CAZyme Information: MGYG000001814_00588

Basic Information

• Species: COE1 sp900753305
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; COE1; COE1 sp900753305
• CAZyme ID: MGYG000001814_00588
• CAZy Family: CBM83
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1521	MGYG000001814_2|CGC2	168897.97	4.0035

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001814	3758087	MAG	Denmark	Europe

• Gene Location: Start: 255037; End: 259602 Strand: -

Full Sequence      

MKRVKGSSTMRRSTAWILSAALVLSACPITADAEELTENGSESVAETSQAVDESETAEQT
EGERLNEGENTNVSEDEKEDQIQESSIEEDIQEESTQETSVEETTEEVPLEDDVVYLNAL
IGNVTRTCPTIGKDGEVTFHYYPQDGEKVESAYVKGSWSGDWSQYFYMTEDENGVWSATT
QLSLEKSYEYGIVVNDNWVGDATNPRNGGNSEILRNPVYNADGSVSIFYYPTGDEQVSLL
YKTAEDNNYHKVTMTQDAYHSALLSATVSEQGEYTYCLEVNGVQTDDLNCSNAAFHITKL
PEDDASVKSPVVNGNEVTFYYFAPTADSVSLAGQMNEWNPSADVMTYNEKTGFWSITRKL
ADGKYEYKFVINGSTWVTDPRNDLQSSGNSLVQVGEDKDPEQGAYQYTIYYLDANHKNVD
GASLWIWSDNENGMQYFFQDTEELADGNTWLKAEVSSDYEVLYIIPRAYDDWAWQDVDKS
YDNEQKQENVTLYLVNGDASVYTELPEIVERESRYVIVEYNRPAGDYDGWNIYSWNTGYG
SEVSVDFEKLGGKMVARIPVADTKESISFCMRRSETDNAWAEKDGGDHTVAIPLDQSVVK
ESFIQGEGVVGNLPYNIGYVTDVINSGVTFYYRDDTLFRKYEESTLKDHVELIWDGEKYP
MVYDEANERYYYTGKLTEGDHYYGYLVNGGLVTDRFNTETAVVNDTTYSAYTYTAFDADV
QAEVIPSEIDYNDNAVLKLTLQSDETQQIEAVEAYADLSELGQSSSFAIDTELMEGTIAL
KEGVSTGVKNIPVTVKDQYGNLYTTTAHVTVKDRDNDGFDWDEAVIYFAVTDRFFDGDSS
NNDAYGTGTYAPAEGSMYHGGDFGGLESKLDYLQKLGVNTVWITPIVENIEDTLNCDGYD
GQHNSGYHGYWASDFTKLNKHLGTPEELQELVDALHARGMKLMVDVVLNHAGYGTEDAFN
NTYIAGKSMLRDEFTTVKGDDKKDALSSLPDFVTEDEQVRDLLIAWQTSWVGNYDIDYFR
VDTVKHVDDTTWKAFKNALTYIDPDFKMIGEYAGAGYATNAGQLRTGQMDSLLDFDFNDQ
AISFVSGNLSTVENFMESRNAGIDNTATMGSFLSSHDEDGLMYRLMNEGNCVDADKAYAL
MKVAATLQITAKGQPVIYYGEELGQTGANNWPYQTNRYDMDWSIANDDNDMLGHYSKLLE
IRNSYTDVFAKGSRTTVAADDADGTLVASRSYGDTTLYVGFNINENESRTVELKLAANTT
YTDLYSNSQYQGDADGMVLIEIPAAKDGGTVVLKVGKAKPSDRPQIKNDSEENTGNNESQ
SSDAGITTGRVMTEPEYTSIDGTTVTGWDKVVDRAFADAQAQMVPLSDSAENAATVQQTV
VNLTLKSHSNMIIPAAVVAKMAASGATYVFSWEDGVITAYTAAVLAQVKGDLDMNIMVSK
DKDFGQGFKSFVLDPRKKAIYGVKLATVMSLGKENAGRTAFIFQRNLTTQGIEFLNSTTI
DEAGNVAVPCVDFTDFVILYQ

Enzyme Prediction     

No EC number prediction in MGYG000001814_00588.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	861	1168	2.1e-106	0.9931972789115646
CBM83	513	607	1.4e-35	0.9895833333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	3.40e-75	819	1218	185	659	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	7.05e-74	825	1205	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.
cd11319	AmyAc_euk_AmyA	1.86e-69	820	1204	5	371	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	7.58e-60	825	1180	6	367	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.
cd11338	AmyAc_CMD	6.43e-58	823	1213	1	388	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
CAJ20070.1	0.0	298	1519	301	1625
ACR74843.1	0.0	405	1293	369	1280
CBK91127.1	2.92e-244	311	1299	286	1294
CBK93942.1	2.92e-244	311	1299	286	1294
AYV73721.1	3.83e-209	298	1300	28	1111

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	3.34e-43	821	1255	6	408	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	4.52e-43	821	1280	7	439	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2B_A	7.69e-43	821	1255	40	442	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]
6SAO_A	1.37e-40	820	1301	5	433	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
6SAU_A	5.55e-39	821	1205	24	375	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	5.05e-46	819	1239	184	670	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q08806	1.24e-41	821	1282	38	485	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
Q10427	5.89e-41	821	1209	19	387	Uncharacterized glycosyl hydrolase C11E10.09c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPCC11E10.09c PE=3 SV=1
P19269	1.94e-36	821	1277	42	486	Alpha-amylase 1 OS=Schwanniomyces occidentalis OX=27300 GN=AMY1 PE=1 SV=1
Q02905	6.84e-36	820	1169	26	360	Alpha-amylase A OS=Aspergillus awamori OX=105351 GN=amyA 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
0.000419	0.371809	0.627127	0.000307	0.000200	0.000132

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001814_00588.