CAZyme Information: MGYG000003631_00012

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Kiritimatiellae; RFP12; UBA1067; UBA1731
• CAZyme ID: MGYG000003631_00012
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1282	MGYG000003631_5|CGC1	139780.18	6.5102

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003631	1663259	MAG	Fiji	Oceania

• Gene Location: Start: 209; End: 4057 Strand: -

Full Sequence      

MRQSPSPDGTLLRWRGDELVVTLELDAPRRGRAVFRTNLGAAAVCRREVIEETETGATPL
ATGWRDVKMRETAPGRFRCALTLDEVGVFAGKCCFFPQGSRTPEWPAGGDLRMKVEPAET
RSGNSIYTVFPRQFGSFREVVRRLGHVMDDMGFRIIQTLPPFPVPATYAVMGELGCPFAA
TDFFSVDPACAEFDRRATPLDQFRELIAAVHAKGGRLFIDLPANHTGWASTLQTHHPEWF
RREPDGAFVSPGAWGVTWEDLVALDYAHPGLREYVADVFLFWVRNGVDGFRCDAGYMIPE
TTWRYVVARVREEYPDTVFMLEGLGGKLEVTDALLARAGMDWAYSEIFQTYDRGQFEWYL
PSANARATQFGALVHFAETHDNDRLAKGGETYARLRVALAALLSHQGAWGITNGVEWLAT
EKIDVHGKNDLNWGASRNLVPLIARLNRLLASHPAFAGVVEQTLVARGDGNFLAVRRSAA
GSGAALLVLANLDCAHGCAAHWDPAAFPEGPAHDLLSGRAMDVHQGLWLEPGGVLCLSGE
PWAPETKAADGRAAKRPTPTDDVPHVTWSFPQDLRRVTCVPAGMALKVLGGQPFRVRVQD
GPRTVAVARGESEVILHLPPYAGDGTSADERRIVFTDYTGGRATRHEARLLVLPPAEKAR
AKLAVAGAEARKCPELRVALANGAGAAAFVPVAWGEIRSQYDALFAANPNPRVPSDRLVV
WTRCRAWLQHEGYSREINADGLEQFRTDPAGRTAEWTFRVPCGLGREVRLGFTLSLAHGA
NAARLSLRRLGAGRRDLKEPVRLVLRPDLECRSFHDTTKAYTGPEAAIERRIAEMVRLDV
AGGELHDEGRWTYSAPHPDEAGRGQEPAGDLFSPGWISVDLATEGASGAVVCSLRGEKGP
FAFPETNAKAPAALPLGDALPRALNLYVARRDDVKTVIAGYPWFLDWGRDTFIFLRGAIA
AGWTDEALQVVEAFARFEDRGTLPNIIHGDTAGNRDTTDAPLWFVLAVRDLGARTGEDLL
KRRGGGKRTLGGVVNSILDHYRDGTPNGIRVDADSGLVWSPAHFTWMDTNYPACTPRCGY
PVEIQALWIAALRFAGRHAEANRAAESLVRLFANGQGLADCLDAPNGEPAAQARRDDSLR
PNQLLAVTLGAVATDSALAREIVLANERLLTPVGIRSLDAADGKYRGVYAGDEDTARKPA
YHNGTVWGWQAPLFAEAAAKCGIWPKEAALSLLAGAVEALNDGVLCHLPEIADGDAPHAQ
RGCRAQAWSDSELLRVWKEING

Enzyme Prediction     

No EC number prediction in MGYG000003631_00012.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	932	1275	3.8e-86	0.978494623655914
GH13	149	345	1.4e-33	0.8952380952380953

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	1.43e-81	934	1275	18	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	5.45e-58	126	458	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	1.85e-54	843	1275	178	601	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	5.79e-29	126	407	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	7.36e-28	127	454	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
AKJ63770.1	0.0	3	1280	13	1423
ABC78593.1	0.0	1	1281	5	1421
BBO75755.1	0.0	3	1282	9	1430
BBO91312.1	0.0	1	1280	7	1427
AQV01271.1	0.0	3	1280	9	1432

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	7.78e-29	113	446	1	343	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]
5CGM_A	2.27e-16	124	493	229	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]
7EKX_A	2.73e-12	933	1280	1056	1522	ChainA, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EKX_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138]
5D06_A	2.73e-12	933	1280	1056	1522	CrystalStructure of the Candida Glabrata Glycogen Debranching Enzyme [[Candida] glabrata CBS 138],5D06_B Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme [[Candida] glabrata CBS 138]
5D0F_A	2.73e-12	933	1280	1056	1522	CrystalStructure of the Candida Glabrata Glycogen Debranching Enzyme (E564Q) in complex with maltopentaose [[Candida] glabrata CBS 138],5D0F_B Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (E564Q) in complex with maltopentaose [[Candida] glabrata CBS 138]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9I1W4	3.54e-21	125	542	210	650	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
Q63T93	8.65e-21	125	455	659	1012	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q2RTZ1	1.25e-18	60	493	179	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
Q8PE50	1.42e-17	124	454	202	556	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
Q6L2Z8	5.24e-17	111	455	177	534	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
1.000041	0.000004	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003631_00012.