CAZyme Information: MGYG000000639_00438

Basic Information

• Species: Treponema_D sp900541945
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900541945
• CAZyme ID: MGYG000000639_00438
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1197		131711.01	4.7378

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000639	2201404	MAG	Madagascar	Africa

• Gene Location: Start: 10281; End: 13874 Strand: -

Full Sequence      

MKKVLCAIGAIVLFAFCSCSNELEENSRDVVSSGGYGSLVVSKSDSERALDIQSLKFASA
SVSGAGISSGREPSAKDISVTDGTGTLTIDNIPAGKNRIITVQALDSSKNEIFGVTMRAV
CDVEAGKTVNVSVNWKTTALGNVFYELNKSGYGVSNISKDDVKIIDSLIDKSVSSFLIDT
ESLASDFKNKILKDKPSFYVLEPASLAFTCNDNGNFKIQVCDPASSVFSGSGTGGTVKNI
APGKWKVLLLDNEGTKVAEKTAVFTSGKESSVSFASVTDKIIVHVEKSAGWTHVYAWVSK
SEKLFGVWPGELMVDSDGDGWFDVVIEKTACSLIFNNGGNKQTDDLSCTAGEWWFKDNVW
NEENPTDSEPPVINSLVMNVASPVSGTVTFTLTASDNKKLKNAELFVDDVKFSEKSFSSL
NDSLVFEWNSSSAKNGEHKISAVVYDAAGNKSEPKTISVVTENENVRPVASITGSIKVSK
GSEKVYSASNSSDKNGTVAGYKWKVVGATIITGSETSENITVKAPDSEGSFTISLVVTDD
EGLDSEETVITVTVKDKVSNDFREETIYFLMTARFYDGDSSNNRWCRSDDSSGNRDNGDY
PWRGDFKGLIEKLDYIKALGFSAIWITPPVLNRSDYDFHGYHAWDMTKIDPRLESAGATY
QDLINAAHAKGIKIIQDIVLNHSCRFGLKNFFVPKYWGDRDNQYWGTSNEINYYDEYNPN
FEYNGLDVEPKSGKAWYNGDLWQKEKPSLSWNPNLSDWGVQKGFNKEGRAYYGCQWPDLR
LFDPEKFHTEWLGNWEDETCQSGTIHEDCIDLNTEAAAVQKYLIDAYTKYIDMGVDAFRI
DTVKHVSRVMFNRHFIPAFKEAGGENFYMFGEVCTRVNETWNHGVAPLSTPFYTWKERTT
FSADDSVAVHEGYEYENRQGVNNQPTSDNHALIGNAYHTPDYSQKSGLDVIDFPMHWNFS
DASSAYNQRQNDKYYNDATWNVVYVDSHDYGPNMDNRYEGGTEAWAENMTYMWTFRGIPC
LYYGSEIEFMAGAPCDKGSSAPLSTTGRAYYGDNIEGSVQVSGFGEWSNATGSMKATLES
PLSKHLSHLNKIRREIPALQKGQYSNEGCSGGMSFKRRFTDDSTDSFVLVSISGDATFSG
LPGGTYTDVVTGDSKTISEGGSITASCSGKGNARIYVLSTAKTPAPGKITGSSPYLK

Enzyme Prediction     

EC	3.2.1.59

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	603	1032	5.4e-180	0.997624703087886

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	2.80e-124	563	1096	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	3.84e-47	561	1026	1	348	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	7.12e-44	566	1027	5	353	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.
cd11352	AmyAc_5	6.20e-40	567	873	2	280	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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	2.82e-38	604	1027	1	326	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	0.0	4	1196	20	1204
ATB40107.1	3.46e-257	558	1197	334	977
AAW03335.1	1.37e-256	558	1197	334	977
ADO70697.1	1.20e-255	558	1197	424	1067
ATB33730.1	4.61e-255	490	1197	257	980

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CYG_A	2.18e-23	562	1189	9	500	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
1QHO_A	1.55e-22	565	1152	9	463	FIVE-DOMAINALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]
3WMS_A	5.64e-20	540	1189	24	536	Thecrystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans [Paenibacillus macerans]
6AIJ_A	9.45e-20	553	1189	26	526	Cyclodextringlycosyltransferase from Paenibacillus macerans mutant N603D [Paenibacillus macerans]
4E2O_A	1.28e-19	556	1124	1	394	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	1.14e-25	551	1032	733	1079	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P08704	3.84e-24	561	1159	39	532	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P31797	1.31e-22	562	1189	40	531	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
Q05884	5.62e-22	604	1137	98	565	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P19531	9.26e-22	565	1152	42	496	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 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
0.000022	0.011436	0.988561	0.000005	0.000007	0.000005

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000639_00438.