dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Fusobacterium_A sp900555845

Lineage

Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Fusobacterium_A; Fusobacterium_A sp900555845

CAZyme ID

MGYG000003919_00455

CAZy Family

PL8

CAZyme Description

Chondroitin sulfate ABC exolyase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
973		112611.08	8.8866

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003919	2190589	MAG	China	Asia

Gene Location

Start: 13057; End: 15978 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000003919_00455.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
PL8	578	812	1.3e-80	0.9919028340080972

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01083	GAG_Lyase	3.25e-105	243	889	25	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	8.48e-72	214	545	6	356	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	3.16e-48	23	183	4	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	1.04e-26	577	812	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.
cd03857	M14-like	0.005	168	234	42	105	Peptidase M14-like domain; uncharacterized subfamily. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVQ18406.1	0.0	8	973	18	982
QNM15141.1	0.0	10	972	11	973
QUH29903.1	7.35e-245	23	947	216	1187
APC49583.1	6.67e-226	24	970	202	1179
QZE14915.1	2.63e-204	39	954	42	1000

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Q1F_A	4.40e-164	24	938	23	980	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	3.10e-93	23	973	41	1020	CRYSTALSTRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION [Proteus vulgaris]
7EIP_A	4.26e-93	23	973	41	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C7S340	6.21e-179	23	938	12	956	Chondroitin sulfate ABC exolyase (Fragment) OS=Proteus vulgaris OX=585 GN=ChABCII PE=1 SV=1
Q8A2I1	5.44e-172	23	938	22	980	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	7.64e-172	23	938	22	980	Chondroitin sulfate ABC exolyase OS=Bacteroides thetaiotaomicron OX=818 GN=chonabc PE=1 SV=2
P59807	2.33e-92	23	973	41	1020	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
0.044103	0.952629	0.002321	0.000343	0.000280	0.000297

TMHMM Annotations download full data without filtering help

start	end
5	24

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