CAZyme Information: MGYG000000507_00354

Basic Information

• Species: UBA2903 sp900768875
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; RF32; CAG-977; UBA2903; UBA2903 sp900768875
• CAZyme ID: MGYG000000507_00354
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
703		81326.67	4.8191

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000507	1876051	MAG	Fiji	Oceania

• Gene Location: Start: 151182; End: 153293 Strand: -

Full Sequence      

MGRERKFKPKATPVLTGSDVGTVSKRGWIIKEKHNHLMDYAASSPITIEHVSPQIDAGRY
AVKREVGDTMDVVCSIFKDGHDLIKAVILCRLADSNEWWETPMTEVNHGLAQWYGQLWFG
TNARYIYTIEAWVDEYGTWLDGTTKKLEAGQDISLELVEGADMVRKTVERLKTIKDVRDE
DARKADLALLQDALKRFDENEDMYQCANILMGNDVSEAMDRWPDREKATRYDRELEVYVD
RERARFGAWYEMDVRSQGSVPGVHGTFKDAEARLPDIQAMGFDVVYMLPIHPIGYAHRKG
KNNSLVCEPGDVGSPYAIGSAEGGHRSIHPQLGTMDDFRSFVAKTHELGMEVAMDFAIQC
SPDHPWIKEHPEWFTFRPDGTIKYAENPPKKYQDIVNVNFYGEHSESLWLELRDTFLFWA
NEGVRIFRVDNPHTKSVPFWEWVIREVQNVYPDTLFLAEAFTRPPMMQMLAKVGFTQSYS
YFAWRESKKDLEEYFTELTQTDEKEFMRPNLFPTTPDIMPMYLHDAPRSAFIIRFILAAT
LSPSYGMLNGYELCENDGIPGREEFNNSEKYEIRTRDWNAEGNIKDVVAAINWIRGENYA
LQEYENLRFYTSENDNIIFYGKMTEDRSNMIFVALSLDPYHGQAGRIWFPTEEMNVAFGG
RFHVEELLSGREFDVRGNELWINLYPAGNQAEIYRVTPIDRAW

Enzyme Prediction     

EC	2.4.99.16

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	271	492	4.2e-89	0.9857142857142858

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11344	AmyAc_GlgE_like	0.0	246	598	1	354	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	7.94e-54	46	241	3	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	7.37e-47	250	530	8	263	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.
COG0366	AmyA	8.28e-21	264	514	25	292	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	5.01e-18	265	530	22	220	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
QNT69253.1	2.97e-271	43	696	32	674
QIB67206.1	2.84e-254	41	698	457	1102
AEO48121.1	7.66e-252	43	698	32	688
ABC22404.1	7.66e-252	43	698	32	688
QXG82040.1	7.66e-252	43	698	32	688

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5VSJ_A	1.24e-173	46	696	21	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	2.35e-173	46	696	21	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	2.72e-172	46	696	41	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	1.16e-171	46	696	21	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	2.17e-171	46	696	41	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
Q2RTZ1	1.53e-252	43	698	32	688	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	7.13e-209	46	686	8	642	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=glgE PE=3 SV=1
Q8KAR6	1.84e-202	46	696	23	666	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OX=194439 GN=glgE PE=3 SV=1
Q3J3M8	3.92e-201	42	696	22	661	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	5.72e-195	42	643	4	590	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2

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
1.000039	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000507_00354.