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CAZyme Information: MGYG000004474_01140

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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 Sodaliphilus sp004557565
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Sodaliphilus; Sodaliphilus sp004557565
CAZyme ID MGYG000004474_01140
CAZy Family GH9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
842 MGYG000004474_23|CGC1 95094.15 6.4743
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004474 2861939 MAG Israel Asia
Gene Location Start: 25469;  End: 27997  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004474_01140.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH9 113 586 1.3e-71 0.9880382775119617
CE4 618 751 1.1e-17 0.9307692307692308

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00759 Glyco_hydro_9 2.02e-55 121 588 7 374
Glycosyl hydrolase family 9.
cd10917 CE4_NodB_like_6s_7s 4.14e-26 640 824 19 171
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, bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC, 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.
pfam02927 CelD_N 5.76e-26 21 103 1 83
Cellulase N-terminal ig-like domain.
cd10948 CE4_BsPdaA_like 2.88e-23 593 833 11 223
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.
COG0726 CDA1 4.92e-23 569 837 12 257
Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT66756.1 0.0 19 839 21 836
QUT98069.1 0.0 19 839 21 836
QUT35459.1 0.0 19 839 21 836
QPH59586.1 0.0 19 839 21 836
QBJ19309.1 0.0 19 839 21 836

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3X17_A 5.21e-39 23 591 18 556
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 8.55e-30 31 612 2 553
Crystalstructure of Zn-binding triple mutant of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4]
5U0H_A 1.98e-26 31 612 2 553
Crystalstructure of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4]
6DHT_A 6.92e-17 16 584 11 557
Bacteroidesovatus GH9 Bacova_02649 [Bacteroides ovatus ATCC 8483]
5O6Y_A 2.23e-16 617 836 16 207
Crystalstructure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P14090 2.66e-25 23 598 341 914
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
P23658 1.12e-22 23 589 4 543
Cellodextrinase OS=Butyrivibrio fibrisolvens OX=831 GN=ced1 PE=1 SV=1
A7LXT3 1.73e-16 11 584 20 571
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
Q05156 3.06e-16 23 595 185 746
Cellulase 1 OS=Streptomyces reticuli OX=1926 GN=cel1 PE=1 SV=1
Q04729 3.18e-15 591 837 34 254
Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

0.003301 0.994682 0.001249 0.000240 0.000233 0.000258

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004474_01140.