logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004892_00283

You are here: Home > Sequence: MGYG000004892_00283

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1858;
CAZyme ID MGYG000004892_00283
CAZy Family CE2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1387 151005.52 4.2721
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004892 1550618 MAG China Asia
Gene Location Start: 334;  End: 4497  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.1.1.72 3.1.1.- 3.2.1.4

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE2 804 1010 1.8e-44 0.9952153110047847
CE2 161 367 4.6e-42 0.9952153110047847

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01831 Endoglucanase_E_like 3.29e-28 161 367 1 168
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
cd01831 Endoglucanase_E_like 3.29e-27 804 1010 1 168
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
pfam17996 CE2_N 2.33e-20 43 152 3 106
Carbohydrate esterase 2 N-terminal. This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyses the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.
pfam17996 CE2_N 6.36e-17 686 795 3 106
Carbohydrate esterase 2 N-terminal. This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyses the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.
cd14256 Dockerin_I 1.39e-12 1317 1371 1 54
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL33310.1 4.28e-35 680 1016 12 357
CQR54111.1 3.41e-34 686 1016 19 356
CBK96966.1 6.53e-34 680 1016 12 357
AIQ28226.1 1.15e-33 681 1016 16 356
AIQ38796.1 1.09e-31 686 1016 19 356

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WAO_A 4.51e-23 699 1016 29 333
ChainA, ENDOGLUCANASE E [Acetivibrio thermocellus]
2WAB_A 1.10e-22 699 1016 29 333
ChainA, ENDOGLUCANASE E [Acetivibrio thermocellus]
3U37_A 1.75e-20 803 1016 166 406
AnAcetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_B An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_C An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_D An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_E An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_F An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_G An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_H An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316]
4DEV_A 3.22e-19 803 1016 166 406
AnAcetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_B An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_C An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_D An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_E An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_F An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_G An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_H An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316]
4XVH_A 7.42e-18 690 1016 8 329
Crystalstructure of a Corynascus thermopiles (Myceliophthora fergusii) carbohydrate esterase family 2 (CE2) enzyme plus carbohydrate binding domain (CBD) [Chaetomium]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P10477 5.49e-21 699 1016 510 814
Cellulase/esterase CelE OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celE PE=1 SV=2
B3PDE5 1.58e-09 744 1015 87 358
Acetylxylan esterase / glucomannan deacetylase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=ce2C PE=1 SV=1
A0A3R0A696 1.30e-06 492 670 819 999
Alpha-L-arabinofuranosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=blArafA 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
0.141314 0.852531 0.004789 0.000551 0.000370 0.000426

TMHMM  Annotations      download full data without filtering help

start end
7 29