involving a tetrahedral transition intermediate, where a water molecule functions as the nucleophile tightly associated to the zinc cofactor.
cd10949 CE4_BsPdaB_like 5.69e-21 625 836 2 188
Putative catalytic NodB homology domain of Bacillus subtilis putative polysaccharide deacetylase PdaB, and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by the putative polysaccharide deacetylase PdaB encoded by the pdaB gene on sporulation of Bacillus subtilis. Although its biochemical properties remain to be determined, the PdaB (YbaN) protein is essential for maintaining spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. The glycans of the spore cortex may be candidate PdaB substrates. Based on sequence similarity, the family members are classified as carbohydrate esterase 4 (CE4) superfamily members. However, the classical His-His-Asp zinc-binding motif of CE4 esterases is missing in this family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUI47497.1 0.0 14 836 11 832
QCQ33880.1 0.0 14 836 11 832
QKH86859.1 0.0 14 836 11 832
QLK84487.1 0.0 14 836 11 832
QCQ47069.1 0.0 14 836 11 832

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3X17_A 3.95e-33 21 591 11 551
Crystalstructure of metagenome-derived glycoside hydrolase family 9 endoglucanase [uncultured bacterium],3X17_B Crystal structure of metagenome-derived glycoside hydrolase family 9 endoglucanase [uncultured bacterium]
5U2O_A 3.71e-20 36 596 2 539
Crystalstructure of Zn-binding triple mutant of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4]
6DHT_A 6.33e-20 28 514 18 497
Bacteroidesovatus GH9 Bacova_02649 [Bacteroides ovatus ATCC 8483]
4CJ0_A 2.16e-18 28 451 30 437
ChainA, ENDOGLUCANASE D [Acetivibrio thermocellus],4CJ1_A Chain A, ENDOGLUCANASE D [Acetivibrio thermocellus]
1CLC_A 2.24e-18 28 451 44 451
ChainA, ENDOGLUCANASE CELD; EC: 3.2.1.4 [Acetivibrio thermocellus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P14090 1.03e-21 25 591 338 902
Endoglucanase C OS=Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) OX=590998 GN=cenC PE=1 SV=2
A7LXT3 1.21e-19 12 514 16 511
Xyloglucan-specific endo-beta-1,4-glucanase BoGH9A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02649 PE=1 SV=1
P0C2S4 1.18e-17 28 451 30 437
Endoglucanase D (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celD PE=1 SV=1
A3DDN1 1.25e-17 28 451 54 461
Endoglucanase D OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celD PE=1 SV=1
Q05156 1.96e-17 19 589 176 735
Cellulase 1 OS=Streptomyces reticuli OX=1926 GN=cel1 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
0.000301 0.999023 0.000170 0.000178 0.000159 0.000144

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000534_02145.