CAZyme Information: MGYG000000733_00889

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; Borkfalkia
• CAZyme ID: MGYG000000733_00889
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
951		105341.21	4.2397

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000733	1893651	MAG	Kazakhstan	Asia

• Gene Location: Start: 22305; End: 25160 Strand: -

Full Sequence      

MRRYGIKFLGALFLAAVLVLQMVPVYALTARADTPAYDISATSETAGHLAASAADGNTST
YWMASEEDDSPELCADLGEVRAVTGYKQIFATSDVWFFTVYGSLDNVNWTPIADYSIGAS
GKSFADSASGFYRYVKVVFFASQNGSAFTSAEFAIESKSLSEGTNVALGMKGYSGSWAAG
FEHESAFDGDTGSYYCANDGNYPQWCGVNWEYECAVNSVEIYLQDYGTYEFEVTAKGMDG
QTVTVAERAVRTGSYFRFETDGLFSNVEYKVYAGPGWANLAEMKVNGFKDLASDKCATAA
QWEIKDGANVFYFPYGAYVDEVRGASSVSISQDGSSWTSVADASTIGSIVNYVKAESDGA
IRLFGTPLERDLAQGLKGSVSDYSNEGFNAEKATTNPEHEDGRNQFWCAESSGGKHWLQI
DLGNVCRVEKVVQRFQDPGSYRFKIEASKDGTDWVVLHDGLSELGSGQKFEVMTGEEKMF
RYVKLTVVEDSGWANSNQFQIIGFGEPVPEHWWQRESGVVRYYPKEQKVSIADMTDKLEY
YRENGMKVIEVHQPYEGAGDIWSGLGATDNYNADPVNGTLDDWAAFLDKAHSLGMYVFMF
GNVGYARDYSPFFEKACMDYANGIASEERDWFLFSETCPDPAKWFWSDTANAYYYAYWEE
GGQIPNYNFDTEAWQAESKRYVTYWADFGFDGVALDAPPAYYFGSADPATVTYESITKPL
NARNIMILPEGTGDYNYIYSYHYTTIQNYNMGQWGGGAWSLGIDAVTDQNARTVDDFIKS
GRDNAVSLGGSAIAPLCFEQKYENVEDYKRKAEAALLTTSGHMAFLHSGTSAFVGQDIIE
TWSEDLRSAVFEMFALQNSFAAFNASGMRYRVPTNDDTVYYAYCRGDLRGNTRGLVVFNY
SGQQAEICVDLSNTGFGGTFFDLLTGKRYESAGDELRLTIPGSSYVILGQF

Enzyme Prediction     

No EC number prediction in MGYG000000733_00889.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	534	748	9.3e-17	0.6910828025477707
CBM32	382	494	5.8e-16	0.8225806451612904

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11334	AmyAc_TreS	4.22e-17	568	699	62	199	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	5.95e-15	568	712	57	200	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.
COG0366	AmyA	1.19e-12	531	752	28	268	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	3.19e-12	535	752	7	237	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.
pfam00754	F5_F8_type_C	1.51e-11	39	152	2	125	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATB27203.1	3.36e-157	39	949	44	991
QQA30230.1	7.37e-129	41	949	52	887
QUT61733.1	7.75e-129	41	949	54	889
QNK56434.1	1.44e-26	39	501	585	961
SDU79006.1	2.16e-26	507	948	50	499

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WY1_A	1.20e-11	512	702	7	208	Crystalstructure of alpha-glucosidase [Halomonas sp. H11],3WY1_B Crystal structure of alpha-glucosidase [Halomonas sp. H11],3WY2_A Crystal structure of alpha-glucosidase in complex with glucose [Halomonas sp. H11],3WY2_B Crystal structure of alpha-glucosidase in complex with glucose [Halomonas sp. H11]
3WY4_A	1.20e-11	512	702	7	208	Crystalstructure of alpha-glucosidase mutant E271Q in complex with maltose [Halomonas sp. H11],3WY4_B Crystal structure of alpha-glucosidase mutant E271Q in complex with maltose [Halomonas sp. H11]
3WY3_A	4.79e-11	512	702	7	208	Crystalstructure of alpha-glucosidase mutant D202N in complex with glucose and glycerol [Halomonas sp. H11],3WY3_B Crystal structure of alpha-glucosidase mutant D202N in complex with glucose and glycerol [Halomonas sp. H11]
5X7U_A	4.46e-10	531	702	32	208	Trehalosesynthase from Thermobaculum terrenum [Thermobaculum terrenum ATCC BAA-798]
5M99_B	5.98e-08	531	707	26	199	FunctionalCharacterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization [Thermotoga petrophila RKU-1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P72235	3.03e-08	534	702	43	216	Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1

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
0.014829	0.983756	0.000524	0.000350	0.000255	0.000249

TMHMM  Annotations     

start	end
5	27