CAZyme Information: MGYG000003889_01508

Basic Information

• Species: CAG-964 sp902789345
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-964; CAG-964 sp902789345
• CAZyme ID: MGYG000003889_01508
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1171		127903.15	4.6777

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003889	1974122	MAG	United States	North America

• Gene Location: Start: 7451; End: 10966 Strand: -

Full Sequence      

MNEKKRFGKKLLSIALATTMVSSVAAVAATTSASAATNSSVSTQAVQPTTGDASTFSWDN
ATVYFLLTDRFNNGDKSNDHAYGRGLDQSGNAVSGVDQSAFFQGGDFAGITQKIEDGYFD
NLGVNAIWLSAPYEQIHGYVVGGDGTSFAHYSYHGYYVLDYTESDKNFGTKEEFRKLVDT
AHNHGIRIVMDIVMNHSGYNSLKDMSEYGFGPVKSGWESYYYAHKNVNNTDYHNYIDYND
SSSGRSSWAKWWGSDWIRCGLPGYTNGGGDDLTMCLSGLPDYKTNQSSNVGIPELLKTKW
NKEGTYNTKVSKYGSSNTVTGYLSDWLAEWVREFGVDGFRCDTAKHVDLQSWNTLKQKCV
KALKEWKSANPDKKLDDLDFWMTGECFPHYVNKDSYYTQGGFDSMINFEFAPATGNSSIP
SANNVESIYSRYANSINNDSSFNVLSYISSHDTVIAKGDRNYNGSFMLMLPGAVQIYYGD
ETNRPETSLPSGSTAGAGHQLRSFMNWNSINQGTLSHWQKVGSFRNNHIAVGAGQHNQIS
AYSSSSGYTFSRTYDNGSIQDSIVATLFAPKNTNLSVNVGSVWGDGTVVTNAYDNTTATV
SGGKVTFNTGANGTILIEGPQSSISMSLKSTEGTTSFYDSTTLTLTLKGADYATVTVDNG
TPFQVKNGESFKIGENSPVGSKINVSLTASNSEDTVTKSYVYTKKDPNAVVKLYFDNTGY
NWSSVYAYIYDDTTTPVTENSAWPGQAMTLNSSSGYYEIEVPEKLLGAGGKVIFAESSSS
GNRYPAEMQTGLSINGTSHKFSKGNTWEEFEITNPTQPTTPTTPTQPTQPTEPPVTYMIG
DISGDNDVTLIDVLMSQKMSLGTLEGTKVQKLAADVNKDGSISVADQVIMLRYLVGYENT
YNVGSIVSEGNTNPTTPTTPTTPTTPTTPTTPTVPTERPTEAPTQVSGNVVYLDFSALQT
GDERFAIWAWGSSNEGQWVDMTKNSSGIYQAEMPSGCSNIVFVRMNGATSENKWDNKWNQ
SEDLTFDSSKPLFKATGWSNEYFNGNWSASSAVGPTNPTSTPTETPTQVSGNVVYLDFSA
LQTGDERFAIWAWGSSNEGQWVDMTKNSSGIYQAEMPSGCSNIVFVRMNGATSENKWDNK
WNQSEDLTFDSSRPTYKATGWANAYFNGSWS

Enzyme Prediction     

No EC number prediction in MGYG000003889_01508.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	105	482	6.9e-147	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	56	556	185	672	alpha-amylase; Reviewed
cd11338	AmyAc_CMD	2.51e-46	69	530	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.
cd11320	AmyAc_AmyMalt_CGTase_like	5.60e-43	62	483	6	350	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.
cd11339	AmyAc_bac_CMD_like_2	3.91e-41	62	498	4	320	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	5.83e-40	61	589	1	504	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT06045.1	5.77e-308	9	816	3	804
BCN30960.1	5.10e-242	1	802	1	799
QMV42547.1	6.07e-214	49	816	32	775
QCT06087.1	7.88e-194	9	618	7	641
CDM67955.1	7.44e-191	43	778	55	797

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4E2O_A	5.00e-24	58	481	7	328	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2A_A	1.20e-23	58	481	6	327	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	1.36e-23	51	481	33	361	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]
1UKS_A	7.92e-22	63	501	17	390	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1UKS_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]
1I75_A	4.17e-21	63	501	17	390	CRYSTALSTRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1I75_B CRYSTAL STRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1PAM_A CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1PAM_B CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1UKQ_A Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011],1UKQ_B Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	2.61e-124	50	535	178	647	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	1.62e-21	101	481	94	462	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P05618	2.43e-20	63	501	44	417	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1011) OX=1410 GN=cgt PE=1 SV=1
P38940	5.06e-20	58	517	131	487	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
P14014	7.41e-20	63	481	51	397	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
0.000661	0.998196	0.000247	0.000370	0.000262	0.000230

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003889_01508.