CAZyme Information: MGYG000001076_02127

Basic Information

• Species: CAG-411 sp000437275
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-411; CAG-411 sp000437275
• CAZyme ID: MGYG000001076_02127
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1213	MGYG000001076_225|CGC1	133406.54	5.244

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001076	3627630	MAG	Sweden	Europe

• Gene Location: Start: 36895; End: 40536 Strand: +

Full Sequence      

MVNEKLKKSLAVAMAASLVATSFPVASYTKVLQAHAKTANKNETSTLAGDTGVSKDDDGV
YKVTMDDTGKITADEDVAADVNTPFSWDNANVYFALTDRFYNGDTSNDHSYGRSEGEANA
ADYKNRTGTFHGGDLKGMTEKIEEGYFDKLGTNAIWITAPYEQIHGALCASKFKHYSYHG
YYVLDYTNVDANMGTEKELETFIDTAHEHGIRVIFDIVMNHAGYADAKTANEYGFGKLAS
NWKDIYYTWDESQYQWYNDYTGEAAQNGSQGMMDPSGDWTTNWWGSSWVRAIGSRFNGYD
GSEGDSNEITKCLDGLPDFKTETTNDPGIPGILKAKWTKEGTYDEKVASTKANMSARGLS
PSVTGYIATWLSDWVEKYGVDGFRCDTAKHIETKEWGKLSSACSKALETWRKNNPNKPGA
QWTDDFWMTGEHWGHGVGKDAYYTTGGFDSMINFSYQRNYNKKPQEMESIYSDYAQKINN
DSSFNVLSYISSHDTPSSRSDEFKYSLLSAHDGGTSGISLLLLPGGVQTYYGDESGRTEW
KSPSGCTGDQIVRSDMNWNSMDTARLEVWQKVGRFRRNHIAVGAGQHKKISDSPYTFSRT
YKGKATVGAETKTDYEDKVVVSLPGSAGTYDVDVSSVFDDGTTLLDSYSGEEYTVNGGKV
SATCDSKGVILLGEISDTTPKAKVTASVGDKSAYTEDKFTTTIKTENVTDATYQINDCTP
VSFTDSADITIGEDTAYEETTTVKVTGKSSIDSSEVSKTFTYKRSKEPTVGQASEGFYLR
MSKAAYEKASGQTGVPLVWIYDDKASYSGASWDSRDKMTLDETGEYYVWQKDTLTSEVYV
IVTAPDADTWRSVPDKKNGGTVKGTLELDPSKEYTDADQIKTITLATGEKATVTVKYVDS
QDKELKTITRVGAVDANYTVYAPKTLSTVSGYELAEGQDTSKTGKFTAEEQTVTFTYTKV
GEVITPTPEVKTPDPTVTPTDDVTPTPTEVVTTVEPTQEPTEAPTEGPTQEPTQEPTQAP
TQEPTAVPTETPKTLEAKVSTNPATKQIAGYAVKITGYAANGSGDYKYRFIVEDAYGNFV
YTKAYTSTASGTWKPRSAGEYVITVYVKDEKSGKITTASKDYKVTSALSVKKFDVKRLKK
LQYQLESLASGGAGTYKYQFSYTYKGKTKIIKKYSSKRICKNAFTKAGVYKITVSVKDKK
GKVVKKTKTVKVK

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	133	535	8.2e-133	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	3.58e-175	75	625	175	681	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	3.89e-38	91	579	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.
COG0366	AmyA	2.54e-37	90	574	1	396	Glycosidase [Carbohydrate transport and metabolism].
cd11338	AmyAc_CMD	2.76e-37	98	581	10	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.
cd00551	AmyAc_family	1.33e-36	92	531	2	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
CDM67952.1	3.77e-203	38	1124	26	1109
CDM67955.1	2.16e-198	38	842	23	791
QCT06045.1	3.58e-182	32	894	23	806
QMV42547.1	2.61e-181	67	862	22	755
CQR56565.1	2.28e-175	83	878	58	796

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	3.11e-20	83	621	2	408	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	3.25e-20	71	621	24	442	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]
4CGT_A	4.73e-19	74	658	1	478	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
6AIJ_A	2.62e-18	73	226	21	166	Cyclodextringlycosyltransferase from Paenibacillus macerans mutant N603D [Paenibacillus macerans]
4JCL_A	4.38e-18	76	226	3	145	Crystalstructure of Alpha-CGT from Paenibacillus macerans at 1.7 Angstrom resolution [Paenibacillus macerans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	3.28e-111	75	590	174	651	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	2.25e-21	128	556	93	478	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P36905	4.34e-20	92	688	391	937	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P21543	7.32e-18	87	669	744	1191	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P16950	8.02e-18	81	678	377	922	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu 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
0.004350	0.990737	0.003229	0.001090	0.000293	0.000247

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001076_02127.