CAZyme Information: MGYG000000502_02236

Basic Information

• Species: Brachyspira aalborgi
• Lineage: Bacteria; Spirochaetota; Brachyspirae; Brachyspirales; Brachyspiraceae; Brachyspira; Brachyspira aalborgi
• CAZyme ID: MGYG000000502_02236
• CAZy Family: GH13
• CAZyme Description: Cyclomaltodextrinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
451		53552.94	4.8603

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000502	2577668	MAG	Fiji	Oceania

• Gene Location: Start: 1980; End: 3335 Strand: +

Full Sequence      

MKVLSYNLFAPLLGNIKNWYSHIDRIKKIGFEWVYINPITYPGFSGSLYATKDYYKYNPA
FFTSSEKDIAEKEIKDFVLYCKNNNIKIMIDLVINHSSKDCNLVEEHFEWYKLKDGKLES
PGAWDNGKWIEWGDLASFNNQKIILNKDNEEIENPIWNYWNELIKHNLELGFSGFRCDAA
YKVNKELWKYLISNAKKENKDIIFFAESLGCSTEDTKDLIESGFDYIASSAKWWDYEGEW
FIEQYNLGRENCKQIAFPSNHDTQRLITEYDGNIWRLKQTFLFTAIVCDMWMITTGDEFG
FYKRCNVVNGNEKDFEKISFDLSEYIKDMAIYIKQNPILKNCGKIVSLDVLENIEKKKKL
EELKKLNENENNEDKKIDIEEKEEIKNPFRKFYKYSLDEKERVFIVINITDKKEEFDAKN
FDIKEDISFDNIVDIKETIEILPYQLKVFKV

Enzyme Prediction     

No EC number prediction in MGYG000000502_02236.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	20	241	3.6e-42	0.9857142857142858

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11313	AmyAc_arch_bac_AmyA	3.08e-33	14	341	19	335	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.
cd00551	AmyAc_family	1.08e-18	23	285	31	245	Alpha amylase catalytic domain family. 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; and 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 this 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	2.37e-17	21	301	8	328	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.
cd11338	AmyAc_CMD	1.53e-16	21	300	60	343	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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	4.53e-15	14	276	26	329	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEM21212.1	4.28e-242	1	449	1	473
ASJ21965.1	6.07e-242	1	449	1	473
QTM08276.1	1.99e-238	1	449	1	474
ANN64130.1	1.62e-237	1	449	1	474
QTM10837.1	1.62e-237	1	449	1	474

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	4.82e-14	14	272	27	279	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
1EA9_C	8.68e-14	14	300	169	459	Cyclomaltodextrinase[Bacillus sp. (in: Bacteria)],1EA9_D Cyclomaltodextrinase [Bacillus sp. (in: Bacteria)]
1J0J_A	4.79e-13	14	335	173	492	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]
1J0H_A	6.35e-13	14	335	173	492	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
1SMA_A	8.08e-12	14	340	173	504	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q63T93	2.44e-16	10	348	16	350	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q08341	3.87e-16	14	343	171	506	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P32818	1.53e-13	14	345	173	509	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 SV=1
Q59226	4.57e-13	14	300	169	459	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
P38940	6.12e-12	14	335	173	492	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000060	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000502_02236.