CAZyme Information: MGYG000003515_00938

Basic Information

• Species: Prevotella sp900769275
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900769275
• CAZyme ID: MGYG000003515_00938
• CAZy Family: GH98
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
885		98501.99	8.1734

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003515	2052370	MAG	Fiji	Oceania

• Gene Location: Start: 4137; End: 6794 Strand: -

Full Sequence      

MKRIITTLLCLLCLTSSMNAQQRRPIDNEHPLWMIHIDVWNAADPQKIIDLMPDDIKPWL
CMNLSLSCQYDKENNVYKMPRSAVRTYKSWASVCQKNGVWFTCQPASGGRTHLQTTDLET
FEYFFKQYPNFLGWNFAEQFWGFDEADMGSATQTGQIALFAELVKMSHEYGGFLTISFCG
NIWSHGLSPVGMMKRNKNLLNACRAYPEAILWLYKYTQPWCFLNAESTTISPFISGLAKN
YGVRYDRCGWCGAMDCVLGQNVAKYPIAAGIGTVMEQCGVNGGAVWDGPETIPDECFKET
SRTTTTDGYTQRNWTTYEGFRGAWIDMWRKVIDGTLYIPSRKEVVDSTRIAIIANTTSGS
DEDKYATWGSLYDGLYKQSDPANRDNGQWMNNGCYFKSTGRYRTIPLCLEMYDDLAKSIP
TKLNRATAKSQWASVSTKQKFFNAKYPVMSKGDLFVSRVQNQLVTYTPYTYLNGKRTATG
HVPLLYNTCDSLTLTLGMLGSGIVREYGDHIDFYLNNFRTDTTALVTETIVIKGAASEPS
YTLRKGLLATGSVTPSWDAEAKTYTLTVKHKGGMEISVSCSGNATDRKAFAASPTPLSIP
KQPSAYRGEIIIEAENMDYKNVKEIKLVNPYGNYFPDIVEFAGNGFVDMGTSSVGMLRHR
LKLNEGEAGEYRISVRYTATTKAGQIRASVNGTSSKLAIEKTDKNDWHKVSFTATLKAGT
NTLVLANTGAVPMYIDQIIYTPADMEEEKYLVTIRNANYGSLTADVTEAAEGQTVTLDIK
ANAGYGLKELKVINGVNFTLGTDISLTTLSNGNTRLTFTMPDDIVTLQPVFAKGENVADG
IDIINADGSKATVIYGINGERRKTMSRGINIVRTADGKTRKVMRR

Enzyme Prediction     

EC	3.2.1.8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH98	20	336	6e-79	0.9908256880733946

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam08306	Glyco_hydro_98M	2.58e-83	20	336	5	328	Glycosyl hydrolase family 98. This domain is the putative catalytic domain of glycosyl hydrolase family 98 proteins.
pfam08307	Glyco_hydro_98C	1.63e-11	341	578	1	267	Glycosyl hydrolase family 98 C-terminal domain. This putative domain is found at the C-terminus of glycosyl hydrolase family 98 proteins. This domain is not expected to form part of the catalytic activity.
cd04083	CBM35_Lmo2446-like	1.32e-08	641	738	23	123	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.
cd02795	CBM6-CBM35-CBM36_like	4.15e-07	612	738	2	122	Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.
cd04082	CBM35_pectate_lyase-like	9.94e-07	641	730	22	113	Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. 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). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB29515.1	0.0	9	831	9	816
QUT78600.1	6.97e-162	23	739	228	935
QUT26887.1	6.97e-162	23	739	228	935
QRQ55178.1	5.39e-161	23	739	228	935
ALJ48334.1	5.39e-161	23	739	228	935

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WMH_A	1.40e-13	20	578	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]
2WMF_A	5.61e-13	20	578	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]
2WMG_A	2.24e-12	202	578	199	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]

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
0.000399	0.998880	0.000196	0.000193	0.000162	0.000153

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003515_00938.