CAZyme Information: MGYG000000271_02221

Basic Information

• Species: Roseburia sp900552665
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp900552665
• CAZyme ID: MGYG000000271_02221
• CAZy Family: CBM82
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1676		184124.07	4.3584

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000271	4008876	Isolate	China	Asia

• Gene Location: Start: 67066; End: 72096 Strand: +

Full Sequence      

MRKLMKSFQKRQSIASRVLCFLLVLAMVVTMVPALGGGNSTVQAAENPTVRLYFEKPDDW
NIPAFNYWNESDVEVDNGDAEKVEVWTSQSRPAMLKDESTGYYYIDIRTNSISGFQIVNG
GTGVGNPAEKKFENCAIIDAINSATSDTSFYLLKNDNGMSWYLDKDKNQVLPEKEKAAAH
KVIIYFEKPENWKTPVINLWGGDFVLDNQGAGDASIAAWGNQDKPKLAVSEAENIYTVTL
TGTTISGFQLVDADTGAETQFDGQSEEVKAINAITTDTSIYYLRDGKGGMKWYKDADKSE
TLIEYKEAGYVSPEVNGREVTFRVPVEKTGDAASVTVPGGMNGWKQDSSDWELKKDETAG
MWSGTFTIAPGKYEYKFALNKTWDVSFSDPANNRVSGTNSVLIVPGLADGKADAMKGIET
ALPEKLTLWSEDGTSSEAPVTYSLKTANKDITLNGNSIIIGKSYTGQIVELTAKAENGQT
SDFVVNVTEKLYTYTIYYYDFDKTHMSENASDLWIWEKNGAGATEGTPFTATETLSDGNE
WLRAEIKLPYTDLQIIPRSKDEWKWQGDTVLYNNSATAENVTLYIVSNSNQAYTTLPELV
KPKSRSIMIEYDRPAKDYEGWNIFTWNSGFGSDVSVAFADINGKMVAKIPVKDSQADLML
SFCMRQSTTDNEWANKDGGDHYVTIPAGQSLVKAVFTQGEGITEVLPYNAGYEMDGANDT
IHFYYRNDTLAAENNLASLDGKVSVVVNGQTCPMTYDAANDRFGYDFTGVSTGDYYYYYV
VGGIEELDAFNSEKADYSGKECSVCHFKKANVSVTASLSQYAMDYNDNNVLSVELTAKDG
EGLETSEIAAITADLSELGLGKEFAIEPELMEGTISCLNTVAAGVKNIPVTVKDIYGNVY
TTATNVTVTERKKSAGDFDWDEAVIYFAVTDRFFDGDASNNDAYGVGDYNVGEKGGSSYH
GGDFAGLNQKLDYLKDLGVNTIWITPIVENITEDQHDNETDTATYGYHGYWASDFTKLNK
HLGKEQQFKALLDAAHSKGMKIMVDVVLNHAGYGREDYFNSILTDADGNSISMIRDSSNT
ISGDDKYDSLSDLPDFVTENKAVTDQLVAWQTEWMSKYNIDYYRVDTVKHVETTTWAAFK
NSLTKINPDFKMIGEYSGAGYANNAGELGTGTMDALLDFDFNDFAQNFVTGNISSVENSL
QKRNNAINNTSVMGSFLSSHDEDTLQYKLVNESKISEEEAYNLMKVAATLQITAKGQPVL
YYGEEIGQGGANNWPLQTNRRDFDWTELEKQKADSNSIYNHYKTMLAIRNAYTDVFARGN
RSTVAVSDADGYEVISRSYGNNTLYVGMNVKEAEKEVVIPVAESAGTVLKNLYDGKTYTV
SADQNVSVTIPAAKDGGTIVLTAETKTEPAPDNTTDDKKPDGKTTEDHNGNQQTSGNNSS
QVNSAVQTTPKQEEQAVAEVTVQEESFANVIEAVNKAKTGSKIRVNLLKTTKIPANVFES
IKGKDMNVTFQVSDQASWIINGKDITGNVTAPIDLGLVVGTSDIPKQKVTALADGNETIQ
LSLNYDGVFGFEGILRLSVGTDHSGKIANLYYYNETTGKFEYYQAAQVKEDGTVDFKFSH
ASDYVIVLNDTDMSQTTGSVIASPKTSDNTPIAAAVILLLFGCALMGTAYRKNKHF

Enzyme Prediction     

No EC number prediction in MGYG000000271_02221.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	962	1271	2.8e-112	0.9931972789115646
CBM82	182	304	6.1e-43	0.9919354838709677
CBM82	50	173	3.2e-42	0.9919354838709677
CBM83	605	700	8.4e-40	0.9791666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	7.05e-76	924	1312	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	6.27e-75	891	1346	143	677	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	3.33e-65	919	1311	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	8.86e-61	924	1309	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.
cd11338	AmyAc_CMD	6.04e-56	922	1320	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	1	1676	1	1674
ACR74843.1	0.0	1	1411	1	1291
CBK91127.1	1.46e-284	177	1408	43	1294
CBK93942.1	3.14e-283	177	1408	43	1294
QKH63022.1	3.26e-208	332	1409	57	1111

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	2.75e-46	920	1375	6	424	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	6.64e-46	920	1375	40	458	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]
6SAU_A	1.43e-42	920	1404	24	460	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]
4E2O_A	2.55e-41	920	1349	7	399	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAO_A	2.09e-40	919	1396	5	430	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
P25718	2.72e-42	902	1346	166	670	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q08341	2.85e-34	922	1391	133	575	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
Q05884	1.54e-33	959	1392	95	604	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P38940	2.80e-33	919	1383	130	569	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q10427	6.91e-33	920	1316	19	387	Uncharacterized glycosyl hydrolase C11E10.09c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPCC11E10.09c 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
0.003235	0.995451	0.000464	0.000377	0.000231	0.000208

TMHMM  Annotations     

start	end
13	35
1651	1670