CAZyme Information: MGYG000002030_01446

Basic Information

• Species: UBA3210 sp900755065
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-449; UBA3210; UBA3210 sp900755065
• CAZyme ID: MGYG000002030_01446
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
353		39790.62	7.4054

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002030	1722017	MAG	Spain	Europe

• Gene Location: Start: 69050; End: 70111 Strand: -

Full Sequence      

MVENASGYDYHSYHAFDFSKVDARYESEDVSFETLLEEVHSRDMKLILDVVFNHTGNFGE
RNLFPMFEKSGDLSAVDCMKLLENSGLPSDYASLSGSQQYDARIANMKNTKNDGSDPNDI
YHHYGNFSWETFGEQVAQIAGDCVDLNTENPIVAEYLVKCYGDFIRMGVDYFRIDTMKHI
SRLTLNNYLLPGLYEYARRCGNDHFYMFGEVCARVREVWNHGIPALSAPFYTWKETKAYP
WGDKETNLASIEQAYTDNSTTSGSRLRPTLSSTASPIMRRITASPAAPASSISRCTGIFS
KPGTLSTSRRTTTVITKTPLTTSSTSIRTIIRRTKYRPSGTIRVPTPGRKTCR

Enzyme Prediction     

EC	3.2.1.59

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	82	262	1.2e-53	0.4014251781472684

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	1.12e-32	2	234	68	203	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.
pfam00128	Alpha-amylase	3.86e-22	6	211	29	215	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.
COG0366	AmyA	3.21e-18	6	233	54	248	Glycosidase [Carbohydrate transport and metabolism].
cd11320	AmyAc_AmyMalt_CGTase_like	1.74e-17	10	275	85	297	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.
cd11352	AmyAc_5	3.55e-15	9	211	78	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEH70845.1	6.07e-88	1	258	427	681
BCJ94880.1	1.18e-83	1	258	314	565
AIQ62238.1	3.58e-83	1	261	664	919
AET61000.1	1.02e-82	1	263	418	675
AIQ71010.1	1.13e-82	1	263	646	903

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1V3K_A	1.36e-11	10	188	97	249	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]
1V3J_A	1.36e-11	10	188	97	249	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]
1I75_A	1.36e-11	10	188	97	249	CRYSTALSTRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1I75_B CRYSTAL STRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1PAM_A CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1PAM_B CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1UKQ_A Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011],1UKQ_B Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011]
1CYG_A	1.36e-11	1	180	83	230	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
3BMV_A	1.81e-11	10	180	98	235	ChainA, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes],3BMW_A Chain A, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q05884	1.09e-13	10	211	140	347	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P31797	7.58e-11	1	180	114	261	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P05618	7.59e-11	10	188	124	276	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1011) OX=1410 GN=cgt PE=1 SV=1
P09121	1.01e-10	10	188	124	276	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt PE=1 SV=2
P26827	1.01e-10	10	180	125	262	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2

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
1.000076	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002030_01446.