dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003684_01189

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Basic Information help

Species

Eisenbergiella massiliensis

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella massiliensis

CAZyme ID

MGYG000003684_01189

CAZy Family

GH151

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
661	MGYG000003684_3\|CGC1	75755.48	5.4194

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003684	6691925	Isolate	China	Asia

Gene Location

Start: 195550; End: 197535 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003684_01189.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH151	24	152	7.5e-22	0.9923664122137404

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14871	GHL6	1.85e-29	24	152	1	135	Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases.
pfam02638	GHL10	5.11e-07	48	224	45	214	Glycosyl hydrolase-like 10. This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,.
cd11313	AmyAc_arch_bac_AmyA	0.001	25	113	24	124	Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
pfam00128	Alpha-amylase	0.005	66	117	52	97	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGH35953.1	4.76e-170	1	613	1	617
QOT11970.1	1.55e-161	1	612	3	618
QHT65569.1	3.57e-136	1	612	39	663
AYQ33819.1	2.64e-133	1	612	30	654
AXE16781.1	1.01e-126	1	612	33	657

PDB Hits help

has no PDB hit.

Swiss-Prot Hits help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003684_01189.