CAZyme Information: MGYG000000354_01715

Basic Information

• Species: CAG-485 sp001701295
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp001701295
• CAZyme ID: MGYG000000354_01715
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1423		155294.19	4.9078

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000354	2905675	MAG	Sweden	Europe

• Gene Location: Start: 50271; End: 54542 Strand: -

Full Sequence      

MKSNGINILMKRSLWAAALTAGTFSLAADINAADATLNRLEIKIGGSNILQNFDPKTTSY
EIELDENTASLATFSAAPSSKEAVVDININGKSYTNHTLGSLQGGENVITYTVKNGTSTE
TYTIKLKTPETIRQEYFTWKNANMYFVLTDRFYNGDTSNDESYHRHRTAGGSDVGTFHGG
DIKGLTEKLDYLDKLGVNAIWITAPYEQMHGWTGGKNDAFAHYAFHGYYTLDWTFMDRNM
GTIDDMRRFVTEAHRRGIRVVMDIVLNHTGYCTLDDCVDYDFGNFNGTPAAGWLPSGGKF
TMWGDNEISFNADTQGKWGNWWGPWVRAFGDRSWGTSAGYVVPGNDDKTLSLAGLPDVVT
ERTQTVDIPSFLLKKWETEKGGDYDNYRLPNAEAWRTSGKGAPADYIINWLAAWVEYFGI
DGFRCDTAKHVELSRWNQLKNACKTALRNWRASDRADEYAKGWTDDFWMTGECFGWQHGD
TGYFTQGGFDSMINFAFNSTEGGTGRTPTVDDWSYYSGFCNGANGRQVLNYVSSHDTGLH
RPGDQKNVATMLLLCPGGAQIYYGDETSRPVIDGKGDAGMATRGDFNWDAVDNDVNLHWQ
KIGQFRRRNPAVGAGTQTSLGDNTYGRKFSENGYSNAVAIRLNTTAGQSYTVNTGDLFAE
GTRVMDGYNTSNSSVVSGGKVTMTASGPVLLIEEYGTVGGGPVPPIPPTPSKPTISASPA
DGTTFTDNITVSLFVSPATDIYYTVDGTEPSAASARYTTPLTFTETTTLKAYAANEAGQT
VKSFTYTKTQGGDDNDKYYVYFVNDRNWDVKVWAWNNSGNCNVNSTYPGDSMTEKNGVLY
WEAPEGKIPTQIIFSNNGGERAGNGDLDFVNGHTYKADGSHSLVQYGPVKPSISVSPAGG
TLKGNGTITITIGNEATSANGSFDSRPITVANGTTTLSVSDYLADGETAAMTISATNTAG
TTDYTCTFTRDDTEPVYTLSGDCRELSIYQIMVGSFQHGEGGASGYSDMWGPEGHRKNGN
LRGIINSLDYIKELGMNAIWMTPIFDSTNGNGGEKLQATGYFCTNYFKIDPKFGTEEEFD
ELIRKAHEKGIYVILDGVFGHHGGVTASSPNGNRIDVTTSQNVRGSDSGNVAYPASLEYF
KEVIRYWMERGVDGWRLDQCYQAYQGGHNYWHELRQEAENVAAERKARGEQWGTLAFMVG
EDWTSAPNITTTQQDGLKSVMDFDGKDNLVNLSSGVGSIGWFITSDAAARGYKDAGVNPT
VFLSNHDTSRVGDFVDVNSRPKELMTRHAAVAAYSGPTCTYYGDEIGDKSGNGNADNKAR
TSGRLSGFTPNEQMVHDYVAKVFKARAENPALWRGTASREDIGNTCVKITKTDAVTGNKV
IVIFSSADTNVSIGGTGLDLINGGNVSSTVNVKAWEPAFIKMN

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	180	567	7.6e-120	0.9972222222222222
GH13	1016	1307	1.8e-76	0.98125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	5.43e-167	112	625	154	663	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	2.88e-49	143	609	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.
cd00551	AmyAc_family	2.03e-48	988	1302	2	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.
cd11338	AmyAc_CMD	1.67e-47	988	1355	4	387	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.
cd11316	AmyAc_bac2_AmyA	1.83e-44	989	1355	4	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CQR56565.1	3.18e-163	137	861	60	770
QKH59997.1	9.32e-162	118	788	26	684
SBU87531.1	5.09e-159	134	788	41	684
BAF93484.1	2.69e-158	134	788	41	684
BAG70894.1	2.69e-158	134	788	41	684

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0H_A	7.08e-28	989	1358	138	509	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
1J0J_A	1.66e-27	989	1358	138	509	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]
5A2A_A	2.43e-27	138	615	5	370	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	4.08e-27	138	615	39	404	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	4.56e-26	134	620	2	376	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
P25718	2.79e-120	113	620	154	651	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	1.37e-29	172	618	90	532	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P38940	2.19e-27	989	1358	138	509	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
P21543	1.00e-26	139	684	744	1185	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P14899	1.74e-25	1019	1307	54	353	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC 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
0.000558	0.998604	0.000240	0.000200	0.000196	0.000175

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000354_01715.