CAZyme Information: MGYG000004088_01702

Basic Information

• Species: Firm-11 sp900548145
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-11; Firm-11 sp900548145
• CAZyme ID: MGYG000004088_01702
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
422	MGYG000004088_35|CGC1	48635.18	5.3487

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004088	2947168	MAG	United Kingdom	Europe

• Gene Location: Start: 5258; End: 6526 Strand: -

Full Sequence      

MELRNMTIYSIFVRNHGGNFAAVEKDIPRIRALGADAVWLLPIHPIGQKERKGALGSPYA
IADYRAVNPEYGTMEDFRRLADTVHRNGMKLMIDVVYNHTSPDSWLAQHHPEWFYHKPDG
SFGNRIGEWSDIIDLDYGNPGLWDYQIETLKSWAEIVDGFRCDVAPLVPLEFWLRARREV
ETVRPGCLWLAESVEPEFIRDNRNRGMVSHSDGELYQAFDLCYDYDIYGDFLSYVQGKTE
LTDYVRALERQESIYPADYAKLRFLENHDRPRMAHLFPERRTRLNWLCWMFFQKGTALLY
SGQEWENDHRPDLFDADPIPMEGPAPLEGLIRRLTALKKDPLFEIGAYSLRACPGDVLTA
VWQERRENGKRLTGCFCLRGNPALVPVELSDGRYENLLKPGTFLRVESGLLSLDGNPAVL
QS

Enzyme Prediction     

No EC number prediction in MGYG000004088_01702.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	15	306	3e-48	0.9297658862876255

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11313	AmyAc_arch_bac_AmyA	5.88e-168	3	340	2	329	Alpha amylase catalytic domain found in archaeal and bacterial 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 firmicutes, bacteroidetes, and proteobacteria. 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.
cd11347	AmyAc_1	2.40e-43	25	350	26	391	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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.
cd11344	AmyAc_GlgE_like	8.47e-38	9	192	5	214	Alpha amylase catalytic domain found in GlgE-like proteins. GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. 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	2.09e-37	7	304	2	355	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	2.10e-37	7	300	1	252	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
AIQ59907.1	3.26e-165	1	422	7	427
AIQ31132.1	1.87e-164	1	422	7	427
AIQ42688.1	1.87e-164	1	422	7	427
BBH26772.1	2.93e-163	2	422	8	438
BBH26770.1	2.93e-163	2	422	8	438

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	4.50e-152	2	421	9	426	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
4GKL_A	4.50e-88	1	397	1	384	Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
5A2A_A	4.70e-25	16	304	39	327	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	6.50e-25	16	304	73	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]
4U33_A	5.56e-24	9	196	257	473	Structureof Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_B Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_C Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_D Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_E Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_F Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U3C_A Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_B Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_C Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_D Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_E Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_F Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q2RTZ1	1.68e-27	18	267	255	504	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgE PE=3 SV=1
Q1D651	9.55e-27	20	193	223	416	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=glgE PE=3 SV=1
Q9I1W4	1.86e-25	9	193	212	423	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=glgE PE=3 SV=1
Q3J3M8	2.83e-23	18	320	230	525	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) OX=272943 GN=glgE PE=3 SV=3
P9WQ17	2.96e-23	9	196	235	451	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000083	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004088_01702.