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CAZyme Information: MGYG000004813_01738

You are here: Home > Sequence: MGYG000004813_01738

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 Proteus sp003144505
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Proteus; Proteus sp003144505
CAZyme ID MGYG000004813_01738
CAZy Family PL8
CAZyme Description Chondroitin sulfate ABC exolyase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1013 113737.58 6.7305
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004813 3063039 MAG China Asia
Gene Location Start: 849;  End: 3890  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.20

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL8 613 856 6.1e-91 0.979757085020243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01083 GAG_Lyase 1.54e-109 323 930 76 693
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 3.21e-72 229 580 10 359
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 1.40e-40 35 190 4 166
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 2.14e-21 594 856 5 247
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.
pfam02884 Lyase_8_C 1.01e-04 871 930 1 59
Polysaccharide lyase family 8, C-terminal beta-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
QKJ48878.1 0.0 1 1013 1 1013
QHN11504.1 0.0 1 1013 1 1013
QIF94996.1 0.0 1 1013 1 1013
QQP26445.1 0.0 1 1013 1 1013
QPB80438.1 0.0 1 1013 1 1013

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Q1F_A 1.35e-137 39 997 27 998
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]
1HN0_A 9.80e-95 8 1000 8 1006
CRYSTALSTRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION [Proteus vulgaris]
7EIP_A 1.35e-94 8 1000 8 1006
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]
6F2P_A 2.09e-07 628 930 391 696
Structureof Paenibacillus xanthan lyase to 2.6 A resolution [Paenibacillus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
C7S340 0.0 24 1013 1 990
Chondroitin sulfate ABC exolyase (Fragment) OS=Proteus vulgaris OX=585 GN=ChABCII PE=1 SV=1
Q8A2I1 3.56e-149 35 997 22 998
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 2.82e-147 35 997 22 998
Chondroitin sulfate ABC exolyase OS=Bacteroides thetaiotaomicron OX=818 GN=chonabc PE=1 SV=2
P59807 7.39e-94 8 1000 8 1006
Chondroitin sulfate ABC endolyase OS=Proteus vulgaris OX=585 PE=1 SV=2

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
0.000535 0.998486 0.000430 0.000192 0.000163 0.000152

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004813_01738.