CAZyme Information: MGYG000000977_01371

Basic Information

• Species: Clostridium sp900539375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900539375
• CAZyme ID: MGYG000000977_01371
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1278		141370.99	4.2462

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000977	2927434	MAG	Australia	Oceania

• Gene Location: Start: 63456; End: 67292 Strand: +

Full Sequence      

MEKLKNHGVKHKLSIIMAVIFFLGLIPVKNLIATATEPLGPVVNPDGTVTISYQYDGDEL
YINGSFTNWQFTKMTKGENNIFSYTTEVLSPGSYEYKFSPEAAWGKDFNQDGETGGAPNS
KFEIKSLGASLNGDGTATFRVRYDGDELYLVGSMNNWTEAIKMTKGTDGVFEITINVEEG
KTYEYKYKVTADMSDWTTGSFNQEGGEGNSSLKVPGKVTAYAPIFNGDGTVTLSYADVSA
SSVYLAGDFVNEVWQPTGLAMTNNGEGLWTITIGQDELSKYSTGDQVQYKFVVNGTQWVT
DPSNTEIVNGNSVFTYQKFDSASAPILNADGTVIFSYADDSASSVSVAGDMNGWDANKTP
MTKNEFGVWTTVFEPVDGTTQIVYKYVVDGTNWILDPNALDSIGDGFGGSNSVFNLTNQV
VEHKKVILKYVREDGNYDGWCLWNWSTGLKEGKVDFEVKDGVAVATFDVSDDCSSVGFKI
MKNDWAEVDIDSDRYIEVDPNSMVTKVVVTSGQLDMFVVPQVTELEMNPGRVDFEFRDND
LYKEDAQETVESVKTILTYEDGTVTEIPMEYDSKNEYFKGSYLNDNLKEGTYSYKFVEVV
NGEEKVSEEKTFEYKVRDISVKASVDPYNVTSSDNAVVSVELTGKNIDKDSIRKVYMDLS
SVGGKAETKMDLSLLDNGKFRQTIAITDNTTAGVKNIPVVVVDVNGQEHKTTFEINVKTK
VSSGKNLDFDFDEASIYQILTDRFLNGNTSNDDPNGNNYDKTAPYTYHGGDFAGITQKIK
DGYLTDLGINTIWISPIVENTDVSQGYEEEGGQYSYHGYWAKDFTILDPHWGTMEEFKEL
IDVAHENGIKIMVDIVINHSGYGTEEIFKDMLRSEDGGDIYTNASSGLPDFRTEDPAVRA
KLITWQLDWLNKAKTEKGNTIDYFRVDTVKHVEDATWKELKSELTKANTQFKMIGEFYGA
DYNTDGGQLQSGQMDALLDFSYKNYATNFVNGKIEDASKTLDERASKLNNSYLLGQFLSS
HDEDGFLTRVDNNLGKQMAAASLQITDKGIPVVYYGEELGMTGLNGMENKDGNRYDMDFS
KATDDNVVYNHYKKLLNTRERYVSIFAKGDRKTIAGSDEEQFSAFERSYNGNTILTLINV
SDEANNIKVKTSFKEGQVLVDAYNNDKEYVVSKDGEVAIELVGMQEGGTAILAPKGLDED
INNDNPSDNDNPSDNDNPSNNNNNNSGNNNSGSNSNNNSGTTSNGNGTKTGDTNTVVVFV
SIVLLSAGVIVFLRKKRA

Enzyme Prediction     

No EC number prediction in MGYG000000977_01371.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	770	1064	6.9e-102	0.9931972789115646

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	7.25e-74	735	1102	4	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	2.30e-64	736	1095	7	383	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.
PRK09505	malS	1.54e-63	729	1136	185	677	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	2.68e-60	735	1099	10	369	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.
cd11338	AmyAc_CMD	3.11e-60	733	1102	1	381	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUD74111.1	1.81e-251	424	1195	1609	2419
ASY51150.1	6.73e-251	424	1195	1609	2419
AWS25652.1	6.73e-251	424	1195	1609	2419
SQI04167.1	7.13e-251	424	1195	1609	2419
ABG83674.1	1.28e-250	424	1195	1604	2414

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2B_A	2.25e-50	720	1195	29	485	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	2.98e-50	733	1195	8	451	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	1.07e-43	732	1178	9	445	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1JF6_A	2.51e-42	733	1181	130	573	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1WZK_A	3.38e-42	733	1181	130	573	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZK_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q08751	3.33e-41	733	1181	130	573	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
P21543	4.75e-41	721	1181	734	1186	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P31797	2.56e-40	718	1145	26	468	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P31746	5.64e-40	711	1156	25	475	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1-1) OX=29334 GN=cgt PE=1 SV=1
P27036	5.66e-39	689	1177	3	498	Cyclomaltodextrin glucanotransferase OS=Bacillus ohbensis OX=1481 GN=cgt PE=3 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
0.010606	0.988147	0.000509	0.000276	0.000212	0.000211

TMHMM  Annotations     

start	end
13	35
1256	1273