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CAZyme Information: MGYG000001681_01388

You are here: Home > Sequence: MGYG000001681_01388

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 sp900761275
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900761275
CAZyme ID MGYG000001681_01388
CAZy Family PL11
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
818 90734.39 4.5773
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001681 2557345 MAG United States North America
Gene Location Start: 4199;  End: 6655  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001681_01388.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL11 1 223 1.5e-73 0.36633663366336633
CE12 603 811 2.2e-63 0.9904761904761905
CBM35 469 576 7.4e-17 0.8739495798319328

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10318 RGL11 7.10e-74 1 202 363 564
Rhamnogalacturonan lyase of the polysaccharide lyase family 11. The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
cd01821 Rhamnogalacturan_acetylesterase_like 1.79e-64 602 812 1 198
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
cd04082 CBM35_pectate_lyase-like 1.06e-49 457 576 5 124
Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.
COG2755 TesA 1.44e-19 601 816 8 212
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229 SGNH_hydrolase 1.67e-11 604 810 1 186
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL17979.1 1.67e-157 384 817 557 988
QNU65479.1 1.72e-125 1 814 387 1018
ADU21778.1 1.04e-108 1 377 402 777
AEY65185.1 1.73e-105 1 442 393 822
ADL50774.1 4.99e-100 1 407 395 796

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4CAG_A 5.84e-45 1 216 373 587
Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]
2Z8R_A 1.99e-40 1 214 366 576
Crystalstructure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8R_B Crystal structure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8S_A Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2Z8S_B Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2ZUX_A Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis],2ZUX_B Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis]
2ZUY_A 1.64e-39 1 218 370 603
Crystalstructure of exotype rhamnogalacturonan lyase YesX [Bacillus subtilis]
2W47_A 2.46e-27 457 576 9 128
ChainA, Lipolytic Enzyme, G-d-s-l [Acetivibrio thermocellus]
2W1W_A 2.61e-27 457 576 9 128
ChainA, LIPOLYTIC ENZYME, G-D-S-L [Acetivibrio thermocellus],2W1W_B Chain B, LIPOLYTIC ENZYME, G-D-S-L [Acetivibrio thermocellus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31528 5.33e-49 604 817 5 207
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
O31526 1.52e-39 1 214 403 613
Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 SV=1
O31527 8.22e-39 1 218 370 603
Rhamnogalacturonan exolyase YesX OS=Bacillus subtilis (strain 168) OX=224308 GN=yesX PE=1 SV=1
O31523 9.02e-29 604 817 8 217
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
P42304 1.16e-18 597 817 173 379
Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2

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
1.000055 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001681_01388.