CAZyme Information: MGYG000000245_00822

Basic Information

• Species: Roseburia sp003470905
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp003470905
• CAZyme ID: MGYG000000245_00822
• CAZy Family: CBM83
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1651		181263.74	5.0779

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000245	4145433	Isolate	China	Asia

• Gene Location: Start: 262180; End: 267135 Strand: -

Full Sequence      

MKNKNILKKTAKKSISWLLILGMLITLPQTPGAVSAAAAGLKTETETVHAEEVETETGVM
NANEAETETEEVETETETVHAEEAETENATVHAENAVTKTDLTVHFKNENNWDKVYVKFG
AGDSWAAVKNFEYCKNYDYGGLLKENSKNKGWYSFKVEKDDALDLNGLFNAGAWGDNNQT
ENFKIEITSETMEVWITGKTVSEEKPESWATGETVSAPVDVTPVSGVESPVLGKDSSVTF
NYEISADKLGTEKLYLMGSLTDWTDGYEMTDEDKDGIYSITVSDKPAGIYEYKFKYGSNW
VTDPANKNYSNGNSKVVIPGLGSDTLEAKVGVTTALPDTLKYYTADGTVADVKPEYTLET
SMDGVSIDEGKLTLSDDVTATDILVIASYKVGDDVYKSTVYVNVVMAQYNYHIYYYADNE
DRVTADSAALWLYGDGVNGTLHDFTDTTEIDGYTWLTYTWTTSLDNISIIAKNPGSEWTW
QAATVNYKNADAAEDVDVYVIHGDTTAYTTIPDIKEATQKHYVLVEYRRNNADYDGWNIY
TWDSGYDDTVKFVENQGSWIAPVRVSSSKESISFCMRHSTDDNEWESKDGGDHMVKIAAG
QRMTKVVFEEGKGIVSYYPDNQGYELDTKNGKVNLYYRDDDLYAENKAGEIASVKVVYDD
NEYEMTYNANTQRWEKTDVVLTEGEHHYYYKVKAAKDSEEVIKLDLFNANKEAGDNPGYS
IFEYYKFNATVSGTMSGKTMDYGDNNVLTVSVNADKINGDTAFKASAVTADLTALGGKKD
FKLDPALMEGSIAVKEGIQAGTYELPVTVKDQYENEYTGKVSVEVTERNKGTDFDWDEAV
IYFAVTDRFYDGNTTNNDAYGTGDYNKDPATGSLSYHGGDFAGLTQKLDYLSDLGVNTIW
ITPIVANEMKKGLATDLPGTLSYGYHGYWASDFTTLNKHLGTEEEFKTLLDSAHKKGMKV
MVDVVLNHAGYDTENYFNSMLNGKNMIRSGADLIEGDTKKGPLSNLPDFMTEDPDVRNLL
VEWQSAWVSKYDIDYYRVDTVKHVDDTTWAAFKNALTRIDPDFKMIGEYAGAGYASDTGT
LRSGEMDSLLDFDFNDQALAFVKGDIDGVEIFMEKRNAAIDNTATLGAFTSSHDEDGLMQ
KIIDEGYTKDQAYNMFKAATVLQMTAKGQVIVYYGEEIGQYGKDNYPYQTNRYDFDWSQA
QNADGSLNTDNEMLVHYQKLLTARNKYSEILAKGDRTKVAGGSKEGYLVFEKSYQGKNVY
VGINLTDTPVVVDKLAVTGKGYKDAYADSKVTEADGTVSFTIPALKAGGTIILGVQEETI
EPDKDIEANAITLNKTDLTLKKGKSYTLKATVTPENSVDKTVTFKSSKSSVAKVDANGKV
TAKKAGTATITATTKNGLKATCKITVTDPATKVYLTPAMSIKKGSSVKLTASVFPKTTTD
KLTWSTSNKKVVTVTKRGKIKGIKTGTATITVKTSSGKKATCKVTVVKSNKKSAGIKLSA
KKLTLKQNATKQLKATLDKNATDKVTWSSSNKKVATVDKNGVVMAVKKGTVTITAKTSGG
KKATCKVTVKVPATKVKLNKTKATVAKGRTLTLKATMTPSSSTDKLTWTSSNKKVATVDK
NGKVKALKKGTVTITVKSASGKKATCKIIVK

Enzyme Prediction     

No EC number prediction in MGYG000000245_00822.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	879	1183	1.1e-101	0.9931972789115646
CBM83	520	611	1.2e-23	0.9791666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	1.12e-78	834	1261	185	677	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	1.91e-78	840	1227	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	8.65e-61	835	1225	5	370	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	1.20e-57	840	1186	6	362	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	1.90e-54	838	1235	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	2.06e-292	225	1325	308	1413
ACR74843.1	5.86e-277	397	1322	357	1289
QKH63022.1	1.61e-224	228	1326	38	1116
QJX64947.1	2.59e-222	227	1313	24	1090
AYV67921.1	7.35e-222	227	1313	37	1103

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.70e-50	832	1296	2	432	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	1.76e-50	828	1296	32	466	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	2.22e-45	836	1266	7	401	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAU_A	1.34e-36	836	1177	24	335	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]
6SAV_A	1.32e-35	832	1179	2	317	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	2.03e-41	819	1247	169	657	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q08806	2.26e-34	836	1185	38	372	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
P21543	1.36e-33	835	1264	743	1144	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	2.61e-33	876	1320	95	625	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P38940	3.67e-33	835	1267	130	539	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 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
0.000670	0.998509	0.000249	0.000191	0.000178	0.000166

TMHMM  Annotations     

start	end
17	39