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CAZyme Information: MGYG000002476_01171

You are here: Home > Sequence: MGYG000002476_01171

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 Yersinia pestis
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia pestis
CAZyme ID MGYG000002476_01171
CAZy Family PL8
CAZyme Description Chondroitin sulfate ABC endolyase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1037 115044.45 6.5157
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002476 4935125 Isolate Russia Europe
Gene Location Start: 1131522;  End: 1134635  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.20

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL8 648 893 1.3e-98 0.9959514170040485

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01083 GAG_Lyase 0.0 296 976 3 693
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 3.64e-179 254 620 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 3.12e-62 46 242 1 167
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 3.85e-27 648 893 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.
cd07578 nitrilase_1_R1 0.008 435 571 49 162
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). Members of this subgroup have two nitrilase domains. This is the first of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AJK15948.1 0.0 1 1037 1 1037
VEB10047.1 0.0 1 1037 1 1037
AYX17192.1 0.0 1 1037 1 1037
AJJ69011.1 0.0 1 1037 1 1037
VEA95214.1 0.0 1 1037 1 1037

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1HN0_A 0.0 8 1036 5 1020
CRYSTALSTRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION [Proteus vulgaris]
7EIP_A 0.0 8 1036 5 1020
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 1.56e-73 52 1037 25 1016
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]
1CB8_A 1.07e-12 604 893 282 561
CHONDROITINASEAC LYASE FROM FLAVOBACTERIUM HEPARINUM [Pedobacter heparinus]
1HM2_A 1.10e-12 604 893 304 583
ACTIVESITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS [Pedobacter heparinus],1HM3_A Active Site Of Chondroitinase Ac Lyase Revealed By The Structure Of Enzyme-Oligosaccharide Complexes And Mutagenesis [Pedobacter heparinus],1HMU_A ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS [Pedobacter heparinus],1HMW_A Active Site Of Chondroitinase Ac Lyase Revealed By The Structure Of Enzyme-oligosaccharide Complexes And Mutagenesis [Pedobacter heparinus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P59807 0.0 8 1036 5 1020
Chondroitin sulfate ABC endolyase OS=Proteus vulgaris OX=585 PE=1 SV=2
C7S340 6.05e-98 54 980 16 911
Chondroitin sulfate ABC exolyase (Fragment) OS=Proteus vulgaris OX=585 GN=ChABCII PE=1 SV=1
Q8A2I1 1.56e-81 49 1034 22 1013
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 2.13e-81 49 1034 22 1013
Chondroitin sulfate ABC exolyase OS=Bacteroides thetaiotaomicron OX=818 GN=chonabc PE=1 SV=2
Q59288 6.03e-12 604 893 304 583
Chondroitinase-AC OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) OX=485917 GN=cslA 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
0.225609 0.658432 0.108280 0.005611 0.001359 0.000685

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002476_01171.