CAZyme Information: MGYG000003642_02596

Basic Information

• Species: RUG572 sp900771305
• Lineage: Bacteria; Verrucomicrobiota; Kiritimatiellae; RFP12; UBA1067; RUG572; RUG572 sp900771305
• CAZyme ID: MGYG000003642_02596
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1322	MGYG000003642_474|CGC1	145131.43	5.6056

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003642	3810265	MAG	Fiji	Oceania

• Gene Location: Start: 5156; End: 9124 Strand: +

Full Sequence      

MALCAFMRQNPEPDSYHLRWKGDLLEVSLTLDAPRRGRAAFRTEIGGAVIARRETIEQND
EGVTPLEKQWRDIPMMEASPGVWKTAVALGEVGIFHGKCCFFPEGGSVPEWPQGGNLTVK
VEPAETRGGNSIYTVFPRQFGSFREVARRLDFIMDTMGFRIIQTLPVFPVPTTYAVMGEY
GCPFAATDFFSVDPAMAEFDPYATPLDQFRELIGAVHAKGGRLFVDLPANHTGWASTLQT
HHPDWFHRAADGKFISPGAWGVTWADLVELDYSHPELRAYMADVFLFWVRNGVDGFRCDA
GYMIPEATWKYIVARVREEYPDTVFMLEGLGGKLEVTDALLNRAGLDWAYSEIFQTYDRG
AFEWYMPAAIDRARKYGALVHFAETHDNDRLAKGGHTWARLRVALAALLSHQGAWGIANG
VEWYATEKIDVHGKSDLNWGASDNLVDFIAQLNHLISHHPDFAGNEPISLVERGDGNFLA
VTRGSTLVLANLDCGRGVSAHWDVAAFPASSDPDDLLLGRRVHAEDGLWLEPGEVRVLSH
CPCAELPPPPLPPVPEGFAVDWNYPEDATRDVCVPAGCALKVVAPHPFRVRVIDGERTLA
VERSVPAPSVDHSVNPQSNNQTILHLPAYVGDGTHANVRELVISVYAPGGVDRRQARVLL
LPPADQARVKLVYTGDEIRRNLAYPGPGGLLETILSDGAGAASRVKLAWGEVRSQYDALF
AANPNPHVPADRLTLWTRCRCWLQHEGYSREINVDCIDHFRADPAGRKAEWCFTVPCGLG
RVAKFVFNLFLAQDGTGTAKLQVRRMPAGDAEVGAPVTLVFRPDLEWRSFHGTTKAQGAV
ENAFAGATRVLDESGFAFVPYGKNEQLVMHVSGGAFHPEGEWSYCVSHAEEAARGQDGCG
DLYSPGWISCPMGIADEAAIEAFYVSDIRVAAFDEQKARRLMSERGEPVVTTALTVPFDA
ALREALKLFIVKRDDVKTVIAGYPWFLDWGRDTFIFLQGAIPGGFGKEALAIVEAFARFE
ENGTLPNIIYGETAGNRDTVDAPLWFIRTLAVLGKKAEKFRPVAESIVANYVKGTPNGIH
VDAESGLVWSPSHFTWMDTNYPACTPRMGYPVEIQALWIAALRYLGGKKWNALADQATAS
LVRFFVRKDEVGGLYDCLDAPNGEPAAQATPDGGVRPNQLFVVSLGVFDSIKQSDNQEIV
RSIVRACAPLVIPGGVRSLARSDGRYRGIYAGDEDTSRKPAYHNGTVWAWPFPMYAEALV
KAGLASKETARSLLASAVENLNAGCVCHVSENADGDAPHAQKGCRAQAWSASELLRVWLA
LS

Enzyme Prediction     

No EC number prediction in MGYG000003642_02596.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	974	1316	1.4e-79	0.978494623655914
GH13	149	351	1e-32	0.919047619047619

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	5.40e-78	969	1316	6	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	1.07e-58	132	464	7	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.
COG3408	GDB1	7.41e-50	853	1316	156	601	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.31e-28	132	413	2	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.
cd11344	AmyAc_GlgE_like	7.64e-24	133	460	5	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABC78593.1	0.0	5	1318	3	1417
BBO75755.1	0.0	9	1319	9	1426
BBO70997.1	0.0	7	1319	7	1426
BBO91312.1	0.0	7	1319	7	1425
AKJ63770.1	0.0	1	1317	5	1419

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	4.24e-30	132	425	15	316	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	6.25e-17	157	459	37	325	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]
1CYG_A	4.23e-14	169	547	76	495	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
5CGM_A	1.70e-13	113	460	213	587	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]
1WZA_A	4.37e-13	133	309	8	208	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q2RTZ1	2.75e-20	113	460	221	589	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	5.34e-19	131	460	659	1011	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q3J3M8	1.25e-18	137	521	226	637	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
Q8PE50	4.92e-18	117	504	188	611	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=glgE PE=3 SV=1
Q9JN46	9.34e-18	137	460	208	546	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
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003642_02596.