CAZyme Information: MGYG000002281_00983

Basic Information

• Species: Bacteroides faecis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides faecis
• CAZyme ID: MGYG000002281_00983
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase SusG

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
692	MGYG000002281_3|CGC2	78028.7	4.701

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002281	6145961	Isolate	China	Asia

• Gene Location: Start: 155474; End: 157552 Strand: +

Full Sequence      

MKKHLHFLSLLWLSMLLTFMTACSDDKNITEPTPDPEPPVEGQWTALAASPDTWDETKRA
DISYQLLVYSFADSDGDGYGDLNGITQKLDYINQLGVKAIWLSPIHPCMSYHGYDVTDYT
KVNPKLGTESDFDRLVTEAHNRGIKIYLDYVMNHTGTDHPWFTEACSSSESPYRNYYSFS
EDPKTDIAAGKIDMITQEGTAGYNAAEWFQISDETSAVKGLLKFTLDWSNASSPTLIVTT
GAKADEDNPDTGTTNAKYLYYGDGICKKFYDKGNNLYELTVDFESTWGLLIRTSNDSSWP
AGTKYGASSSSEKVTLNKEFKLTNAGTPANIMFDSQQITYFHSHFCTDWFADLNYGPVDQ
AGESPAYQAIADAAKGWIARGVDGLRLDAVKHIYHSETSEENPRFLKMFYEDMNTCYKQQ
GHTDDFYMVGEVLSEYDKVAPYYKGLPALFEFSFWYRLEWGINNSTGCYFAKDILSYQQK
YAGYRSDYIEATKLSNHDEDRTSSKLGKSADKCRLAASVLLTSAGHPYIYYGEELGLYGT
KDNGDEYVRSPMLWGDSYTTSYTDKTDATVSKNVKTVADQQTDAHSLLNIYLTLTRLRNT
YPALAEGSMTKHPVYNESQEKDYKPIAAWYMTKDQEKLLVIHNFSGTAMQLPLTDKIEKV
LFVNGEAQQNTDNDNYTLKLGGYASVVFRLSN

Enzyme Prediction     

EC	3.2.1.1	3.2.1.135	3.2.1.54

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	80	540	1.3e-133	0.9968152866242038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11316	AmyAc_bac2_AmyA	6.28e-163	61	607	1	403	Alpha amylase catalytic domain found in 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.
cd11333	AmyAc_SI_OligoGlu_DGase	1.78e-69	64	599	6	427	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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.
cd11331	AmyAc_OligoGlu_like	5.34e-62	62	608	7	450	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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.
cd12961	CBM58_SusG	1.04e-60	222	331	1	110	Carbohydrate-binding module 58 from Bacteroides thetaiotaomicron SusG and similar CBMs. This group includes the starch-specific CBM (carbohydrate-binding module) of SusG, a cell surface lipoprotein within the Sus (Starch-utilization system) system of the Human gut symbiont Bacteroides thetaiotaomicron. It represents the CBM58 class of CBMs in the carbohydrate active enzymes (CAZy) database. SusG is an alpha-amylase, and is essential for growth on high molecular weight starch. SusG-CBM58 binds maltooligosaccharide distal to, and on the opposite side of, the amylase catalytic site; it is one of two starch-binding sites in SusG, the other being adjacent to the active site. SusG-CBM58 is required for efficient degradation of insoluble starch by the purified enzyme. Its starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. It may play a role in product exchange with other Sus components.
cd11334	AmyAc_TreS	1.37e-59	58	598	3	447	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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
QUT41573.1	0.0	1	692	1	692
QUT69415.1	0.0	1	692	1	692
QMW86069.1	0.0	1	692	1	692
AAO78803.1	0.0	1	692	1	692
CAZ78746.1	0.0	1	692	1	692

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6BS6_A	0.0	24	692	2	670	SusGwith mixed linkage amylosaccharide [Bacteroides thetaiotaomicron VPI-5482],6BS6_B SusG with mixed linkage amylosaccharide [Bacteroides thetaiotaomicron VPI-5482]
3K8K_A	0.0	24	692	1	669	Crystalstructure of SusG [Bacteroides thetaiotaomicron],3K8K_B Crystal structure of SusG [Bacteroides thetaiotaomicron],3K8M_A Crystal structure of SusG with acarbose [Bacteroides thetaiotaomicron],3K8M_B Crystal structure of SusG with acarbose [Bacteroides thetaiotaomicron]
3K8L_A	0.0	24	692	1	669	ChainA, Alpha-amylase, susG [Bacteroides thetaiotaomicron],3K8L_B Chain B, Alpha-amylase, susG [Bacteroides thetaiotaomicron]
1WZA_A	1.06e-60	64	687	8	484	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
7JJT_A	5.87e-58	64	681	33	508	ChainA, Alpha-amylase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8A1G3	0.0	1	692	1	692	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
P14899	3.85e-69	62	690	36	498	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P20845	6.16e-60	62	656	41	491	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
P39795	9.56e-36	62	691	13	558	Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2
Q45101	7.28e-35	62	666	9	535	Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1

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
0.000000	0.000001	1.000054	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002281_00983.