CAZyme Information: MGYG000002263_00577

Basic Information

• Species: Ruminococcus_E sp900543095
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp900543095
• CAZyme ID: MGYG000002263_00577
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1348	MGYG000002263_4|CGC2	145752.38	4.4298

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002263	1880579	MAG	Peru	South America

• Gene Location: Start: 100019; End: 104065 Strand: -

Full Sequence      

MKKNGVSRCTSLILSLCIILTCISFSFTSAVAVTVDDDNAVSLSSTAAGSLVEDDGFTWD
NATVYFLLTDRFKNGNKSNDHSYDRATDANGSPLSGWDTNPGTFHGGDFAGITQTIEDGY
FDDLGVNALWISAPYEQAHGYCDSGKGFAHYSYHGYYVLDYTETDANFGTAEEFETLVDT
AHKHGIRVIMDIVMNHTSYNTVKDMEDYNFGTLLPGASDFKYKLDNVSDVNSYIDYKSSA
SDWGRWWSNDWIRSGLPGYTEGSGDDYTMSLVGLPDFRTEQTQPVSIPPILKTKWTKEGT
YNQKVAKYGNSNTVTGYISTWLAEWVKNYGVDGFRCDTAKHVEKSSWNQLKTACVAALKT
WRQNNPDKPGANWKEDFWMTGEHWDHGVSYDEYYTQGGFDSMINFSTCGGESLAGSGVAN
IYQGYADSINTKDGFNVLSFISSHDETLARGNENTMIYNGSAFLLLPGGVQIFYGDESNR
PLYQGVAFDGYGGSGHSLRSDMNWDSLNTNVLAHWQKVGQFRNDHVSVGAGENIKLSATN
GVAFGRTYDKNGVKDKVAAAIGCSANRDVTIDVSSVWSDGQNLVNTYDQSSAIVTNGKVT
FNSGANGTILVQEPDGRPLLSVKGNPKFSGTQTLTVSLEGCDTAKCSIDGGNKFLVQNGS
TFTIGNTAYDGDTIKVTLEAENDRGTSSSSFSFLKVAQEEVVDPTTPTTPGEKAKLIVKT
WDGSAPYAYVWTGDSNALLGAWPGTKLTSKNADGNYYIELDTTDTYNVVLNNGSGTQSSN
ITNLNGTTTIEVTNSSYGTKIIGGGSDEPTEESVTIRVKPYGSSVPNLYVWDNSDTSIHG
SWPGAKLSEKDDDGNYIVTIPNKKSVNAILNEGSSQTPDITDISGDVTIEITSADYSTYK
LTRNETPLSGMKLLKKEAREVKILTASDYTSESWSTVSSAMTVADSLIAQGDAADAAAIE
SAVAQLQSAKTALKLATPTLSYAVIGQSTIKGYSAPEAKVTVTVDSKTYTAVADDITGEY
QVTASALARSSKIAVSAERNGISSGTLNYNMTSGNITGGDKPTQPTTEPTQPTTEPTQPT
TEPTTATQPTEPTSASSADKSLTVKATSNFFPSYTQKFDENTNTVTVTYYLKSDKSLLDS
QWVLSYDPTFLKFNKEKNSNVDCLMPCVSSGSYANLEPVEKDGTPIIGKIYGNSVNLRLD
KLKTSDGNEVAFVTATFDVLKSGSTTVDLFVDVITISDANDNDEAVVENGVIGSYTTPVT
RTTRVYEGQYQGATDYIYGDVDLNKIINVKDATYIQKYLASSASLTDIQKALADVNSDNK
ITIIDATLIQKYIAQLQSDSRVGQPYNK

Enzyme Prediction     

EC	3.2.1.98	3.2.1.1	3.2.1.60	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	107	478	2.1e-140	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	57	557	185	675	alpha-amylase; Reviewed
COG0366	AmyA	4.46e-46	62	511	1	398	Glycosidase [Carbohydrate transport and metabolism].
cd11339	AmyAc_bac_CMD_like_2	2.46e-42	63	525	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.
cd11338	AmyAc_CMD	2.49e-42	70	525	10	381	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.
cd00551	AmyAc_family	2.62e-39	63	474	1	253	Alpha amylase catalytic domain family. 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; and 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 this 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
BCN30960.1	0.0	55	1049	56	1052
QCT06045.1	0.0	1	886	1	888
QCT06087.1	2.35e-198	38	677	35	730
CDM67955.1	5.66e-196	24	774	37	797
CDM67952.1	6.23e-186	53	777	70	807

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	3.27e-31	58	572	5	409	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	5.99e-31	58	572	39	443	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	2.45e-25	58	543	6	383	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAO_A	2.73e-25	59	602	6	426	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
4JCM_A	9.22e-24	64	756	45	615	ChainA, Cyclodextrin glucanotransferase [Evansella clarkii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	5.12e-120	57	553	184	668	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P31797	1.19e-22	23	241	9	209	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
Q05884	1.31e-22	95	405	85	370	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
O30565	1.49e-22	64	235	33	201	Cyclomaltodextrin glucanotransferase OS=Brevibacillus brevis OX=1393 GN=cgt PE=3 SV=1
Q08806	9.77e-22	59	605	38	489	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 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
0.005399	0.992621	0.001049	0.000354	0.000284	0.000275

TMHMM  Annotations     

start	end
12	34