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CAZyme Information: MGYG000000959_01723
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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 | Ruminococcus sp900752785 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900752785 | |||||||||||
| CAZyme ID | MGYG000000959_01723 | |||||||||||
| CAZy Family | GH10 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 13406; End: 16213 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH10 | 100 | 425 | 1.9e-87 | 0.9933993399339934 |
| CBM22 | 554 | 679 | 3.3e-35 | 0.9618320610687023 |
| CE4 | 723 | 845 | 7.6e-23 | 0.8692307692307693 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam00331 | Glyco_hydro_10 | 2.05e-94 | 101 | 425 | 1 | 310 | Glycosyl hydrolase family 10. |
| smart00633 | Glyco_10 | 2.44e-87 | 140 | 423 | 1 | 263 | Glycosyl hydrolase family 10. |
| COG3693 | XynA | 1.44e-63 | 129 | 428 | 56 | 342 | Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]. |
| cd10954 | CE4_CtAXE_like | 1.66e-62 | 727 | 918 | 1 | 180 | Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases. |
| cd10917 | CE4_NodB_like_6s_7s | 3.40e-44 | 727 | 906 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CAL91982.1 | 3.84e-163 | 99 | 427 | 9 | 335 |
| CAA77476.1 | 1.71e-160 | 97 | 427 | 626 | 953 |
| AAS31752.1 | 1.71e-160 | 97 | 427 | 626 | 953 |
| CDG46726.1 | 1.23e-156 | 97 | 426 | 24 | 351 |
| AEQ16451.1 | 1.16e-148 | 97 | 427 | 15 | 344 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2W5F_A | 5.62e-97 | 2 | 426 | 103 | 527 | ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2W5F_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus] |
| 2WYS_A | 1.60e-94 | 2 | 426 | 103 | 527 | ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WYS_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WZE_A Chain A, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WZE_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus] |
| 6D5C_A | 8.54e-52 | 97 | 425 | 19 | 349 | Structureof Caldicellulosiruptor danielii GH10 module of glycoside hydrolase WP_045175321 [Caldicellulosiruptor danielii],6D5C_B Structure of Caldicellulosiruptor danielii GH10 module of glycoside hydrolase WP_045175321 [Caldicellulosiruptor danielii],6D5C_C Structure of Caldicellulosiruptor danielii GH10 module of glycoside hydrolase WP_045175321 [Caldicellulosiruptor danielii] |
| 6FHE_A | 1.19e-51 | 101 | 424 | 13 | 339 | Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct] |
| 5OFJ_A | 1.63e-51 | 100 | 427 | 10 | 339 | Crystalstructure of N-terminal domain of bifunctional CbXyn10C [Caldicellulosiruptor bescii DSM 6725] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P29126 | 3.42e-161 | 97 | 427 | 626 | 953 | Bifunctional endo-1,4-beta-xylanase XylA OS=Ruminococcus flavefaciens OX=1265 GN=xynA PE=3 SV=1 |
| P51584 | 1.21e-102 | 2 | 741 | 114 | 744 | Endo-1,4-beta-xylanase Y OS=Acetivibrio thermocellus OX=1515 GN=xynY PE=1 SV=1 |
| Q60037 | 1.39e-58 | 1 | 424 | 284 | 690 | Endo-1,4-beta-xylanase A OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=xynA PE=1 SV=1 |
| Q60042 | 2.55e-57 | 1 | 424 | 280 | 686 | Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1 |
| P26223 | 6.70e-51 | 100 | 429 | 2 | 340 | Endo-1,4-beta-xylanase B OS=Butyrivibrio fibrisolvens OX=831 GN=xynB PE=3 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 |
|---|---|---|---|---|---|
| 1.000030 | 0.000003 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |