dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003279_02133

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Basic Information help

Species

Alistipes sp900541585

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900541585

CAZyme ID

MGYG000003279_02133

CAZy Family

PL8

CAZyme Description

Chondroitin sulfate ABC endolyase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
983	MGYG000003279_17\|CGC7	109463.46	6.6273

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003279	3216844	MAG	United States	North America

Gene Location

Start: 582742; End: 585693 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003279_02133.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
PL8	592	841	4.3e-93	0.9959514170040485

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01083	GAG_Lyase	1.83e-121	229	918	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	1.19e-98	220	562	7	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	2.01e-40	32	189	5	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	2.02e-34	592	841	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
CBK63375.1	0.0	1	983	1	983
QRQ49161.1	1.53e-314	24	983	16	960
QUT44903.1	3.06e-314	24	983	16	960
QDM10823.1	1.88e-308	1	983	1	953
QUT78860.1	1.88e-308	1	983	1	953

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HN0_A	2.87e-132	13	980	13	1017	CRYSTALSTRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION [Proteus vulgaris]
7EIP_A	2.87e-132	13	980	13	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	5.21e-99	33	982	24	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]
6F2P_A	1.98e-09	655	914	434	694	Structureof Paenibacillus xanthan lyase to 2.6 A resolution [Paenibacillus]
1J0M_A	1.60e-06	715	918	481	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
P59807	1.57e-131	13	980	13	1017	Chondroitin sulfate ABC endolyase OS=Proteus vulgaris OX=585 PE=1 SV=2
C5G6D7	4.51e-107	33	982	24	1014	Chondroitin sulfate ABC exolyase OS=Bacteroides thetaiotaomicron OX=818 GN=chonabc PE=1 SV=2
Q8A2I1	1.63e-105	33	982	24	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
C7S340	4.94e-102	34	955	15	963	Chondroitin sulfate ABC exolyase (Fragment) OS=Proteus vulgaris OX=585 GN=ChABCII PE=1 SV=1
Q9AQS0	9.40e-06	715	918	506	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
0.000342	0.998958	0.000175	0.000185	0.000167	0.000158

TMHMM Annotations help

There is no transmembrane helices in MGYG000003279_02133.