CAZyme Information: MGYG000004180_02125

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides
• CAZyme ID: MGYG000004180_02125
• CAZy Family: PL8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
923	MGYG000004180_19|CGC1	104320.94	5.7017

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004180	4626686	MAG	United Kingdom	Europe

• Gene Location: Start: 40002; End: 42773 Strand: +

Full Sequence      

MNLRNKVSLLVFFFVTIPLFAQTPQRELERLRQNYIRSFISNDEQTASLVELLSGIQPET
EISDQVVVELHQRYPFNIEKITGYIETIREDGSWPDIDYNDRKRSGWSVKQHADRVLELA
KLYRAEEGDCHWGPKLESVIHQALGYWFREKPVCKNWWYNQIGIPKTLGPAFLLMKERLS
PEEKAGAIEVMENAKFGMTGQNKVWLAGNVLIRGLLQDDFGLVKAARDTIVSEITTGMQE
GIKSDWSFHQHGPQQQFGNYGLAFLTEMSAYSGLFAGTVFALSEAQQDILNSFLLNGYRW
IVWKGYMDVNALDRQLFHSAQIHKAFSLAFATNALMRGSSGDDIRQMNEFLQDNYAPERK
GSAFTGHKHFWDSDQTVHRSPAWMASVKMASDRVIGTELVNEDNLKGFYMGDGALYTYCR
GDEYLNIFPFWDWRKIPGITSYESEAPVPAFFHYGAHVRNKTAFVGGVTDGQAGMTAMIL
DRDGLQAYKSWIFTRDYVLCLGAGIHSDSTLAVTTSIDQRVKHGDLLRYAGGDWLPVQGK
YVSSAEKLRFFHDNTGYILLQPSACVAVSEKRSGRWCDFMGSYAPKTVEGEIVGLYIDHG
KEDNAGYQYLILPASTSEKTAAFPVQDIRVIRNDKAVQAVAAGGCFYVTAYEPQKLDLQE
DLWVDIQTPGIYMFHRHNGNWQIEAADPTHKQPFLSLKMNGQDVKAVFPPSHEPGKSISV
QPFINAPSVTEIKVDGKRDDWKIAPAVTGLTAPWDGAEKDGTAFYVCHDKKNLYFLYVVS
DTTLVYNDEKTEASVGNGDRIEFFMSKDPEMKTYYCAEIDPQGKVMDYEAHAYRKFDFSW
DFKDLKLATYVGKDSYRVEGSISLRSLKALGLVSPDGEIRMGVYRADYFGDAGDRVIWSS
WIVPDAAEPDFHIPSSLGVLKLE

Enzyme Prediction     

No EC number prediction in MGYG000004180_02125.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL8	367	616	1e-64	0.9884169884169884
CBM9	734	922	3e-18	0.9945054945054945

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01083	GAG_Lyase	3.48e-150	72	688	17	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	1.03e-85	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	1.13e-29	79	346	27	315	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	1.93e-13	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.
cd00241	DOMON_like	1.71e-05	746	901	4	158	Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT47778.1	0.0	1	897	1	897
QDO71119.1	4.92e-275	27	720	26	721
QUT90440.1	7.35e-272	27	720	26	721
ALJ58447.1	6.78e-270	1	720	1	721
QCT78112.1	1.94e-269	5	674	2	656

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CB8_A	8.03e-83	77	721	23	678	CHONDROITINASEAC LYASE FROM FLAVOBACTERIUM HEPARINUM [Pedobacter heparinus]
1HM2_A	1.30e-82	77	721	45	700	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	4.24e-40	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	4.24e-40	156	699	124	714	Crystalstructure of the Arthrobacter aurescens chondroitin AC lyase [Paenarthrobacter aurescens]
2WCO_A	1.51e-33	156	641	139	667	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q59288	7.13e-82	77	721	45	700	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
Q9AQS0	4.91e-28	94	640	68	674	Xanthan lyase OS=Bacillus sp. (strain GL1) OX=84635 GN=xly PE=1 SV=1
Q59801	1.00e-19	156	680	182	759	Hyaluronate lyase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=hysA PE=3 SV=1
Q53591	2.65e-14	85	613	291	897	Hyaluronate lyase OS=Streptococcus agalactiae serotype III (strain NEM316) OX=211110 GN=hylB PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000427	0.998769	0.000237	0.000190	0.000193	0.000172

TMHMM  Annotations     

start	end
7	24