logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004281_02505

You are here: Home > Sequence: MGYG000004281_02505

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 Parabacteroides sp900552465
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900552465
CAZyme ID MGYG000004281_02505
CAZy Family PL8
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
923 MGYG000004281_33|CGC1 104624.91 5.3847
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004281 4813571 MAG China Asia
Gene Location Start: 23518;  End: 26289  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004281_02505.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL8 367 616 2.1e-65 0.9884169884169884
CBM9 734 902 1.3e-17 0.8956043956043956

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01083 GAG_Lyase 2.16e-148 60 688 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.
pfam02278 Lyase_8 3.66e-87 367 616 1 252
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.
pfam08124 Lyase_8_N 3.28e-30 91 344 43 313
Polysaccharide lyase family 8, N terminal alpha-helical 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.
cd09620 CBM9_like_3 3.90e-14 734 914 1 197
DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.
cd09622 CBM9_like_HisKa 1.51e-05 727 814 59 146
DOMON-like type 9 carbohydrate binding module at the N-terminus of bacterial sensor histidine kinases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this family are located at the N-terminus of bacterial sensor histidine kinases and may constitute or contribute to the ligand-binding moiety.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT47778.1 0.0 1 897 1 897
QDO71119.1 2.96e-271 3 720 4 721
QCT78112.1 4.46e-268 5 677 2 659
CAH07300.1 4.46e-268 5 677 2 659
ANQ60073.1 4.46e-268 5 677 2 659

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1CB8_A 4.52e-87 77 720 23 677
CHONDROITINASEAC LYASE FROM FLAVOBACTERIUM HEPARINUM [Pedobacter heparinus]
1HM2_A 7.46e-87 77 720 45 699
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]
1RWA_A 2.90e-36 156 699 124 714
Crystalstructure of Arthrobacter aurescens chondroitin AC lyase [Paenarthrobacter aurescens],1RWC_A Crystal structure of Arthrobacter aurescens chondroitin AC lyase [Paenarthrobacter aurescens],1RWF_A Crystal structure of Arthrobacter aurescens chondroitin AC lyase in complex with chondroitin tetrasaccharide [Paenarthrobacter aurescens],1RWG_A Crystal structure of Arthrobacter aurescens chondroitin AC lyase in complex with chondroitin tetrasaccharide [Paenarthrobacter aurescens],1RWH_A Crystal structure of Arthrobacter aurescens chondroitin AC lyase in complex with chondroitin tetrasaccharide [Paenarthrobacter aurescens]
1RW9_A 2.90e-36 156 699 124 714
Crystalstructure of the Arthrobacter aurescens chondroitin AC lyase [Paenarthrobacter aurescens]
2WCO_A 1.19e-29 156 642 139 668
Structuresof the Streptomyces coelicolor A3(2) Hyaluronan Lyase in Complex with Oligosaccharide Substrates and an Inhibitor [Streptomyces coelicolor A3(2)],2WDA_A The X-ray structure of the Streptomyces coelicolor A3 Chondroitin AC Lyase in Complex with Chondroitin sulphate [Streptomyces violaceoruber]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q59288 4.08e-86 77 720 45 699
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
Q59801 2.80e-24 156 700 182 782
Hyaluronate lyase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=hysA PE=3 SV=1
Q9AQS0 1.32e-23 81 639 53 673
Xanthan lyase OS=Bacillus sp. (strain GL1) OX=84635 GN=xly PE=1 SV=1
Q53591 2.17e-17 85 682 291 967
Hyaluronate lyase OS=Streptococcus agalactiae serotype III (strain NEM316) OX=211110 GN=hylB PE=1 SV=2
Q8A2I1 1.26e-10 376 680 606 922
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

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
0.000350 0.998871 0.000224 0.000188 0.000187 0.000162

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004281_02505.