CAZyme Information: MGYG000004431_00355

Basic Information

• Species: COE1 sp001916965
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; COE1; COE1 sp001916965
• CAZyme ID: MGYG000004431_00355
• CAZy Family: CBM83
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1524	MGYG000004431_1|CGC2	169834.65	3.9741

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004431	3494954	MAG	Israel	Asia

• Gene Location: Start: 335300; End: 339874 Strand: -

Full Sequence      

MKRVKGSSTMRRSTAWILSAALVLSACPVTAEAEELAENGSESVSETDQAMDESETAEQT
EDEHLNEGENTNASEEEKENQIQESSVEDDIKWEAAQEASTQEALTEETVEEATEEVSLE
EAAVSMYAATGNVTRTCPAIGKDGEVTFHYYPQDGEKVESAYVKGSWSGDWSQYFYMTED
DNGVWSATAQLSLEKSYEYGIVVNDNWVGDSTNPCSDGNSEILRNPVYNDDGSVSIFYYP
SGDEKVSLLYKTADDNYHEVTMTQDACHSALLSATVSEEGEYTYCLEVNGVKTDDINCSN
ASFHITKLMEDDPSVKSPVVNGNEVTFYYFAPTADSVSLAGQMNDWNPSADAMTYNEKTG
FWSITKELEDAKYEYKFVINGGTWVTDPRNDLQSSGNSLVQVGEDKEPEQGTYQYTIYYL
DTNHKSIDGASLWIWSDNVAGTQYFFQETEELTDGNAWLKAEVSSDHEVLYIIPRAYDDW
SWQDVDKSYDNEQKQENVTLYLVNGDTKAYTEIPDIVERESRYVIVEYSRPAGDYDGWNI
YSWNTGYGSDVSVGFEKLGDKMAARIPVVDTKESISFCMRKSETDNEWAEKDGGDHTVAI
PLDQSVVKASFIQGEGIVYNLPYNIGYITDSINGEITFYYRDDTLFRNYEEAALKDHVEL
IWDDEKYPMSYDETNERYYYTGKLTEGDHYYGYLVNGELVTDRFNTETAVVNGTTYSAYT
YTTFNVDIQAEVTPSEIDYNDNAVLKLTLQADEAEQIEAVEAYADLSELGQSSSFAIDTE
LMEGTIALKEGVPAGIKNIPVNVKDQYGNHYTTTAQVTVKERDNDGFDWDEAVIYFAVTD
RFFDGDSSNNDAYGTGNYAPAEGSMYHGGDLAGLESKLDYLQNLGVNTVWITPIVENIED
TLDCDGYDGQHNSGYHGYWTSDFTQLNKHLGTQEELQELIDALHARGMKLMVDVVLNHAG
YSTEDIFNNTYIEGKNMLRDSSTTVKGDDKKDALSSLPDFVTEDGQVRDLLIAWQTSWVS
NYDIDYFRVDTVKHVDDTTWKAFKNALTYIDPDFKMIGEYAGAGYATNAGQLRTGQMDSL
LDFDFNDQAISFVSGNLSTVENFMESRNAGIDNTATMGSFLSSHDEDGLMYRLMNEGSRV
DSDKAHALMKVASTLQITAKGQPVIYYGEELGLTGVNNWPYQTNRYDMDWSIANDDNDML
GHYSKLLEIRNSYTDVFAKGSRTTVSADDANGTLVASRSYGDTTLYVGFNINENESRTVE
LKLAANTTYTDLYSNSQYQSDADGVVQIEIPAAKDGGTVVLKAGKAKPSDRPQIKNDSEE
TANNESQDSDSSTTTGKPANEAEYTSLDGITVTGWDKVIDLAFADAKTQMASIENPSSMQ
QMVVNIALKSDFNMVIPEEVVAKMAASNATYVFLWENGVVTAYTASALAQIKGDLDLNIM
VSKDKDFGQGFRSFVLEPRKKTIYGVKLATVMLLGEENAGKTAFIFQRNITTQQMEFLDS
TIIDEAGHVAVPFVDFTDFVILYK

Enzyme Prediction     

No EC number prediction in MGYG000004431_00355.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	869	1176	1.6e-104	0.9931972789115646
CBM83	521	615	2.3e-36	0.9895833333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	4.89e-76	833	1213	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.
PRK09505	malS	5.90e-75	827	1242	185	672	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	3.07e-70	828	1212	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	2.00e-59	833	1188	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	6.45e-58	831	1221	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	317	1522	312	1625
ACR74843.1	0.0	413	1301	369	1280
CBK91127.1	1.24e-238	242	1301	190	1287
CBK93942.1	1.24e-238	242	1301	190	1287
APT18363.1	1.17e-209	335	1304	166	1197

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4E2O_A	1.12e-42	829	1284	7	435	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2A_A	2.75e-42	829	1263	6	408	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	6.24e-42	829	1263	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]
6SAV_A	6.68e-39	828	1296	5	430	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Rhizomucor pusillus]
6SAV_B	9.01e-39	828	1296	5	430	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Rhizomucor pusillus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	2.82e-46	827	1247	184	670	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q08806	9.20e-42	829	1290	38	485	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
Q10427	2.63e-40	829	1217	19	387	Uncharacterized glycosyl hydrolase C11E10.09c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPCC11E10.09c PE=3 SV=1
Q05884	2.95e-39	855	1314	84	625	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P19269	4.43e-37	829	1270	42	464	Alpha-amylase 1 OS=Schwanniomyces occidentalis OX=27300 GN=AMY1 PE=1 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
0.000737	0.291100	0.706975	0.000654	0.000341	0.000174

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004431_00355.