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CAZyme Information: MGYG000000224_01055

You are here: Home > Sequence: MGYG000000224_01055

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 Bacteroides sp003545565
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp003545565
CAZyme ID MGYG000000224_01055
CAZy Family PL8
CAZyme Description Chondroitin sulfate ABC exolyase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
966 107742.33 8.2885
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000224 3747034 Isolate China Asia
Gene Location Start: 237206;  End: 240106  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000224_01055.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL8 577 822 5.1e-95 0.9919028340080972

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01083 GAG_Lyase 8.61e-125 273 902 54 693
Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of secreted bacterial lyase enzymes capable of acting on glycosaminoglycans, such as hyaluronan and chondroitin, in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen. These are broad-specificity glycosaminoglycan lyases which recognize uronyl residues in polysaccharides and cleave their glycosidic bonds via a beta-elimination reaction to form a double bond between C-4 and C-5 of the non-reducing terminal uronyl residues of released products. Substrates include chondroitin, chondroitin 4-sulfate, chondroitin 6-sulfate, and hyaluronic acid. Family members include chondroitin AC lyase, chondroitin abc lyase, xanthan lyase, and hyalurate lyase.
pfam09093 Lyase_catalyt 6.02e-121 204 548 1 361
Lyase, catalytic. Members of this family are predominantly found in chondroitin ABC lyase I, and adopt a helical structure, with fifteen alpha-helices which are at least two turns long and several short helical turns. The bulk of the domain is formed by ten alpha-helices forming five hairpin-like pairs and arranged into an incomplete toroid, the (alpha/alpha)5 fold. Additionally, two long and two short alpha-helices at the N-terminus of the domain wrap around the toroid. At the C-terminal end of the toroid there is one additional short alpha-helix. This domain is required for degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucoronosyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
pfam09092 Lyase_N 8.88e-55 20 177 3 165
Lyase, N terminal. Members of this family are predominantly found in chondroitin ABC lyase I, and adopt a jelly-roll fold topology consisting of a two-layered bent beta-sheet sandwich with one short alpha-helix. The convex beta sheet is composed of five antiparallel strands, whilst the concave beta-sheet contains five antiparallel beta-strands with a loop between two consecutive strands folding back onto the concave surface. This domain is required for binding of the protein to long glycosaminoglycan chains.
pfam02278 Lyase_8 1.25e-37 577 823 11 248
Polysaccharide lyase family 8, super-sandwich domain. This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDM10823.1 0.0 14 965 15 951
QUT78860.1 0.0 14 965 15 951
QDH53841.1 0.0 14 965 15 951
QRM99235.1 0.0 14 965 15 951
CBK67690.1 0.0 14 965 15 951

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1HN0_A 1.18e-125 16 964 36 1017
CRYSTALSTRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION [Proteus vulgaris]
7EIP_A 1.65e-125 16 964 36 1017
ChainA, Chondroitin sulfate ABC endolyase [Proteus vulgaris],7EIQ_A Chain A, Chondroitin sulfate ABC endolyase [Proteus vulgaris],7EIR_A Chain A, Chondroitin sulfate ABC endolyase [Proteus vulgaris],7EIS_A Chain A, Chondroitin sulfate ABC endolyase [Proteus vulgaris]
2Q1F_A 1.89e-117 6 966 2 1014
Crystalstructure of chondroitin sulfate lyase abc from bacteroides thetaiotaomicron wal2926 [Bacteroides thetaiotaomicron],2Q1F_B Crystal structure of chondroitin sulfate lyase abc from bacteroides thetaiotaomicron wal2926 [Bacteroides thetaiotaomicron]
2E24_A 2.13e-11 555 902 353 697
ChainA, Xanthan lyase [Bacillus sp. GL1]
1J0M_A 8.37e-11 555 902 353 697
CrystalStructure of Bacillus sp. GL1 Xanthan Lyase that Acts on Side Chains of Xanthan [Bacillus sp. GL1],1J0N_A Crystal Structure of Bacillus sp. GL1 Xanthan Lyase that Acts on Side Chains of Xanthan [Bacillus sp. GL1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8A2I1 2.79e-126 5 966 1 1014
Chondroitin sulfate ABC exolyase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=chonabc PE=1 SV=1
C5G6D7 1.06e-125 5 966 1 1014
Chondroitin sulfate ABC exolyase OS=Bacteroides thetaiotaomicron OX=818 GN=chonabc PE=1 SV=2
P59807 9.03e-125 16 964 36 1017
Chondroitin sulfate ABC endolyase OS=Proteus vulgaris OX=585 PE=1 SV=2
C7S340 6.39e-100 24 942 15 966
Chondroitin sulfate ABC exolyase (Fragment) OS=Proteus vulgaris OX=585 GN=ChABCII PE=1 SV=1
Q9AQS0 5.08e-10 555 902 378 722
Xanthan lyase OS=Bacillus sp. (strain GL1) OX=84635 GN=xly 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
0.000422 0.998659 0.000329 0.000198 0.000180 0.000163

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000224_01055.