CAZyme Information: MGYG000001795_01692

Basic Information

• Species: Amulumruptor caecigallinarius
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor caecigallinarius
• CAZyme ID: MGYG000001795_01692
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1128	MGYG000001795_10|CGC2	124697.67	4.4266

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001795	2604985	MAG	Denmark	Europe

• Gene Location: Start: 66112; End: 69498 Strand: -

Full Sequence      

MNLKKMLLGGMVALGTLGQQAMASAEFNANRTDFRDETIYFAMTTRFYDGDPKNNVCTWD
KQEQQISTKDPAWRGDFAGLIEKLDYIKALGFTAIWITPVVQNGSGIDYHGYHAMDMSSV
DLRYESRTEWGSEKDVDFQDLIDAAHAKGMKIVLDVVLQHTGNFGEVNINPLFTRNQNIR
NQASIEACMKPDNERLGGASYWKLPNEGSVTQYSERFKYFKNPQYDTQNIYHHYGTGWNW
DLPNRWWGQIAGDCVDLNTENDYVAQYIVDCYGKFIEMGVDAFRIDTTGHISPLTFNTQF
IPQFHEIANRPEVKAKRLNGVDFYMFGECCQRFQGSVVYRDQPNLSSYFYTWKSDQSLMD
QFKASSSLSWWEQQNLPEGHDSPVGPMAVCESDTQDKPRSNNVWMQNGQWHEPDYSQASG
FNVIDFPVHYSFSSVSSIMGLFSQDNYYNDASFNVVYVDSHDYSPGPNDGIRFNGGTSQW
AENLSWMFTFRGIPCLYYGSEVEFMAGKTIDDGMSTALNNTGRAYFGHYLEGDVSATDFA
EYTASGQVAATLKGDLAHHIQQLNKIRAAVPALRKGQYTFDGCSADGGWAFKRAYKDSYA
LVAVNGGATFSDVPAGTYTDIVTGQTYTGGGSITVTAPSTQGQLRVLVKDWTGGKVVEDG
KFIYTSSPVAQGGNPTATDPGASFFYTKADAVDESVGMNFSPNGGSFKTETLTVTVTLTA
GATSGTYTVAGQSTQTINQGESKTFTVGAGMSYGETVTVSWTATGKEGNESGTVTYKKVD
PNAVITVFCKASTAPNLYAWRTGTETSLNGAWPGTKMSQTTEVNGQTFYYQDFPGEEDIS
IIFNNGSAKTGDITGITESVYYEYDGNTTATKLDIPVGPTKPSVSASPASGTTFNESIKV
TLSSSVDIHYTINGDEPNASSPVYNEPLTFYETTTLKTYVENEVGSNVQTFIYTKTDTPV
GDDVCVYYDGNWTNVSIYVYNDGGSMTSWDNAPAMTIDPATGYYMYTLPEEFETSQVIFK
SNGQQYPGQNQPGLQVNGKSMIYHHNTNEWVEYTPLGFEDITDMNANKLDIQVIGGQLVI
YSEQQTSIDVTSLTGQRHTIYLYPGVNTVESLANGFYVVEGQKVMLNR

Enzyme Prediction     

EC	3.2.1.59

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	74	507	2.9e-111	0.997624703087886

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	4.09e-104	35	570	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	2.02e-45	33	525	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.
pfam00128	Alpha-amylase	1.59e-39	75	502	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.
cd11340	AmyAc_bac_CMD_like_3	3.12e-39	38	513	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.
COG0366	AmyA	8.14e-35	38	609	2	486	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNT65573.1	0.0	8	1126	8	1113
QNT65571.1	0.0	17	987	5	989
QNT65572.1	0.0	4	901	5	894
QCT07168.1	2.11e-182	29	648	139	773
QEH70845.1	1.30e-178	26	663	353	962

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1A47_A	4.93e-28	29	681	7	512	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	8.63e-28	29	681	7	512	ChainA, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes],3BMW_A Chain A, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes]
5A2B_A	1.68e-26	9	605	18	432	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2A_A	1.85e-26	34	605	6	398	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	1.43e-25	34	605	7	399	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	8.46e-29	32	636	742	1185	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P26827	3.02e-27	29	681	34	539	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2
P31797	5.62e-24	19	620	25	485	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P09121	1.71e-23	12	637	17	500	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt PE=1 SV=2
P14014	1.74e-23	30	624	42	496	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1

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
0.000291	0.999053	0.000177	0.000177	0.000159	0.000143

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001795_01692.