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CAZyme Information: MGYG000001622_02851

You are here: Home > Sequence: MGYG000001622_02851

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 Enterocloster sp900549235
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster sp900549235
CAZyme ID MGYG000001622_02851
CAZy Family PL11
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
689 MGYG000001622_27|CGC1 78733.59 4.9577
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001622 3555335 MAG China Asia
Gene Location Start: 27871;  End: 29940  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001622_02851.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL11 433 676 2.7e-17 0.4141914191419142

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10318 RGL11 5.79e-11 271 645 117 527
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AGC68608.1 4.49e-217 1 674 1 663
ANW98952.1 4.49e-217 1 674 1 663
ANX01481.1 4.49e-217 1 674 1 663
AGI39619.1 4.49e-217 1 674 1 663
ADQ05930.1 1.89e-207 1 676 1 666

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Z8R_A 1.18e-06 271 645 120 529
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 1.59e-06 271 645 124 550
Crystalstructure of exotype rhamnogalacturonan lyase YesX [Bacillus subtilis]
4CAG_A 8.12e-06 271 648 127 539
Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31526 6.59e-06 271 645 157 566
Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 SV=1
O31527 8.63e-06 271 645 124 550
Rhamnogalacturonan exolyase YesX OS=Bacillus subtilis (strain 168) OX=224308 GN=yesX 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
1.000032 0.000011 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001622_02851.