CAZyme Information: MGYG000003186_01673

Basic Information

• Species: Gleimia europaea_A
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Gleimia; Gleimia europaea_A
• CAZyme ID: MGYG000003186_01673
• CAZy Family: CBM41
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
756	MGYG000003186_5|CGC1	83742.57	4.4101

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003186	1919828	MAG	United States	North America

• Gene Location: Start: 84487; End: 86757 Strand: +

Full Sequence      

MRVKSLWAGLLSLVLLFAGLVAVPIQANATETSVDVKVKPLASVSESDYGNYSVWLWYSG
EDGKSVPLHVGADGELQAAFSIPEGATNAGMLVRRAQDGNEWAHQSQDVTLEVGKNLQVS
VVETEQSKNWQIDVTEQAAPSPEPGENPDPSSYTAEITVHYVRYTGNYVGWNIWTWLPNQ
DGQSVALTEGTATWSVESDQPITRVGVILRRSTPDNEWAEKNTSDDLFITEFKDGKAEVW
IAQGDPNVYYSQDDVPATPDLSCHELYSKEFNDKYFYDGELGSLYTPASTTFRLWAPTAA
SVSLVNYSNSGEVLPMTKGERGTWEYVFEGDANMMEYRYRIEFEDGKVDESPDPYARSST
ANSTRSVVIDVANVNPQGWDGARMKPFSGIEDATIYEAHVRDMTIAPNNGISNKGKFLGL
TETGTKTEKGNVSGLDYIKSLGVTHVQFLPMYDFYTVDETGDLGYDKQYNWGYDPVNYNV
PEGSYASDPTDPASRVRDMKAMIDAVHDAGMYVVMDVVYNHVYDTQLSPLQRTVPGYYFR
HTDGCALQNGTGVGNETASEQPMMRKYMIDSLKFWAQEYSIDGFRFDLMGIHDVETMNEI
RSELNKIDKSIVMLGEGWNMGNHPEGVKGANQDNATLMPGISFFNDKFRDTMKGTHNTQA
GTGYVSGGGADNVAWDVFNLIKGANHVRNYADASQSVNYNEAHDNLTMYDKLRGSLPGAS
EEDIVRRHAFATQIQFLSNGANFVHAGQEALRTKGG

Enzyme Prediction     

No EC number prediction in MGYG000003186_01673.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	435	749	8.4e-111	0.9965397923875432
CBM41	156	252	8.2e-16	0.9705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	270	756	1	490	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	0.0	391	756	1	370	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	1.44e-113	257	754	41	524	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	3.39e-100	272	754	116	710	alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. 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 is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102). [Energy metabolism, Biosynthesis and degradation of polysaccharides]
TIGR02102	pullulan_Gpos	4.13e-93	45	754	121	814	pullulanase, extracellular, Gram-positive. 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. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOX06609.1	4.50e-234	267	756	3	492
AKK04760.1	2.09e-195	265	756	8	504
VEH04954.1	2.07e-183	266	756	3	509
AKA96305.1	2.93e-183	277	756	13	489
SNV14072.1	4.01e-183	277	756	13	489

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	2.15e-146	254	756	16	522	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]
6JHI_A	3.35e-145	254	756	16	522	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	3.35e-145	254	756	16	522	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
2E8Y_A	2.12e-126	271	756	96	577	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]
3WDH_A	3.36e-126	268	756	97	578	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	3.44e-127	157	754	23	707	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.16e-125	271	756	96	577	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2UNG0	2.61e-67	149	754	341	950	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	3.31e-67	149	754	326	935	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	3.58e-67	149	754	348	957	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000846	0.998310	0.000207	0.000254	0.000185	0.000176

TMHMM  Annotations     

start	end
5	27