CAZyme Information: MGYG000000666_01189

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829
• CAZyme ID: MGYG000000666_01189
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1427		159654.02	6.361

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000666	4523435	MAG	Kazakhstan	Asia

• Gene Location: Start: 11704; End: 15987 Strand: -

Full Sequence      

MNPVQTPEPGTHLLLYTGDVLTFVLRTEGRGRAYLRTNIGNAAVRRAETISIVDHGLVPA
GQDWHDIPMTDEGNGVFSLRLGLVETGHFEAKCCFLPEKSEEFLWPDGPNVHVNVGPAAY
CCANSIYCAFVRQFGPNRTKSVTVPPDPETAAAESRLDGRNYTVIPPSGTFRDLIRELDH
IFDRLQCRILHLLPINPTPTVYARMGRFGSPYASLNFKAVDPALAEFDKTATPLEQFMEL
VDAVHARNGKLMIDIAINHTGWASRIHEMHPEWLKRKPDGTILSPGAWGTVWEDLTELDY
GNKELWKYIADIFILWCDRGVDGFRCDAGYMIPVPAWEYIIARVREIYPDIIFLLEGLGG
DPAVTTRLLDYANMNWAYSELFQNYSRQQIEGYLNYAWKESRGNGLMVHYAETHDNSRLA
AVSECYARMRTALSALASMNGAFGFANGVEWFAREKIDVHEARGLSWGAASNQVEFIGRL
NTILRRHPAFHNGASVRFVDSGSPHGLLIARADASGRNRVLVAVNLDCEHPATLTWNPVE
TGSSGLTVYDLLCKETVKIQVIEHTKLALELPPGWVRCLSCDASALEEIKAPAMPEKRRV
SKLEFQEACTMVLKTLTCLRGSSVLTENDRIETLAEHLLESPEAFLRTLVDGGSEPPFVR
WQWPEDVRRKVMVPPGKFLLVLSPLRFRAKVYLQERLLQQFDSLVDSGGRHFAIFYPLAA
ELPHKRALLHFAAFEEGKIIRETGHLLLLAPDIFQTMLSCSHHHIRNNVLTFLQANGRGA
LTHLRLDMPAVSSRYDAVMLANLNTDHPEDRHIMFRRIRMWLLHHARSQEVSLCCLKNFE
FAADGGGIWNYHVPTGNGLYVDLSLKIEMVQQKNQVRISLLRHTTGGLDMLPDPATVRLI
LRPDVEDRGFHCATKASGLESVWPRKVRFLENGFEFTPAEGRTLSLIASGGRFQPGDEWS
YMIWQPNEAARGLDPNSDAYSPGYFEFTLAGGDTAQIAAAIRTAMEPDVMTPHPPVPADF
RAETDSSLEKRMLESMRSFVVKRGSLKTVIAGYPWFLDWGRDTLIAARGLIAAPEFREDV
KAILKQFAMFAENGTIPNTIYGDNVGNRDTSDAPLWLFTAVADLCAAEGSTRFVESGIRD
GRTLRDVLEEIARGIQSGTPNGIRMDPASGLVFSPPHFTWMDTNYPAGTPREGYPIEIQA
LWFAALRFLSTISKEPEEWKRLAELVRSSILHLFLSSDGRWLSDCLHGSSGTLAAQAVRD
DHIRPNQLFAITLGAVTDRTLCETILETCAVLLVPGAIRSLADRKTEYPLPVYGADGRLL
NDPVHPYWGTYEGDEDTRRKPAYHNGTAWTWPFPSYCEAYAMTYGAAGKATARALLSSSE
LIMRSGCVGQIAEILDGDYPHTQRGCDAQAWSMTEFYRVWKLLHSSM

Enzyme Prediction     

No EC number prediction in MGYG000000666_01189.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	1045	1417	2.7e-92	0.9731182795698925
GH13	185	369	7.3e-32	0.8428571428571429
GH13	304	436	2e-18	0.3626666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	4.49e-75	1038	1418	5	374	Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).
cd11313	AmyAc_arch_bac_AmyA	7.10e-57	160	493	13	336	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.
COG3408	GDB1	2.99e-40	899	1412	131	595	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd11344	AmyAc_GlgE_like	9.76e-31	168	488	19	355	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	2.00e-28	169	441	22	247	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
AQV01271.1	0.0	4	1420	8	1429
AOY59008.1	0.0	4	1420	8	1429
ABC78593.1	0.0	5	1426	7	1423
ABW66661.1	0.0	5	1425	16	1433
BBO70997.1	0.0	5	1420	9	1425

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	5.53e-32	160	456	21	319	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	5.12e-16	192	508	44	349	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]
4U33_A	1.07e-15	166	550	273	673	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]
5CGM_A	3.64e-14	166	527	248	626	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]
1CGY_A	5.78e-11	212	535	100	445	ChainA, CYCLOMALTODEXTRIN GLUCANOTRANSFERASE [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q2RTZ1	2.01e-25	141	527	226	628	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
Q63T93	1.00e-22	169	531	676	1054	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q9I1W4	7.18e-21	169	527	227	601	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
Q1D651	1.25e-20	170	527	222	594	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=glgE PE=3 SV=1
Q6L2Z8	2.58e-20	159	527	189	569	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) OX=263820 GN=glgE PE=3 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
1.000056	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000666_01189.