CAZyme Information: MGYG000003295_01094

Basic Information

• Species: CAG-312 sp002437405
• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; CAG-312; CAG-312; CAG-312 sp002437405
• CAZyme ID: MGYG000003295_01094
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
793		87386.66	5.8509

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003295	2127186	MAG	Mongolia	Asia

• Gene Location: Start: 6688; End: 9069 Strand: +

Full Sequence      

MSTIRAWWRKADEIVLVFPRDIPQVIPHIYVSGAGTGFRVLRPQPAEFAKLSSYYIDGGS
VRFRLDPAACNSGALPDCDYYVCGSFNGWANAVKNPVWRMKPDSRGVLWLPVPLAALDSS
QGAVLFKFASGDGRWIEPNSEAPNAVSDRNGNHNLKISADTTGRNILVLKFDGACDPTVE
IRVKIPQMKVDMPVAAAELLRSIYSSSRLGAYRHGGGTKFSIFAPRAKAAYLRYWAKGSP
TSRVLYATSHDGAVWTATADEDLQGYRYAWHIDGDKSLPSSNFDVRFSVADPYANAFETS
SGAAIVKYYDEIPDAPTDFTPPPWHELSIMEVHVRDVLANACADLSDGERLTFAGLTKWL
KSPDCYLRRAGVNCVELQPVQEFTAENRADYEWGYMPVGWFAPASSYATDPQNATQNDDL
RNLVNAFHEAGIAVLFDVVYNHYGEPNYLGYIDSGYYFETASDGSLMNFSGCGNDVRAKS
PMALRLIIESLAALLVKYGADGFRFDLAELLGMGALREIETCVKRIKPSAILIAEPWSFR
GHIGASLKSTGYASWNDGFREFMLSYAKGEGNCDGFKYFMAGSRGGYASFPTQTVNYLES
HDDMCLFDRITSAHGNPSRWDLRRYKLAYALVFLAVGIPMAAEGFDLIRTKGGLNNTYKN
GAANALDYIRGTYFSGECAWLRSLAKFRLSESARALRLSENKSEGYFEFFTSDGTSAAGV
LFNASGESDAKRIFAALNPTGGEVELPAPDCVKTMKQIADIDRFNEAGLTDFVMDAQATV
KLPPISLAIWCER

Enzyme Prediction     

No EC number prediction in MGYG000003295_01094.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	366	644	1.5e-58	0.9826989619377162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	2.99e-78	218	750	21	588	pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.
cd11341	AmyAc_Pullulanase_LD-like	4.06e-78	329	688	5	406	Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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.
COG1523	PulA	1.66e-74	217	693	31	590	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11326	AmyAc_Glg_debranch	4.09e-64	323	688	12	430	Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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.
cd11325	AmyAc_GTHase	1.39e-49	291	640	1	352	Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYY35929.1	8.25e-205	7	793	11	809
ADE54637.1	2.08e-181	5	790	8	806
ATC63384.1	3.81e-180	74	793	83	810
QXD22729.1	1.42e-177	26	790	36	811
QXD26807.1	1.42e-177	26	790	36	811

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	1.89e-58	144	750	249	887	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	6.12e-53	203	749	35	618	Crystalstructure of Pullulanase from Paenibacillus barengoltzii complex with beta-cyclodextrin [Paenibacillus barengoltzii],6JFJ_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin [Paenibacillus barengoltzii],6JFX_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltopentaose [Paenibacillus barengoltzii],6JHF_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii],6JHG_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii in space group P212121 [Paenibacillus barengoltzii]
3WDH_A	9.71e-53	204	713	106	626	Crystalstructure of Pullulanase from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDI_A Crystal structure of Pullulanase complexed with maltotriose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDJ_A Crystal structure of Pullulanase complexed with maltotetraose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11]
6JHH_A	7.21e-52	203	749	35	618	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	7.21e-52	203	749	35	618	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C0SPA0	2.97e-48	189	697	82	622	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840	1.07e-42	194	786	210	836	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
P9WQ25	5.97e-38	209	658	27	556	Glycogen operon protein GlgX homolog OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgX PE=1 SV=1
P9WQ24	5.97e-38	209	658	27	556	Glycogen operon protein GlgX homolog OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=glgX PE=3 SV=1
P0A4Y5	5.97e-38	209	658	27	556	Glycogen operon protein GlgX homolog OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=glgX 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
1.000042	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003295_01094.