CAZyme Information: MGYG000001927_01660

Basic Information

• Species: Prevotella sp900547005
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900547005
• CAZyme ID: MGYG000001927_01660
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1111		122448.95	4.9386

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001927	2803818	MAG	Denmark	Europe

• Gene Location: Start: 5613; End: 8948 Strand: -

Full Sequence      

MERFKHLLFVVMAFLVFATTNAFAQSDFNANRTDFRDETIYFAMTTRFYDGDPMNNVLCW
DGVENQKKNNDPCWRGDFKGLIDKLDYIKALGFTAIWITPVVQNASGFDYHGYHAMDFSK
VDLRYESHKEWNSSEDVTFQTLIDKAHAKGIKIILDIVLNHTGNFGEATLQPIFKRDGNI
KNQAYIDACMTPTDLLGSDYSTLQPGFQYQRRLAMMKNTDGKNHDTKNYWHHFGMFNWDD
NSRWWGQIAGDCVDLNTENPATYEYLIKCYGEFIKMGVDGFRIDTTGHISRLTFNSTFIP
AFQKLGEQYKDKRLGSAPFYMFGECCARFGGVIYRGDHSLSSHFYTWKSPQSLVDEFNGY
TAEWWAQQVRPGDSEPVGNMLTCQKDVDFSEKSDNVFMKDGAWHEPDYSKASGYNVIDFP
MHYNFNNAGQAVRIAQEGDHYYNDASWNVVYVDSHDYCPGPNDGIRFNGGTSQWAENLAL
MFTFRGIPCIYYGSEVEFQKGVAIDKGPDLALANSGRAYFGAYLEGNVTATDFGEYTADG
NVAQTLNADLAQHIRRLNQIRQAVPALRKGQYTWDGCTADGGWAFKRAYKDSYALVAING
GATFENVPAGTYVDLVTGQQYTGGGSITVDAPQTQGQLRVLVKDWKGGKVGEDGQFIYAS
SPVAHGGSVTFSDPGTTQYYTADDAPGNPDIKFNPAGGAFKTENITVTATLNEAATSGWY
KVGEDGEKKELVGAGASSTFTIGDGMSYGQTVTVYYGATDGTAETSGKATYKKVDPNATI
TIYVKASSAPNLYAWAGANNELNGAWPGKKMSNKTTVNGEEYYCQEFADVESLNVIFNNG
TSKTADIEGIDADAYFTYDGGTGYKDITGEISLDPTNVTVKANKATGTYYQSVDVTLTAS
KNDATIVYTTNGSEPTASSDKATGSKSFTFTQTTTLKAGALVDGVVKNVVSYVYTISNEQ
PNNVTLYYDNANNWSNVYCYAYVNDGAVKNAEWPGKPMTFDATLTINGKTGWWVYTMPDN
LKEAQVLVNNGNGAQYPGADEPGVFMEGKSKVLTGTTLSDLPTGISSVVTTPIANVFRVY
TLDGRAINGVKSTKDLRKGVYIVNGRKLVVK

Enzyme Prediction     

EC	3.2.1.1	3.2.1.98

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	177	501	3.7e-85	0.6983372921615202
CBM26	965	1039	4.9e-16	0.9066666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	6.73e-115	36	564	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	7.20e-53	34	495	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.
pfam00128	Alpha-amylase	8.57e-42	76	496	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.
COG0366	AmyA	8.54e-39	39	603	2	486	Glycosidase [Carbohydrate transport and metabolism].
cd11340	AmyAc_bac_CMD_like_3	9.45e-39	39	507	5	364	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNT65572.1	0.0	1	1111	1	1117
QNT65573.1	0.0	15	1111	14	1114
QNT65571.1	0.0	15	1111	2	1114
QCT07168.1	1.32e-200	30	654	139	790
QCT07981.1	1.24e-199	26	650	129	734

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1A47_A	6.71e-29	30	629	7	471	CGTASEFROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR [Thermoanaerobacterium thermosulfurigenes],1CIU_A Thermostable Cgtase From Thermoanaerobacterium Thermosulfurigenes Em1 At Ph 8.0. [Thermoanaerobacterium thermosulfurigenes]
3BMV_A	1.18e-28	30	629	7	471	ChainA, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes],3BMW_A Chain A, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes]
1CYG_A	2.55e-27	29	618	3	458	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
1V3K_A	3.24e-26	30	631	7	473	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]
1QHO_A	7.50e-26	36	501	7	370	FIVE-DOMAINALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	4.54e-31	33	501	742	1079	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P26827	2.37e-28	2	629	3	498	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2
P31797	5.17e-27	14	618	19	489	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P08704	7.07e-27	34	634	39	535	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P19531	4.60e-25	36	501	40	403	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2

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
0.000219	0.999154	0.000150	0.000152	0.000138	0.000133

TMHMM  Annotations     

start	end
7	26