CAZyme Information: MGYG000004490_00992

Basic Information

• Species: Muribaculum sp003150235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Muribaculum; Muribaculum sp003150235
• CAZyme ID: MGYG000004490_00992
• CAZy Family: GH13
• CAZyme Description: Periplasmic alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
567		65099.64	4.8818

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004490	3323418	MAG	Israel	Asia

• Gene Location: Start: 23736; End: 25439 Strand: +

Full Sequence      

MKKSHLFLLLSIIGLQSIKAEPKPDFDWGNANVYFVITDRFANGDPSNDINYGRITDYGS
ERLNAATFHGGDFKGMLQKAGEGYFKELGIDVVWMTDVYEQIHGWMSGSGSVNDFPHYGY
HGYYPLDYTQIDKNYGTVEEFRSLVDELHRQGIRVMLGANLNDPGYPTLLDAVQLGFADT
GLTEQEAAGHIRDWSFDKFFEGRIEWKGWYDRGWIRMPDEGWDESNPLQATLFGMPDFKD
ESNEPVKIPDFLKRKWKREGKSNDAWVNPSARELRKDRNWSPIQYVIAWISSWVEEFGID
GFRCDIVENVHLNRWKELNEACNAALEKWRDNHPECPASKWTDRFYMTGDFDNAGIDYKP
EYADAGFSSMVNFFLPKHGDLDGIVYTWQAYADSVQAHPDWHPFSYLNNSYHRDADMSNM
IDCATTLLLSPGVSQVFYGDETGRKLNDARLNVDSDQAFRSDMDWDDVDTLQLKHFQKLG
KIRNTHPAIGKGRQTTIDTHTCYREYKNDRLIIRVRPIEKQPIVVSPFFPDGTHLTDLCT
GNMATVTNGTVTFPVYENNVAVIAPAW

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	71	442	5.4e-114	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	9.67e-141	8	513	171	677	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	2.68e-31	32	486	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.
cd11340	AmyAc_bac_CMD_like_3	8.96e-27	33	463	6	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.
cd11338	AmyAc_CMD	9.47e-26	39	492	10	387	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.
smart00642	Aamy	1.53e-23	35	157	1	88	Alpha-amylase domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCD35939.1	0.0	1	565	1	565
QIL88611.1	6.92e-191	25	555	40	570
ASW43710.1	8.76e-145	2	563	3	553
BAF93484.1	8.57e-141	2	566	7	596
BAG70894.1	8.57e-141	2	566	7	596

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2B_A	2.20e-26	9	526	21	430	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]
5A2A_A	1.60e-25	23	526	1	396	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	3.10e-24	23	526	2	397	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6AIJ_A	7.55e-18	1	549	1	484	Cyclodextringlycosyltransferase from Paenibacillus macerans mutant N603D [Paenibacillus macerans]
3VM7_A	7.90e-18	1	343	1	266	ChainA, Alpha-amylase [Malbranchea cinnamomea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	9.09e-93	15	513	173	670	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P21543	7.68e-22	27	562	743	1193	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P32818	2.70e-19	27	496	130	510	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 SV=1
P08704	1.30e-18	15	563	26	547	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P29964	1.38e-17	33	524	134	539	Cyclomaltodextrinase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=Teth39_0676 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
0.000320	0.998863	0.000243	0.000204	0.000188	0.000170

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004490_00992.