dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001645_01962

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Basic Information help

Species

Eubacterium_G sp900550135

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_G; Eubacterium_G sp900550135

CAZyme ID

MGYG000001645_01962

CAZy Family

GH93

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
697		76630.61	6.1949

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001645	2556758	MAG	United States	North America

Gene Location

Start: 88; End: 2181 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001645_01962.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH93	49	349	1.1e-85	0.8957654723127035
CBM13	557	694	5.3e-26	0.6914893617021277
CBM35	433	551	6.7e-23	0.9915966386554622

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14200	RicinB_lectin_2	3.05e-31	592	679	2	89	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	1.91e-18	558	631	15	88	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	2.00e-16	638	695	1	58	Ricin-type beta-trefoil lectin domain-like.
cd04081	CBM35_galactosidase-like	4.10e-16	431	551	1	125	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.
cd04082	CBM35_pectate_lyase-like	1.48e-12	431	551	1	124	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU16706.1	0.0	7	607	9	611
QJA00803.1	1.62e-205	24	595	22	588
BAJ74916.1	1.03e-203	20	602	30	605
QZD56017.1	2.68e-198	10	596	20	599
SDT10365.1	6.51e-197	27	603	36	606

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3A71_A	3.21e-44	54	401	22	332	Highresolution structure of Penicillium chrysogenum alpha-L-arabinanase [Penicillium chrysogenum],3A72_A High resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobiose [Penicillium chrysogenum]
2YDT_A	1.80e-36	64	373	37	326	ChainA, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],5M1Z_A Chain A, Exo-1,5-alpha-L-arabinofuranobiosidase [Fusarium graminearum]
2W5N_A	8.47e-36	64	373	37	326	ChainA, Alpha-l-arabinofuranosidase [Fusarium graminearum]
2YDP_A	1.15e-35	64	373	37	326	ChainA, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_B Chain B, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_C Chain C, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum]
2W5O_A	3.96e-35	64	373	37	326	ChainA, ALPHA-L-ARABINOFURANOSIDASE [Fusarium graminearum]

Swiss-Prot Hits help

has no Swissprot hit.

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
0.000645	0.594733	0.403776	0.000402	0.000237	0.000189

TMHMM Annotations help

There is no transmembrane helices in MGYG000001645_01962.