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CAZyme Information: MGYG000004845_00277

You are here: Home > Sequence: MGYG000004845_00277

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; Monoglobales_A; UBA1381; UBA4716;
CAZyme ID MGYG000004845_00277
CAZy Family PL11
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
972 MGYG000004845_1|CGC3 107320.19 4.0599
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004845 2789282 MAG Sweden Europe
Gene Location Start: 285088;  End: 288006  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004845_00277.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL11 59 649 1.2e-231 0.9948542024013722
CBM32 855 967 2.7e-19 0.8709677419354839

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10318 RGL11 0.0 60 634 1 564
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.
pfam07833 Cu_amine_oxidN1 1.61e-32 709 800 1 92
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam18370 RGI_lyase 4.60e-30 58 142 1 86
Rhamnogalacturonan I lyases beta-sheet domain. This is the beta-sheet domain found in rhamnogalacturonan (RG) lyases, which are responsible for an initial cleavage of the RG type I (RG-I) region of plant cell wall pectin. Polysaccharide lyase family 11 carrying this domain, such as YesW (EC:4.2.2.23) and YesX (EC:4.2.2.24), cleave glycoside bonds between rhamnose and galacturonic acid residues in RG-I through a beta-elimination reaction. Other family members carrying this domain are hemagglutinin A, lysine gingipain (Kgp) and Chitinase C (EC:3.2.1.14).
pfam00754 F5_F8_type_C 1.37e-14 854 967 9 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam07833 Cu_amine_oxidN1 2.31e-08 678 739 38 93
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ARV97666.1 7.81e-208 58 649 34 612
ASB56148.1 7.81e-208 58 649 34 612
ARW01748.1 7.81e-208 58 649 34 612
AOL28430.1 7.81e-208 58 649 34 612
QGI20729.1 9.60e-208 58 649 40 618

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Z8R_A 4.11e-208 58 649 3 581
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]
4CAG_A 1.57e-203 58 649 9 588
Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]
2ZUY_A 4.50e-195 57 663 5 614
Crystalstructure of exotype rhamnogalacturonan lyase YesX [Bacillus subtilis]
5ZU6_A 2.09e-19 851 955 39 144
ACBM32 derived from alginate lyase B (AlyB-OU02) [Vibrio]
5ZU5_A 2.30e-17 851 955 39 144
Crystalstructure of a full length alginate lyase with CBM domain [Vibrio splendidus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31526 6.10e-207 58 649 40 618
Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 SV=1
O31527 3.75e-194 57 660 5 611
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000273 0.998968 0.000203 0.000181 0.000183 0.000161

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004845_00277.