CAZyme Information: MGYG000001076_02287

Basic Information

• Species: CAG-411 sp000437275
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-411; CAG-411 sp000437275
• CAZyme ID: MGYG000001076_02287
• CAZy Family: CBM83
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1837		202843.06	5.2101

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001076	3627630	MAG	Sweden	Europe

• Gene Location: Start: 11008; End: 16521 Strand: -

Full Sequence      

MKVSKKLKSIISAILVIAMVITLLPNGQIIKAAEGMNINIHFYDKDKAYAGKVYMQYWQP
GTATVSTKKEHFDSWDVDRYPLEDESATQGEDWYGLNLQGSVQGFQFLDETGKQNTNGTV
YLPGMKEYQGDLYYMDGKWYTENPVKNKDAKEADLNVEAKEVFYLVGDIAKAKWEATDTT
YPLTKNADGTYSIVLKDIAAGNYAFKVLQDPENFAWDKAWGGEGSGGNYELTVKSKSNVT
ITMDPADTTHKLTVTTEAAENSDVKSPIYNGDGTITFQYVSNTSGASIGVRGNVKTTKKK
SVIKAQQMETLKDGSYLYVATSAAITEPGLYRYNFYELTDKGELGKELGDPNSTTLYSGT
GAFVRNPVISSIGLVTIYYPYDGKDAQVYYKSTSSSNKEVLKPGDKVTKTTAEEYGYTVV
DMKEDSDFSGGGMYSAKFYDKEDTYSYVLVKDGVVVEDVCNYNGNTFKETNVDEIALTVD
SPVVMEDGTTVKFMYYDKDFTSGTLSVAGEFNNWTKDVDMMTMDKDAKGVWSIEKEGFTP
GIYQYKFVQNGSNWMADPLAKMSGTSDGNSAFVVPGFAPKTALQVQKGKTLTLPKTVLKY
TANVKKAEEAEVTYQLKDETQKGVSLKDGVLSVDEDYKEDSIQLILTDGKVSSTCTVEAV
GKMYTYTIHYYAEDNSTYANRDLWIWEQSGKAYNTGYTFNKDDYKDPKGRTWATATYSFP
TNAINVIVRSKGEWSYEESTRAITLPEGQESGEFWILQEGNKAFSEYADEFDTGVKRYVV
VEYDRPNKDYQGWNLYTWNASKAYNEISNFFTEVNGKYQTTFTIDELTSNVGYLLRSGTP
TDSSWSGIEKDMEGDRSIQTPVDQKVIKVKLKQGSLEAEYLPFNKGYELDPDNKQIKFYY
RDDDLYLKDELETLKSVKLEVAGKTVDMTYNKDNQRYEYTLKNAVNGTYEYCYDVTPASG
SAVTVLDAFNSNKNEAGTKSVLVYKDLTTKVAVTCTNSSISYDENTLIGVSLDNSEVKVQ
EAYADLTALGGSAKTEIDTTLLTLSIGVKDSVSVGTKTVPVYVKDQYGKTHKGSVKITVK
QRIKTDDKDFDWDESVIYFMVTDRFCDGNKVNNDAYGVGDYDPNGPSSYHGGDFAGVTSK
LDYLKNLGVNTIWITPIVENVLEAQTATADGKNVPSYGYHGYWASNFEALNKHLGTVDEF
HTLIDEAHARGIRIMVDVVLNHSGYGTKDSSQFAGMYRENNVEGNDILGEQDGLPDFATE
REEVRNKLISWQKAWVSEIGMTSKGNTIDYFRVDTVKHVDKTTWTAFKNAMTDYSSKFKM
IGEYYGASATDDFGMLHDGKMDSLLDFSFNDMATLFVKGKLESIEEQMETRNSTMDNVGT
FGSFLNSHDEDGFKSNLQQSYSEEQADALSKVAASLSITAKGQPVIYYGEEIGLTGENNY
PYQTNRYDMKFDNLDASQQAMLTHYQTLLKIRNDYSKLFAKGSRSYVAGSDKEQYMAFKR
SYKGESAVVALNITDSSKKVTMTVKEFAGQVVTDVYSGKEYNVDKLGKVEITIPANSNGG
TAILVVAGQKATDKITIANLTKAKTNGVSLIANGKNEKTGDNNISWTFSANDLKLASTSA
LKDINVTATVSNASSNAKVAAILKKDSKNKNGALISLAHTGTLGVNAKVKVDVSAQSEIA
YGSKVYVYRVSGSKLQQIVNDTAKVTKDGYVTLYVGQGGDYVLLAKKPSSAVITTLPNQI
KVTAASSVKAGKKTSISVAVPSVSMKKVSAFNEDSMKKLQSAQVGVKVIYATSNKKVATV
SSTGVVKGVKKGKCTISITIRTSDGQKKIVKKKVVVK

Enzyme Prediction     

No EC number prediction in MGYG000001076_02287.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1132	1437	1.8e-103	0.9931972789115646
CBM83	776	875	1.4e-18	0.9895833333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	4.12e-79	1094	1475	2	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.
PRK09505	malS	4.94e-69	1090	1510	185	678	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	3.28e-62	1091	1473	5	370	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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	2.12e-58	1096	1472	6	387	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.
cd00551	AmyAc_family	2.97e-54	1096	1428	1	253	Alpha amylase catalytic domain 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; and 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 this 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
QKH63022.1	1.99e-258	480	1569	38	1108
AYV73721.1	3.39e-256	479	1569	37	1108
AYV67921.1	6.67e-256	479	1569	37	1108
QJX64947.1	1.24e-255	479	1569	24	1095
SQI61915.1	2.49e-237	478	1569	37	1116

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.06e-50	1092	1544	6	435	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	2.73e-50	1092	1544	40	469	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]
4E2O_A	9.22e-47	1092	1544	7	437	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAU_A	3.15e-38	1092	1567	24	459	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]
6SAO_A	2.56e-36	1091	1524	5	418	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q05884	2.81e-38	1121	1571	87	617	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P21543	6.77e-38	1091	1553	743	1186	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P04830	4.27e-35	1087	1517	34	468	Cyclomaltodextrin glucanotransferase OS=Paenibacillus macerans OX=44252 GN=cgtM PE=1 SV=2
P25718	5.59e-35	1081	1502	174	657	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P08704	8.23e-35	1091	1528	39	513	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt 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
0.000265	0.999074	0.000198	0.000160	0.000150	0.000138

TMHMM  Annotations     

start	end
7	29