CAZyme Information: MGYG000000129_00900

Basic Information

• Species: Marseille-P4683 sp900232885
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Marseille-P4683; Marseille-P4683 sp900232885
• CAZyme ID: MGYG000000129_00900
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
647	MGYG000000129_3|CGC5	73389.43	4.6702

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000129	2720267	Isolate	Canada	North America

• Gene Location: Start: 263960; End: 265903 Strand: +

Full Sequence      

MTPLETIQRAVDKIQQGEEYYIPAWWNYLSTSCRKDENRPGEVIVDPRRYYSDCLKKILQ
DPKRQAEASVEGSVMYSMMPRAFTAWNHTSDGELESGTLLKCIALLPRLKQMGVDLVYLL
PIFLSSHAFGKGELPSPYCIQDILSLDPELGDRLIPQITPEEQFAAFVEACHRLGMRVAL
DFVFRTAARDNVMIREHPDWFYWIKADDRDELQAPGIPGAGHQVVSADNVDALYQSPDMA
KFIECFVEPPEEQQWRWVVEEADRQGKGVLDVCIDRLGICTLTGFADTINDPQPPWTDIT
YLKFYFDPSPAAQRNLPAQELPPFLAQDGVKCSVFEGGNPNRQLWDTIAGVIPHYITRYG
LDGARIDMGHALPAPLYREIVRRIKACKPDFLLWSEEFSPENAPRAAQDGNHFITGDLWE
IWKNTPSNRVNHRVAKGLQSVLPVTAAVEMADTPRAPLMAGGEGQAKAIFRMLSLLPNNV
LLINNGQELGEIQPMNLGLCNDETGRFVLPPDHPMYGKLAFFDRVRFDWLNPGIEERVRW
MTEIIDLRRRYGSWIQDKDAFDWDTLDRDGELTALYYQKEGKALAAVVNRGAETRQVDFS
KIFDGSLKGIRSFEVIASDGFSLEGQDKSGELQEFGFVLLESKEEMR

Enzyme Prediction     

EC	2.4.1.-	2.4.1.25

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	104	209	5.1e-20	0.4523809523809524

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11335	AmyAc_MTase_N	0.0	41	551	1	534	Alpha amylase catalytic domain found in maltosyltransferase. Maltosyltransferase (MTase), a maltodextrin glycosyltransferase, acts on starch and maltooligosaccharides. It catalyzes the transfer of maltosyl units from alpha-1,4-linked glucans or maltooligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose. MTase is a homodimer. The catalytic core domain has the (beta/alpha) 8 barrel fold with the active-site cleft formed at the C-terminal end of the barrel. Substrate binding experiments have led to the location of two distinct maltose-binding sites: one lies in the active-site cleft and the other is located in a pocket adjacent to the active-site cleft. It is a member of the alpha-amylase family, but unlike typical alpha-amylases, MTase does not require calcium for activity and lacks two histidine residues which are predicted to be critical for binding the glucose residue adjacent to the scissile bond in the substrates. The common reaction chemistry of the alpha-amylase family of enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. 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.
cd11313	AmyAc_arch_bac_AmyA	1.64e-34	70	551	2	330	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.
cd11344	AmyAc_GlgE_like	1.31e-20	76	203	5	131	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.
cd00551	AmyAc_family	1.10e-16	74	184	1	98	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.
COG0366	AmyA	1.01e-13	73	209	1	133	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI60933.1	0.0	1	647	1	647
ANX00914.1	8.38e-144	4	616	8	639
AGC67976.1	1.18e-143	4	616	8	639
ANW98378.1	1.18e-143	4	616	8	639
AGI39011.1	1.18e-143	4	616	8	639

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GJU_A	1.39e-120	4	605	3	616	Maltosyltransferasefrom Thermotoga maritima [Thermotoga maritima MSB8],1GJW_A Thermotoga maritima maltosyltransferase complex with maltose [Thermotoga maritima]
3DHU_A	2.52e-15	64	202	4	124	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	1.15e-12	106	201	31	118	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]
5CGM_A	1.90e-11	73	201	229	360	Structureof Mycobacterium thermoresistibile GlgE in complex with maltose at 1.95A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CGM_B Structure of Mycobacterium thermoresistibile GlgE in complex with maltose at 1.95A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CIM_A Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CIM_B Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CJ5_A Structure of Mycobacterium thermoresistibile GlgE APO form at 3.13A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CJ5_B Structure of Mycobacterium thermoresistibile GlgE APO form at 3.13A resolution [Mycolicibacterium thermoresistibile ATCC 19527]
4U33_A	4.03e-10	76	201	257	385	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
Q3J3M8	5.80e-11	54	203	196	341	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
Q9JN46	2.12e-10	54	203	178	323	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q2S498	6.95e-10	52	202	177	325	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Salinibacter ruber (strain DSM 13855 / M31) OX=309807 GN=glgE PE=3 SV=1
D7BMJ2	9.39e-10	76	201	225	356	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Arcanobacterium haemolyticum (strain ATCC 9345 / DSM 20595 / CCUG 17215 / LMG 16163 / NBRC 15585 / NCTC 8452 / 11018) OX=644284 GN=glgE PE=3 SV=1
Q9RP48	1.64e-09	73	201	228	359	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000129_00900.