CAZyme Information: MGYG000000389_01506

Basic Information

• Species: Roseburia sp900550935
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp900550935
• CAZyme ID: MGYG000000389_01506
• CAZy Family: CBM83
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1556		170331.8	4.7843

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000389	2762523	MAG	Sweden	Europe

• Gene Location: Start: 3291; End: 7961 Strand: +

Full Sequence      

MRNQRILKKAAKKTISWLLILGMMVTLPQLPVDMVYAAETNEAVIEAETETEEAGLQDTE
TTETETAAVEEEEASEEAENKAAATSTNVTIHFKNENNWDKVYAKFGAGDSWDAIANYEY
CKSTAFGGVVNANSKNTGWYSFKVVKSDTLDINGLFNSGAWGTGKQTENFKVEITDDTME
VWITEDWTTKTVKVSSTAPSGWVAGETATAPVDPATLSSVKSPVLNVDGSVTLNYEISAD
KLGTSKLYLMGNLTDWDTGAEMTDEDNDGVYSITITDKAPGTYEYKFKYGENWVTDPANT
KFSNGNSVATIPGLGEDGIEAVIGEKAALPETLKLYAADGTVSDVAVSYSLSSAVEGVTL
SGNELTLSDAVTAASFEVTATYQDYTSKVTVSVVAEQYQYHIYYYADNPDRVTADSAALW
LYGKNVDGALYNFTDVEEIDGYTWLKATWTTSLSEISIIARNPADWSWQAATVNYKNTQK
EKDVNIYIIHNDTTAYTTAPNVEEATQKHYVLVEYKRADNNYDGWNIYTWDNGYDDTYTF
EDCNGSKIAAVRVAASKENISFCMRHSTAENAWESKDGGDYMVTITPGQRITKVLFEEGK
GIVSYYPDNMGYEMKDGKVSFYYRDDEKFIENKAGDYTSVKVVFDDKTYDMAYNTAEQRW
EKTGLDLTEGKHHYCYQIKTETEETTVTDSFNTEKETVNGQEYSVFEYYRFDASVAGAFS
QSTMDYADNNVLKVNVTAGQSAGGSTLKAADVSVDLTAVGGPAQFKIKPELMEGTIAVKE
GTAAGTYALPITVTDQYGNTYTGSASVEVKARDKGDDFDWDEAVIYFAVTDRFYDGNTAN
NDAYGVGDYNTDPATGSLSYHGGDFAGLTDKLDYLSQLGVNTIWITPIVANEMKAGLDTD
LAGTLSYGYHGYWASNFTALNKHLGTEEEFKTLLDSAHARGMKVMVDVVLNHAGYNTEDY
FNSQLQGKDMIRSGENLIEGDTKKGPLSELPDFMTEDEDVRNLLVEWQSSWVSKYDIDYY
RVDTVKHVDDVTWAAFKNALTKIDPDFKMIGEYAGAGYGSDTGTLRSGEMDSLLDFDFND
QALAFVKGNIDSVENFMENRNAAIDNTATLGAFTSSHDEDGLMQKIIDEGYTEEQAYRMF
YAATSLQMTAKGQVVIYYGEEIGQYGKDNYPYQTNRYDFDWSKAQLADGSINTGDAMLSH
YKKLLAIRNEYSEVLAKGDRVKVAGGDTDKYLVFKKSYQDQNVYVGINLKDEPVTISGLS
VAGSGYEDLYGNAEVTEAADGTVSVTIPALSAGGTVVLAQQTSEDDTVKEIHAKKVYLTP
SLCLKKGATAKLQATVFPKNMTDELSWSSSNKKVVSVSKTGKVKALKTGKATITVKAANG
KKATCKVTVVKKNKKAASIKLNKKKLTLKKGGYTQLKATVTKNTTDKITWKSSNKKVATV
DKNGVVTGLKKGTATITVKTSGGKKATCKVTVKAAKQTVKVKLNKTKVTLAKGKTVTLKA
TVTPSSANEKLTWSSSNKKVATVSKKGKVKAIKKGTATITVKTSSGKKATCKVTVK

Enzyme Prediction     

No EC number prediction in MGYG000000389_01506.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	863	1167	4.2e-102	0.9931972789115646
CBM83	508	599	5.8e-22	0.9791666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	1.59e-76	824	1211	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	4.28e-75	775	1245	131	677	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	5.73e-57	819	1209	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	5.69e-55	824	1170	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	7.61e-55	822	1219	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	2.12e-304	233	1310	320	1414
ACR74843.1	1.41e-275	81	1315	41	1297
QJX64947.1	8.58e-215	222	1298	26	1090
AYV73721.1	1.73e-214	222	1298	39	1103
AYV67921.1	4.75e-214	222	1298	39	1103

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	3.37e-46	820	1258	6	410	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	8.12e-46	820	1258	40	444	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	9.41e-42	820	1252	7	403	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAU_A	8.62e-34	820	1211	24	375	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]
6SAV_A	1.96e-33	819	1287	5	427	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	5.98e-37	800	1214	166	643	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q08806	1.29e-32	820	1169	38	372	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
P38940	1.91e-32	819	1256	130	544	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q05884	1.12e-31	860	1292	95	607	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
A0A7U9P668	4.57e-31	819	1256	130	544	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 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
0.001511	0.997528	0.000334	0.000213	0.000191	0.000181

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000389_01506.