logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003233_01713

You are here: Home > Sequence: MGYG000003233_01713

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 pleomorphus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Sodaliphilus; Sodaliphilus pleomorphus
CAZyme ID MGYG000003233_01713
CAZy Family GH9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
836 MGYG000003233_171|CGC1 94142.41 7.0529
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003233 2919315 MAG United States North America
Gene Location Start: 37449;  End: 39959  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003233_01713.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH9 114 589 2e-74 0.9952153110047847

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00759 Glyco_hydro_9 7.72e-59 117 588 2 374
Glycosyl hydrolase family 9.
pfam02927 CelD_N 1.32e-31 22 104 1 83
Cellulase N-terminal ig-like domain.
cd02850 E_set_Cellulase_N 7.57e-29 23 109 1 86
N-terminal Early set domain associated with the catalytic domain of cellulase. E or "early" set domains are associated with the catalytic domain of cellulases at the N-terminal end. Cellulases are O-glycosyl hydrolases (GHs) that hydrolyze beta 1-4 glucosidic bonds in cellulose. They are usually categorized into either exoglucanases, which sequentially release terminal sugar units from the cellulose chain, or endoglucanases, which also attack the chain internally. The N-terminal domain of cellulase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.
cd10917 CE4_NodB_like_6s_7s 8.46e-22 637 821 17 171
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.
COG0726 CDA1 1.08e-19 583 833 23 256
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
QUT35459.1 0.0 7 836 8 836
QPH59586.1 0.0 7 836 8 836
QUT66756.1 0.0 7 836 8 836
QUT98069.1 0.0 7 836 8 836
QQA29127.1 0.0 7 836 8 836

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3X17_A 3.78e-39 21 591 15 556
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 1.48e-27 32 611 2 553
Crystalstructure of Zn-binding triple mutant of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4]
5U0H_A 3.28e-24 32 611 2 553
Crystalstructure of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4]
6DHT_A 4.03e-23 24 584 18 557
Bacteroidesovatus GH9 Bacova_02649 [Bacteroides ovatus ATCC 8483]
4CJ0_A 3.46e-21 22 380 28 369
ChainA, ENDOGLUCANASE D [Acetivibrio thermocellus],4CJ1_A Chain A, ENDOGLUCANASE D [Acetivibrio thermocellus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A7LXT3 2.41e-22 24 584 32 571
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
P0C2S4 1.90e-20 22 380 28 369
Endoglucanase D (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celD PE=1 SV=1
A3DDN1 2.04e-20 22 380 52 393
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
P14090 4.68e-20 21 597 338 913
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
Q05156 4.01e-19 21 595 182 746
Cellulase 1 OS=Streptomyces reticuli OX=1926 GN=cel1 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
0.489420 0.472163 0.035385 0.001236 0.000600 0.001185

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003233_01713.