CAZyme Information: MGYG000000555_00893

Basic Information

• Species: Cellulosilyticum sp900556665
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Cellulosilyticaceae; Cellulosilyticum; Cellulosilyticum sp900556665
• CAZyme ID: MGYG000000555_00893
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1182	MGYG000000555_66|CGC1	131858.26	4.4117

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000555	2866181	MAG	China	Asia

• Gene Location: Start: 5130; End: 8678 Strand: -

Full Sequence      

MKKSLLAALVSMSFVCESLFSPYLMASPLNNLTYATTSSTTLNTLNDTSNANFSWDNTTV
YFVLTDRFVNGNTSNDNSYGRVKTDSWGKNIGTFHGGDIAGLTQKLNDGYFENLGVNTIW
LTAPYEQAHGFVGGGSEGDFAHYSYHGYYPLDYTMMDKNMGTIEEMRKFVDTAHEKGIRV
VLDVVMNHVGYLTLQDMADYNINPTNTSLSNLANWRPNKNAGETWHSYHSTLLDYDGHAS
EWAKWWSSGWIRAGVAGYTAGDGSDTKQNLSGLPDVKTEVTSNQGLAPILKTKWAKEQSG
YDAWILPAAKNLRRDLGISPSDYQVKWLAAWVKEFGIDGFRVDTAKHVDMFRWAQLKDAC
TEALQEWRQNNPNKPGADWDEDFWTTAEVFDHGANKSNYHTSGKFDSVINFCFPKNGNIG
AIDSTYQSYANSINGSDDWNVLSYISSHDKGLARGNMIDLGSTLLLSPGGIQIFYGDETN
RPAGECGSDKDQGSRSDMNWSNMDKSTLTHWQKIGQFRNNHIAVGAGSHTKLNASPYTFQ
RSYHKNGIDDDVIIVLGASGPTTINVSSVFADNSVVRDAYTGATATIQNGNVTITPDANG
VILLELKEFSPLPKIAISPTSSTTPKKYYTDSLEVTVTLKDSLYGAYRINNGAWVPFQDK
AVITLDKDLPLETTTKIDVKSSNDYGTVEQSASYLKTVIKPATVHFYKPAAWSTPYVYYY
TDDESTNTVKWPGVQMTDEGGNWYSFTTSDLESAYFIFNDQKNQVPGVDEEGFNISDEQW
YKNGTWTPIKPPTQTPPTVKEGELKLFMYKPINWGTNLNAYVYNENSSDVATIASWPGVQ
MNNEGDDLYSITLDKKWLNSKVIFNDGQNQYPAKTGLTVDASRGYIDGSWELCPVEQDNT
LSLSISPENTTFSDTLTLTLNAKNATSATYQINDGEEIPYTDGEEIVIGEDATDNEAITV
TLNVTKDTDTRSETYTYTKIPNTSLKAYFDNSTFNWSNLHAYIYTETASGVDMVEAWPGV
SMNYEGNDIYSYELPEGWENARVIFNNGGSNQYPEASQPGLELTKETPAMIYQNGDWITY
EGTVIPDSKKFYFDNSTYNWSTVKAYIYDESNGNVMQIQNWPGTEMTNEGNNIYSYTFTK
DWNDPKVIFTNGSIQIPAQGQTGFSLENNMILENGIWTNFNK

Enzyme Prediction     

EC	3.2.1.98	3.2.1.60	3.2.1.-	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	97	479	1.2e-139	0.9972222222222222
CBM26	703	768	7.3e-20	0.9066666666666666
CBM26	987	1057	2.1e-18	0.9066666666666666
CBM26	809	878	9.3e-16	0.8933333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	51	555	183	678	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	5.81e-43	59	521	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.
cd11320	AmyAc_AmyMalt_CGTase_like	5.11e-32	59	520	6	389	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	2.39e-31	57	523	1	383	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.
cd11340	AmyAc_bac_CMD_like_3	1.99e-30	59	498	5	370	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADZ82879.1	0.0	3	1178	10	1064
QEH68420.1	0.0	3	1178	10	1157
AZK49196.1	1.26e-259	50	791	126	860
CQR56565.1	3.76e-247	53	798	60	804
QMV43648.1	8.44e-247	11	798	11	792

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	2.99e-21	55	597	6	439	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	4.25e-21	55	597	40	473	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]
1CYG_A	5.02e-20	60	602	14	473	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
6CGT_A	3.50e-19	48	591	7	467	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
1CGT_A	4.62e-19	48	591	7	467	ChainA, CYCLODEXTRIN GLYCOSYL-TRANSFERASE [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	4.79e-132	47	555	179	671	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P21543	7.51e-25	42	595	731	1185	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	2.53e-20	92	676	93	691	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P31797	4.27e-20	6	602	5	504	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P14014	1.18e-18	48	591	41	501	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA 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
0.009929	0.984172	0.005062	0.000292	0.000244	0.000260

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000555_00893.