CAZyme Information: MGYG000004026_01854

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873
• CAZyme ID: MGYG000004026_01854
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
669		73393.59	5.2088

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004026	2540060	MAG	United Kingdom	Europe

• Gene Location: Start: 23354; End: 25363 Strand: +

Full Sequence      

MHGWTGGKNDQFPHYAFHGYYALDWTYIDRNMGTVEEFREFVTEAHRRGIRVVMDIVLNH
TGYCTLDDCVDYDFGNFNGTPTAGWMPSSGKYTMWSTDNAVSFNADSQGKWGNWWSQWVR
AFGDRSWAAGAGFAPAGGDNYTQSLAGLPDVVTEKTASVAIPPFLKMKWQQENSGDYLDY
RLPNLDSWRCDNAGSPADYIIHWLAGWVEEFGIDGFRCDTAKHVELSRWKQLKEACNAAL
TAWRNSSRADSYAKGWTDAFWMTGECFGWEHGDTGYFTQGGFDSMINFAFNSSEGSTGRT
PSTGDWEYYSNFCNGSNGRQVLNYVSSHDTGLHRLGDQKKVATMLLLCPGGAQIYYGDET
SRPMMSGCGDQSMATRSDFNWDAVDNADNLHWQKIGQFRRRNPAVGGGRQTNLGGDTYAR
TFTDGDYSNAVVIKLNTQAGRSYTVNVGSAFAEGAKVMDGYNTQNSATVSAGKVTMTASG
PVLLIEPFGQIGQITPPTPQAPTVTADPASGATFSSTLTVKLTNSDGSQIRYSLDGPATA
SSALYTAPITLDKTTTVHTYTANANGHRNQSFTYTKTDTPPVPPVPDNTIYFDNSSANWS
TVKVHYWGGTEASSWPGKDMQPVGNNVFSFTCPEGTTGLVFNNGNGKKTADLNFVSGHIY
NREGDQGEY

Enzyme Prediction     

EC	3.2.1.98	3.2.1.60	3.2.1.-	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	360	4.7e-104	0.9111111111111111

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	4.43e-116	1	413	256	658	alpha-amylase; Reviewed
cd11338	AmyAc_CMD	2.54e-22	18	404	85	383	Alpha amylase catalytic domain found in 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). 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.
cd11339	AmyAc_bac_CMD_like_2	1.40e-21	8	402	71	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.
COG0366	AmyA	2.05e-20	15	359	56	355	Glycosidase [Carbohydrate transport and metabolism].
cd11313	AmyAc_arch_bac_AmyA	3.90e-20	18	408	58	336	Alpha amylase catalytic domain found in archaeal and bacterial 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 firmicutes, bacteroidetes, and proteobacteria. 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
CQR56565.1	5.67e-124	1	551	135	666
SBU87531.1	3.55e-123	1	511	119	610
BAB04132.1	3.55e-123	1	511	119	610
BAF93484.1	1.92e-122	1	511	119	610
BAG70894.1	1.92e-122	1	511	119	610

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OT1_A	9.99e-10	18	405	381	690	ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]
5A2A_A	8.31e-09	16	359	73	327	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	9.07e-09	16	359	107	361	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]
3K8L_A	2.54e-08	13	359	84	511	ChainA, Alpha-amylase, susG [Bacteroides thetaiotaomicron],3K8L_B Chain B, Alpha-amylase, susG [Bacteroides thetaiotaomicron]
6BS6_A	2.54e-08	13	359	85	512	SusGwith mixed linkage amylosaccharide [Bacteroides thetaiotaomicron VPI-5482],6BS6_B SusG with mixed linkage amylosaccharide [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	5.88e-89	1	413	255	651	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	1.15e-21	16	477	139	601	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P36905	5.57e-10	18	490	485	926	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P21543	6.42e-09	4	237	804	959	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q8A1G3	3.57e-08	13	359	107	534	Alpha-amylase SusG OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=susG PE=1 SV=1

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
1.000083	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004026_01854.