CAZyme Information: MGYG000000356_00766

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; VUNI01
• CAZyme ID: MGYG000000356_00766
• CAZy Family: CBM83
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1520	MGYG000000356_5|CGC3	167166.2	4.2989

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000356	2991584	MAG	Sweden	Europe

• Gene Location: Start: 108881; End: 113443 Strand: -

Full Sequence      

MKKKHIGRRLSSLLLAIVMILTLIPGVPIRSYAEGSSENVSITMHFQSEDAWEQVCTKIA
QGESWGAIPGYVYANSWPGAAVEEDSQNAGWYSFTITMNAGEQFNCIFNNGNNGKQTENI
CFTPDKSGTEKWVVQKTDKTQISDSAPAGWKTSTSNAPVDPSANSKFKSPVINSDRTVTF
QLDATGTYKNTSEVRLMGTVGGTDWETGLQMEKDGDVFRVTTGVQNPGIYEYKFKCDADW
ITDPLNAEIANGNSKLVVPGLAGESKTVKAGEKTALPETLKLYAADGSVTDETVTYQLKD
SALGKTVTLENGNILVPAGSGLTQVELTATAGSNSADVTVQVVEKTYTYNIYFYDSIEAH
MSTDAADIWMWENNGKNLPVGKFTELVTLDDGNQWLKATVTTSATDIGFIPRSAGEWKWQ
TANFNYNNKDKQDEVSLYVVNGDETVYTKLPEIKEARNRYVVVEYDRPAGDYDGWNIYSW
NSGFGSETEIYSQEINGKHTMIIPVKDSKADFTLGFCMRKTEEDNAWAEKDGGNHEVVVP
ADQNVVKVKFEQGKGITETLPMNKGYEMNGNESEISFFYRDDMLLTENNESSLKDKVKVV
INGTEHKMAYDEENERFVYQMTGCETGEYTYYYIVDGERKTDSFNANKKIVDGEEVSYFT
FKKFSDLSIRAALNEAAMNYNDNNVLSVSFAGKDAKVFTEEEIDNITADLSELGLGTMQI
HPELMQLSISAASDTTVGEKTIPVTMTDIYGNIYDTTASVTVTARDKDTFDWDEAVIYMT
CTDRFFDGNTENDKAYHTTDVYDPDGSLSYHGGDFAGLEQKLDYLDSLGVNTIWITPIVD
NADTTTTKDDETIPSTGYHGYWASNFTSLNPHLGTEKEFQSLIEAVHAHGMKLMVDVVLN
HAGYNTEDTFNSVLVDQDGNAVPMIRDSSNSITGDDVYASLSGLPDFVTENSEVRDQLVE
WQTDWVEKYDIDYYRVDTVKHVDSVTWAAFKNALTEANADFKMIGEYFGAGYASTAGELG
TGSMDSLLDFDFNDEAQKFVTGNLSEVESFLEKRNSSINNTAMLGAFLSSHDENSFVDKL
INDSGMTEEEALKVFKVAASLQLTSKGQAVIYYGEELGQHGLDNYPYQTNRYDFDWTEEA
KQEKDDSSMLNHYKKLLSIREANSLLLARGTRTDIQTSDEEGYSIFERSYQGDTLTIGLN
ISDGAKKVSFHTDYAAGTILKDLYGGSSYTVDKDQNVTVTIPSAENGGTVILSKVTSEAI
DPTPVVPAGGKDTKTEGTKTEETKTEGTKTETVKTTDTAGGTASATDWDAVVAAIKGAAD
GETITVAMDEKGILSSRAIEALKGTSKKLVLDMGNGIKWIIDGKNIEKVPTSDIDMKVKF
GSSSIPDAVIKASDLGDHLEKILTFSLEHDGEFGFMPTLSLEIGKEYAGKYANLFYYNPK
TNKLEGKTSVKIADDGTVEFTFRHASDYLISVTENAVMSENKIVPDTGDTQNGEAYLLLI
ALGAAAIAAAGYQKKKAGMR

Enzyme Prediction     

No EC number prediction in MGYG000000356_00766.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	813	1121	9.3e-108	0.9897959183673469
CBM83	458	553	9.5e-32	0.9791666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	2.19e-71	776	1163	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	8.05e-71	770	1194	185	674	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	6.45e-61	771	1160	5	369	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	1.58e-58	776	1162	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	3.54e-54	774	1166	1	384	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	0.0	167	1516	310	1672
ACR74843.1	0.0	2	1272	10	1298
CBK91127.1	2.51e-241	68	1264	193	1303
CBK93942.1	2.51e-241	68	1264	193	1303
QKH63022.1	4.95e-209	169	1280	39	1130

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.43e-48	772	1226	6	424	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	3.54e-48	772	1226	40	458	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	4.06e-44	766	1226	1	431	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAU_A	6.61e-37	757	1245	4	453	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]
6SAO_A	2.02e-36	771	1244	5	439	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q05884	6.38e-42	799	1263	84	624	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P08704	1.48e-38	761	1263	28	558	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P25718	4.30e-36	770	1197	184	670	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q08806	8.83e-34	772	1241	38	485	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
P26827	5.14e-33	776	1262	43	526	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2

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
0.000249	0.999066	0.000166	0.000222	0.000154	0.000139

TMHMM  Annotations     

start	end
12	29
1495	1512