Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; | |||||||||||
CAZyme ID | MGYG000004599_02123 | |||||||||||
CAZy Family | PL30 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 53; End: 2521 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL30 | 72 | 783 | 0 | 0.9957865168539326 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd01083 | GAG_Lyase | 5.28e-54 | 64 | 781 | 17 | 690 | 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 | 1.25e-53 | 428 | 714 | 2 | 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. |
pfam02884 | Lyase_8_C | 3.22e-12 | 725 | 787 | 1 | 62 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT37261.1 | 0.0 | 2 | 813 | 3 | 813 |
QQA29924.1 | 0.0 | 2 | 813 | 3 | 813 |
QUT61434.1 | 0.0 | 2 | 813 | 3 | 813 |
BBK86575.1 | 0.0 | 2 | 813 | 3 | 813 |
QUT65873.1 | 0.0 | 2 | 813 | 3 | 813 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1CB8_A | 1.25e-25 | 291 | 779 | 192 | 634 | CHONDROITINASEAC LYASE FROM FLAVOBACTERIUM HEPARINUM [Pedobacter heparinus] |
1HM2_A | 1.34e-25 | 291 | 779 | 214 | 656 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q59288 | 7.36e-25 | 291 | 779 | 214 | 656 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000733 | 0.674291 | 0.324195 | 0.000288 | 0.000248 | 0.000225 |
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