CAZyme Information: MGYG000003534_01605

Basic Information

• Species: Treponema_D sp900769325
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900769325
• CAZyme ID: MGYG000003534_01605
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1192		131365.12	4.705

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003534	2560433	MAG	Fiji	Oceania

• Gene Location: Start: 5870; End: 9448 Strand: +

Full Sequence      

MKNLKKVLFFSIVFAILFLSGCADSLQSEDKVQNQFGTLKVSSSDSKSRVLDIEEIKFAS
CVISGTGINVSEAPSKSGLAVEGGVGTFSIENIPIGKNRIVTVQAYASSTEKMDGVTLRA
VTDIVSGENSVVVNWSTTALGNVFYYLLNSGYDISSVTKDGISQIENAIPTDIHPSLVNA
KKIAEDFSSSSLSSSTEYKNTPATLRFIYNNLSESEYYVQVTDPSSAKKMFTAGQTDVEN
IAPGTWKVYIFSKDGKTVLERKVLNTFTSGETLNLGDISPTKLTDIIVHAKVPYIYIWDS
GTSADKIEFTSMNDEGNGWYGYTIGASSAGIIFLSQANWSAKISGDLSRTTPGEYWFKDD
TWYDYNPDKPLTPVIKASVLPGTYLEPQTVTLAGSNSSDIIYYTTDGTEPSSSSFVYSSP
IKVSNTMTIKAFGYNEGAEPQKGSVYEFAYKIDPDADVVPPVITPNKKSGKYTEALSDIK
FTITDNKSNGVKVYYTTDGSVPTESSSEYLTITSGSTSGTGKSFSVDVKETLSIKLLAVD
AYGNKTSASYTYRVTDGSVVDFREESIYFLMTTRFYDGDTSNNEYCWDEGGEYLKFGAND
CAWRGDFKGLAEKLDYIKALGFSAIWITPVVENASGIDYHGYHAYDFSKVDPRYESTGFT
YQDLIDACHKKGIKVIQDIVLNHSGNFGERNIFHMFDKETTPYVNKDIDIPVSGAATKRS
PFMKLATDGSYGAKALSKALGGKDYESSIGSVQYGARIDAMKEDSNDTDFIYHHCKTIDW
NSEACQLGQMAGDCVDLNTENPKVAEYLRNCYVNYINMGVDAFRIDTVKHISRLTFNNEF
IPQFMEAGGESFFIFGETCARYRGRWNEGVPALSPSFYTWTEDKDFSWSKTDHAANSKAA
SAHFETYRGDFVHPAWSDGIANHLLNGNDYHTPDWTKRSHLDQIDFPMHWAFSNASDAFN
TAVQTNDPDFNDATWNVVYVDSHDYAPDNAPEGQRYAKPEEWPRNMNLMFTFRGIPCIYY
GSEIEFMSGAPIDPANTCTSLDQSGRAYFGDYLEGDVKASGFGEYTASGTVQDTLNHPLA
QHVIRLNKIRRAIPALQKGQYSTEGCSGGIAFKRRYKDDTVDSFVLVAIGAQATFTGVPT
GEYIEVITGKTVSCSGTLTSDSIEKDNMRVYVLKTPSCDITEQIGVAGAYLK

Enzyme Prediction     

EC	3.2.1.1	3.2.1.98

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	604	1029	6.9e-146	0.997624703087886

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	1.16e-111	563	1093	1	344	Alpha amylase catalytic domain found in bacterial 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). This group of CMDs is bacterial. 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.
cd11320	AmyAc_AmyMalt_CGTase_like	1.40e-50	561	1048	1	377	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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.
cd11340	AmyAc_bac_CMD_like_3	2.94e-42	567	1029	6	357	Alpha amylase catalytic domain found in bacterial 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). This group of CMDs is bacterial. 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.
cd11319	AmyAc_euk_AmyA	1.04e-40	561	1036	5	343	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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	5.55e-40	605	1034	1	334	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSI03197.1	8.69e-296	1	1191	8	1204
AIQ52956.1	3.39e-274	312	1192	348	1184
AET61000.1	3.52e-274	284	1192	73	948
QDY82638.1	7.91e-273	263	1192	58	948
AOK92813.1	1.16e-272	284	1192	74	949

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CYG_A	2.04e-26	560	1149	7	458	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
6WNI_A	1.83e-22	563	1129	32	461	ChainA, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]
1V3K_A	2.03e-22	561	1036	11	374	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3K_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3M_A Chain A, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3M_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]
3CGT_A	3.52e-22	562	1188	12	504	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans],8CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans],9CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans]
1V3J_A	3.54e-22	561	1036	11	374	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3J_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3L_A Chain A, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3L_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	1.34e-31	561	1036	743	1084	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P31797	1.25e-25	560	1149	38	489	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
Q05884	1.78e-24	605	1114	98	547	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P08704	2.70e-23	560	1160	38	536	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P27036	6.72e-22	560	1171	35	511	Cyclomaltodextrin glucanotransferase OS=Bacillus ohbensis OX=1481 GN=cgt PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000032	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
7	26