CAZyme Information: MGYG000000854_00220

Basic Information

• Species: Paraprevotella sp900548345
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp900548345
• CAZyme ID: MGYG000000854_00220
• CAZy Family: GH98
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
957		107970.91	5.7921

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000854	2733305	MAG	China	Asia

• Gene Location: Start: 98463; End: 101336 Strand: +

Full Sequence      

MKRCLLMMLCLFLLGDMALYAQSRRPIDNKHPMWLIHIDVWNNADPQKIIDLIPADIKPY
VCMNLSLSCQYDNDLKMHKMPQNAVQTYKSWASVCCRNNMWFTCQPASGGKTHIKDDDLE
TFEYFFKNYKNFLGWNYAEQFWGFDDPEDDSSSSQPSRIALFAKLVEMSHNYGGFLTISF
CGNIWSHGLNPVGMLKRNANLLANCKKYPEAILFLYKYTTAGCWYNNESVTLAPFISGLA
KNYGVRYDNCGWNGALGAIFGEDSKHGRTYPGAAGIPPVLEQTCLNGACVWDGPELIWTE
CFKEKSKTTVSGYTRRNWTTFSTFDNIWVDMFRKVLDGTIYIPSREEVVERTKFALVSDI
APANDNTSLKARAYATPETLYDGIYKQDDPFNRDNGQMDKNNCYYKKTGRYQTIPVLFPL
EHCDDLAKSINTKLTRTDYDNNFGNWQNETMKQVKLNRLYPEVSKGDMFVARNHNELLCY
TPYSYLNYKVASKASVPLQYNSCTSLELNFPRFSSAVVKEYNDRIVFYLNNFRSDTVASV
TDVIKVVGASSKPAYSYKDRVSTKSVITEEWNAETATYTCSVSHMGPLDLTIHCEGANVD
DRSTDYLSDEPIAELPQQPTAYYGELVIEAEDMDYKNVKENVTHAYNSSYRELRGHSAMG
FQVLGTSTAAALRNATMINFGGTYNVTVKYMSQAKAQVMVSCGSVSRKVLTLSASGETWQ
TVSFETTLKSGSNTFTLTNVGGKNVYIDNVTFTPLQLDDPIDEVWTDLMPEMFHQWSGVD
ATAVDNGPVDCAYGLNTETWLPYGDGNVNYLRYADLSDYATLEITVTQGTPRLLFNRYTD
GGSYIGFEPDNAVFMTKVVANGNGTISYYYDLAAIKEQDGYVHLNAIKGVGEWSGADKPI
VTAMRLTTSGIGTVEVRPVAKERNMPTDEIYDLFGRRVYTLVKGHVYIIGGKKVLYR

Enzyme Prediction     

EC	3.2.1.8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH98	22	340	5.7e-86	0.9877675840978594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam08306	Glyco_hydro_98M	1.13e-88	21	340	5	328	Glycosyl hydrolase family 98. This domain is the putative catalytic domain of glycosyl hydrolase family 98 proteins.
cd04083	CBM35_Lmo2446-like	4.23e-05	629	752	4	125	Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.
cd04081	CBM35_galactosidase-like	9.07e-05	628	742	3	115	Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.
smart00606	CBD_IV	4.21e-04	678	752	47	129	Cellulose Binding Domain Type IV.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB29515.1	6.52e-283	11	850	10	842
AOZ99817.1	3.16e-176	24	753	37	742
QUT78600.1	2.84e-173	24	750	228	934
QUT26887.1	2.84e-173	24	750	228	934
QRQ55178.1	2.20e-172	24	750	228	934

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WMH_A	3.47e-07	21	592	27	581	Crystalstructure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae TIGR4 in complex with the H- disaccharide blood group antigen. [Streptococcus pneumoniae TIGR4]
2WMG_A	1.04e-06	343	592	326	581	Crystalstructure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae TIGR4 (Sp4GH98) in complex with the LewisY pentasaccharide blood group antigen. [Streptococcus pneumoniae TIGR4]
2WMF_A	1.37e-06	21	592	27	581	Crystalstructure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae TIGR4 (Sp4GH98) in its native form. [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000243	0.999117	0.000140	0.000173	0.000151	0.000143

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000854_00220.