CAZyme Information: MGYG000002897_00498

Basic Information

• Species: Varibaculum cambriense
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Varibaculum; Varibaculum cambriense
• CAZyme ID: MGYG000002897_00498
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
765		85520.41	7.5292

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002897	2017891	MAG	United States	North America

• Gene Location: Start: 120995; End: 123292 Strand: -

Full Sequence      

MAGDTPRSRKTRSTTSSAGQKAKTSKSAAANSRKTPVRTKAASSAAKTDATAKAKTAAAS
KAKTTTSVPRKRVSRAKAAAPKAAAAKPLNLVSPEARLARIPVTEVEPVFEDGLWPAKAV
ENESFPVRATVFREGHDALGAEVVLVDPQGKETMRARMYDVAPGLDRLEAWIKPTAVGDW
TFRVDTFCDPYQTWAKEASIKVQADQDVEMEFELGARLFERAANGEAVNNPTQQAPDAKS
AARLLDAAKAMRDQSRPAQERLSVGLHSSIRGIFRAYPLRDLLESSRTYPLRVDRERALY
GSWYEIFPRSIGAYKDQEGHWHSGTLRTAAADLPRIAGMGFDVAYLTPVHPIGTTFRKGR
NNTLGATPEDPGSPYGIGSPEGGHDAIHPDLGNFDDFDYFVKKAKGLGLEVALDLALQCS
PDHPWVKDHPEWFKHRPDGTIAYAENPPKKYQDIYPLIFDQDYRGLYNAVRDVIQKWIDH
GVTIFRVDNPHTKPVQFWQEILAEFHQKHPEVLFLAEAFTRPAMMRTLAQVGFHQSYTYF
TWRNTRKEIEEYFQEVAWESSPYMRPSFWPTTHDILTQVMVDGGIQAFKMRAVLAATGSP
NWGIYTGYELVENVQRPGFEEQIDNEKYEYKPRDYSGETAQEMMGLLTTLNGIRRRHPAL
QRLRNLKIHETTHPSVVCFSRHLDAWESPTGVADTVIVVVNLDPHDTAIGAIHLDLSALK
ISGSSSSCFKVRDELDGKVYDWSSANYFELNPFDRPAHIMSVEAS

Enzyme Prediction     

EC	2.4.99.16

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	330	549	2e-89	0.9809523809523809

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11344	AmyAc_GlgE_like	0.0	300	658	1	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.
pfam11896	DUF3416	1.35e-64	100	295	2	185	Domain of unknown function (DUF3416). This presumed domain is functionally uncharacterized. This domain is found in bacteria and archaea. This domain is about 190 amino acids in length. This domain is found associated with pfam00128.
cd11313	AmyAc_arch_bac_AmyA	5.12e-45	304	662	8	335	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.
cd00551	AmyAc_family	1.67e-20	304	600	3	249	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	4.85e-19	303	584	3	305	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOX82269.1	0.0	90	764	75	749
QWW20372.1	1.89e-314	98	763	6	670
QYB16254.1	5.34e-311	98	763	6	670
QPK80604.1	1.29e-300	95	763	3	670
QDC25451.1	3.53e-300	93	764	48	713

