CAZyme Information: MGYG000001791_00368

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; UBA953; W0P29-029
• CAZyme ID: MGYG000001791_00368
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
831		94891.72	8.2065

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001791	1747323	MAG	Denmark	Europe

• Gene Location: Start: 6969; End: 9464 Strand: -

Full Sequence      

MTSRLLKKISSLLPKFLPNPRLSSAYWVTNNTFFISLDRDWGNSLSMPSLSMKSGRKILS
VSRVPPSFWAGASGYHCEGNDVVFMLLPSIYRDYDIQEGAEIYVAGTFNDWAPARRPEWK
MEYRSYGGFSAWILQVPKSRFFDGGKKEEEQFKFVTASGRWLEPPAGWFNMVRDDKGNAN
LCLSSLRTGWCAFRVVCEALQNSDQADEVIWEAPKERFSLPIRSGYFLSFLFSPVLLGAR
VERGGKETTFRIFVPRATQINLFVRRTDSAPAISEAMVPIGNGVWEARIPENLHGRHYDY
FIDGRNIDATSAFDPARPVLDPYAKACVSREGPGIVIDEHRFGYPKKKFTAPHLSDLVIA
EVHLRDLIARHPKFRDLKRPLGFRDLAAWVRSDDCYLKKLGVNAVELQPIQQFDSEKAED
YHWGYMTTNWFAPASAYASDPARATQMEEFRDLVAAFHEEGFAVILDVVYNHVGEPNHLF
RIDKNYYFNLDFHGNFTNWSGCGNDYRADRPMSKRLIADSLIWLIERYGADGFRFDLAEL
IGLPALKSVEDAVKSRFPDCILIAEPWSFRGHIAGALRKTSYSSWNDGFRDYAAKFVHNG
VNIDGLRYFLSGSPEYFATFPAQTINYTESHDDRCWLDKITECPRFNAASPTVRDRRRTH
IMFAFLLSSLGTPMLAEGQDFLRTKHGKNNTYLDGAENALDYARLKKFAGTHEFVSRWIR
FRLSSLGRLFRQRKNVSKGFFRFYPDQTNTAAVAVFNDDRAQGRLQYILTLNPRTAQTCV
QIPEARFAGFRLIANTEEFDLEGVPAEEGFGFEGGMLLLPALSCSLWIRRE

Enzyme Prediction     

No EC number prediction in MGYG000001791_00368.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	396	679	2.9e-59	0.986159169550173

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	6.43e-84	237	733	12	535	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.
cd11326	AmyAc_Glg_debranch	9.11e-82	353	722	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.
cd11341	AmyAc_Pullulanase_LD-like	2.50e-80	356	722	2	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	1.30e-79	249	724	70	587	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PRK03705	PRK03705	1.61e-51	233	722	8	558	glycogen debranching protein GlgX.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SDR66894.1	4.48e-233	21	827	14	821
QYY35929.1	2.19e-229	25	830	9	809
AKC82493.1	1.12e-222	24	827	10	812
AOS45154.1	2.40e-221	21	828	14	822
AHF89626.1	4.40e-220	27	831	13	839

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	2.06e-56	248	783	327	884	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
3WDH_A	2.65e-54	246	692	118	583	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]
2E8Y_A	1.00e-53	247	722	114	613	Crystalstructure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Y_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Z_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E8Z_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E9B_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis],2E9B_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis]
6JEQ_A	6.90e-48	246	704	48	540	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]
6JHH_A	7.66e-47	246	704	48	540	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C0SPA0	1.37e-52	247	722	114	613	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840	2.27e-46	246	809	232	828	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
O22637	3.79e-46	150	692	3	632	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
B5XTQ8	2.00e-42	234	702	9	537	Glycogen debranching enzyme OS=Klebsiella pneumoniae (strain 342) OX=507522 GN=glgX PE=3 SV=1
Q8KR69	8.70e-42	234	700	9	533	Glycogen debranching enzyme OS=Dickeya chrysanthemi OX=556 GN=glgX PE=1 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
1.000039	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001791_00368.