CAZyme Information: MGYG000000044_03146

Basic Information

• Species: Parabacteroides merdae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides merdae
• CAZyme ID: MGYG000000044_03146
• CAZy Family: PL8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
932	MGYG000000044_8|CGC3	105960.03	5.6464

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000044	4300426	Isolate	United Kingdom	Europe

• Gene Location: Start: 110658; End: 113456 Strand: -

Full Sequence      

MNLRNKVSFFLLSFVAVPLFAQTPQQELERLQQNYIQSFISNDDRMASLVELLSGIQPET
EISDQVVVELHQRYPFNVEKIAGYMETIREDGSWPDINYNDQKRSGWSVKEHADRVLGLA
KLYRAEEGDCHWEPKLESVIHLALGYWFREKPVCKNWWYNQIGVPKTLGPAFLLMKEQLN
PEEKEAAIEVMENAKFGMTGQNKVWLAGNVLMRGLLQDDFELVKAARDTIVSEIMTGMQE
GIKSDWSFHQHGPQQQFGNYGLAFLTEMSSYSGLFAGTVFALNKEQQGILNSFLLNGYRW
IVWKGYMDVNALDRQLFHSGQIHKAFSLAFATNALMRGSSAEDIRQMNEFLKDNYAPERK
GSAFIGHKHFWDSDQTVHRFSTWMASVKMASDRVIGTELVNEDNLKGFYMGDGALYTYCR
GDEYLNIFPFWDWRKIPGITAYESEAPVPAFFNYGAHVRNKTAFVGGVTDGETGMTAMVL
DRDGLQAHKSWIFTRDYVLCLGAGIRSDSILAVTTSVDQRVKRGDLLRYADGNWLPVQGK
YVSSPEEQRFFHDNTGYILLQPSAYVAISEKRSGRWCDFMGSYAPKMVEGEIVSLYIDHG
REDNADYQYLILPASTAEKTAAFAVQDIRVIRNDTSIQAVAAGNCFYVTAYEPQVVNLQK
DLQVDLQTPGIYMFRLHNGNWLIEAADPTHKQHSLSLKMNGKDVKIVFPPCHEPGKSISA
QPFISAPFSKGIKVDGKQDDWKNVSAVTGLIAPWDGAEKDKTAFYACHDQKNLYFLYEVS
DTTLVYNDEKTEASVGNGDRIEFFMSKDPEMKTYYCAEIDPKGKVMDYEAHNYRKFDFNW
NFKDLKLATSVGKDSYRVEGSISLKTLRKLGLISPEGEIRMGVYRADYFDDAGERVIWSS
WIVPDAAEPDFHIPSSLGILKLENFVPLSRLK

Enzyme Prediction     

No EC number prediction in MGYG000000044_03146.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL8	367	616	1.3e-63	0.9884169884169884
CBM9	734	922	1.1e-19	0.9945054945054945

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01083	GAG_Lyase	7.32e-143	79	688	32	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	1.58e-83	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	9.55e-27	63	346	14	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	3.33e-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.
cd09618	CBM9_like_2	2.93e-08	724	899	2	181	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 subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT47778.1	0.0	1	897	1	897
QDO71119.1	2.69e-274	27	719	26	720
QUT90440.1	5.69e-271	27	719	26	720
ALJ58447.1	7.43e-269	27	719	26	720
QCQ41166.1	1.67e-262	5	675	2	657

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CB8_A	6.70e-83	77	718	23	675	CHONDROITINASEAC LYASE FROM FLAVOBACTERIUM HEPARINUM [Pedobacter heparinus]
1HM2_A	1.09e-82	77	718	45	697	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	1.69e-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	1.69e-36	156	699	124	714	Crystalstructure of the Arthrobacter aurescens chondroitin AC lyase [Paenarthrobacter aurescens]
2WCO_A	3.59e-33	136	641	119	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	5.95e-82	77	718	45	697	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	7.80e-24	156	640	146	674	Xanthan lyase OS=Bacillus sp. (strain GL1) OX=84635 GN=xly PE=1 SV=1
Q59801	7.76e-20	156	639	182	725	Hyaluronate lyase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=hysA PE=3 SV=1
Q53591	1.82e-13	41	613	247	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
0.000495	0.998594	0.000261	0.000209	0.000216	0.000190

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000044_03146.