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5VSJ_A	7.32e-243	100	762	20	661	ScoGlgEI-V279S in complex with a pyrolidene-based ethyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VSJ_B Sco GlgEI-V279S in complex with a pyrolidene-based ethyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VT4_A Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VT4_B Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VT4_C Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VT4_D Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound [Streptomyces coelicolor A3(2)]
4U2Y_A	1.47e-242	100	762	20	661	ScoGlgEI-V279S in Complex with Reaction Intermediate Azasugar [Streptomyces coelicolor A3(2)],4U2Y_B Sco GlgEI-V279S in Complex with Reaction Intermediate Azasugar [Streptomyces coelicolor A3(2)],4U2Z_A X-ray crystal structure of an Sco GlgEI-V279S/1,2,2-trifluromaltose complex [Streptomyces coelicolor A3(2)],4U2Z_B X-ray crystal structure of an Sco GlgEI-V279S/1,2,2-trifluromaltose complex [Streptomyces coelicolor A3(2)],4U31_A Sco GlgEI-V279S in Complex with maltose-C-phosphonate [Streptomyces coelicolor A3(2)],4U31_B Sco GlgEI-V279S in Complex with maltose-C-phosphonate [Streptomyces coelicolor A3(2)],7MEL_A Chain A, Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 [Streptomyces coelicolor A3(2)],7MEL_B Chain B, Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 [Streptomyces coelicolor A3(2)],7MGY_A Chain A, Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 [Streptomyces coelicolor A3(2)],7MGY_B Chain B, Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 [Streptomyces coelicolor A3(2)]
3ZSS_A	1.79e-241	100	762	40	681	Apoform of GlgE isoform 1 from Streptomyces coelicolor [Streptomyces coelicolor],3ZSS_B Apo form of GlgE isoform 1 from Streptomyces coelicolor [Streptomyces coelicolor],3ZSS_C Apo form of GlgE isoform 1 from Streptomyces coelicolor [Streptomyces coelicolor],3ZSS_D Apo form of GlgE isoform 1 from Streptomyces coelicolor [Streptomyces coelicolor],3ZST_A GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin bound [Streptomyces coelicolor],3ZST_B GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin bound [Streptomyces coelicolor],3ZT5_A GlgE isoform 1 from Streptomyces coelicolor with maltose bound [Streptomyces coelicolor],3ZT5_B GlgE isoform 1 from Streptomyces coelicolor with maltose bound [Streptomyces coelicolor],3ZT5_C GlgE isoform 1 from Streptomyces coelicolor with maltose bound [Streptomyces coelicolor],3ZT5_D GlgE isoform 1 from Streptomyces coelicolor with maltose bound [Streptomyces coelicolor],3ZT6_A GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT6_B GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT6_C GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT6_D GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT7_A GlgE isoform 1 from Streptomyces coelicolor with beta-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT7_B GlgE isoform 1 from Streptomyces coelicolor with beta-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT7_C GlgE isoform 1 from Streptomyces coelicolor with beta-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT7_D GlgE isoform 1 from Streptomyces coelicolor with beta-cyclodextrin and maltose bound [Streptomyces coelicolor]
5CVS_A	7.25e-241	100	762	20	661	GlgEisoform 1 from Streptomyces coelicolor E423A mutant soaked in maltoheptaose [Streptomyces coelicolor],5CVS_B GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked in maltoheptaose [Streptomyces coelicolor]
4CN4_A	1.45e-240	100	762	40	681	GlgEisoform 1 from Streptomyces coelicolor E423A mutant with 2-deoxy- 2-fluoro-beta-maltosyl modification [Streptomyces coelicolor],4CN4_B GlgE isoform 1 from Streptomyces coelicolor E423A mutant with 2-deoxy- 2-fluoro-beta-maltosyl modification [Streptomyces coelicolor],4CN6_A GlgE isoform 1 from Streptomyces coelicolor E423A mutant with maltose bound [Streptomyces coelicolor],4CN6_B GlgE isoform 1 from Streptomyces coelicolor E423A mutant with maltose bound [Streptomyces coelicolor],5LGV_A GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked in maltooctaose [Streptomyces coelicolor A3(2)],5LGV_B GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked in maltooctaose [Streptomyces coelicolor A3(2)]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D7BMJ2	8.53e-264	98	763	27	688	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
Q9KY04	1.99e-241	98	762	9	652	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 2 OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=glgE2 PE=1 SV=1
Q9L1K2	4.92e-241	100	762	20	661	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=glgE1 PE=1 SV=1
Q8G784	1.95e-216	100	763	73	746	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Bifidobacterium longum (strain NCC 2705) OX=206672 GN=glgE PE=3 SV=1
C6A9K7	6.26e-200	84	763	37	724	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Bifidobacterium animalis subsp. lactis (strain Bl-04 / DGCC2908 / RB 4825 / SD5219) OX=580050 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
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002897_00498.