dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

UBA4855 sp900540395

Lineage

Bacteria; Firmicutes; Bacilli; RFN20; CAG-826; UBA4855; UBA4855 sp900540395

CAZyme ID

MGYG000000974_00238

CAZy Family

CBM32

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
947		107205.74	4.4127

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000974	1617589	MAG	Australia	Oceania

Gene Location

Start: 129593; End: 132436 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000000974_00238.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	523	745	1.2e-20	0.7165605095541401
CBM32	176	283	8.2e-16	0.8870967741935484

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0366	AmyA	5.37e-12	520	688	28	201	Glycosidase [Carbohydrate transport and metabolism].
cd11334	AmyAc_TreS	5.83e-12	557	686	62	197	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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.
cd11316	AmyAc_bac2_AmyA	2.25e-10	578	706	78	204	Alpha amylase catalytic domain found in 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.
pfam00754	F5_F8_type_C	4.82e-10	176	265	6	107	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam00128	Alpha-amylase	4.08e-08	520	692	3	179	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
ATB27203.1	2.69e-136	31	903	34	953
QQA30230.1	3.16e-123	28	913	37	866
QUT61733.1	3.32e-123	28	913	39	868
QNK56434.1	1.39e-23	41	288	585	835
VEU81207.1	4.34e-18	499	685	4	195

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OT1_A	1.59e-11	523	688	354	506	ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]
4M8U_A	2.60e-10	498	686	1	200	TheStructure of MalL mutant enzyme V200A from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]
5BRQ_A	4.57e-10	499	689	11	213	Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580]
5BRP_A	4.57e-10	499	689	11	213	Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580]
4MAZ_A	5.96e-10	498	686	1	200	TheStructure of MalL mutant enzyme V200S from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54796	9.32e-12	499	685	3	194	Glucan 1,6-alpha-glucosidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=dexB PE=3 SV=2
P39795	1.57e-10	501	689	8	207	Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2
Q9P6J3	8.45e-10	500	689	12	216	Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mal1 PE=2 SV=1
P20845	3.04e-09	557	686	104	234	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
Q45101	3.23e-09	501	685	4	199	Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.016392	0.418452	0.563871	0.000629	0.000343	0.000283

TMHMM Annotations help

There is no transmembrane helices in MGYG000000974_00238.

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