CAZyme Information: MGYG000002169_01137

Basic Information

• Species: CAG-1435 sp000433775
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-314; CAG-1435; CAG-1435 sp000433775
• CAZyme ID: MGYG000002169_01137
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
860	MGYG000002169_31|CGC1	94179.72	4.3817

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002169	1570892	MAG	Denmark	Europe

• Gene Location: Start: 5037; End: 7619 Strand: +

Full Sequence      

MKRKLSVILLCLLAVVCIVLVACVDDPTAGGLPTDVPESATEPTLVLHYERQNPDDYLKW
GFWIWTDGGEEGQLFKLNYQDDFGGVAMYPLSDFGAERDSLIGIIPRLIASWTKDCDADR
MLDLSQCEMGADNFIHIYLTQGDQNLYKDAEEMKYNVTATFTAYDKITVNARQEMASVTI
FEATQSVAVQNGPAKEIVCALPQNHTLRLAEGYTAEVQFADGKKVTATVDMKALYGTDAF
TDAFYFDGELGAMYSATETTFRVWSPVSTKIVLNIYQKGNGEETPVSYDMQSGQKGTFEA
VVSGDLAGKYYTYTVYNHVYSTGVEIVDPYAKSAGLDGERGMIVDFSKTNPLGWENVSPI
AYDRKQLVVWETHVADVTSSQTWTGTESNRSRFLGLIEEGTTYTEGNVTVKTGFDHIKEL
GVNAVQLLPIFDQANDESARIFNWGYNPLNYNVLEGSYSSDATDGYTRIKEFKQVVAAFN
GAGINIIMDVVYNHVNAAGGSNFDVLMPGYYFRYGANGSMSDGSGCGNETASEHAMFRKF
MIDSVCFWASEYKLGGFRFDLMGVHDVETMNMLADALKLINPNIVIYGEPWTGGTSALSS
SQQAVQSNANSLRGVGQFNDQLRDALIKGGLAAVTDKGWITNESAVSSSDVSKIMEGLKG
ITACTNSITDPNKTTNYVTCHDNYTLFDRISAAGITDEATVKKMAMLANSVVLTSNGTAF
MLAGEEFLRTKGGDGNSYQSGYEVNQLDYSLKITHADMFENYRKLIALKTHCGGLCLSQE
QVQQAYKVQSLDGGAVIVIEVTDSENGTMYTIVHANGVAKDVAVNLEGYTLYLDTLGVTQ
ELSSQTEVLPFQTLIAQKAM

Enzyme Prediction     

No EC number prediction in MGYG000002169_01137.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	415	726	3.9e-101	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	239	828	1	590	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	368	769	4	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	2.77e-110	204	828	33	635	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877	PLN02877	1.37e-84	220	750	189	798	alpha-amylase/limit dextrinase
TIGR02102	pullulan_Gpos	2.32e-72	42	731	111	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
QOS39053.1	9.08e-260	25	859	40	888
VEU82346.1	5.02e-177	1	837	1	858
QLY39684.1	1.01e-174	45	838	73	900
QWB95757.1	5.58e-166	39	826	23	854
BCR36445.1	1.60e-162	44	769	29	789

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	1.76e-117	240	769	30	558	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	2.62e-116	240	769	30	558	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	2.62e-116	240	769	30	558	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
7LSA_A	1.15e-115	221	855	43	709	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	1.69e-114	221	855	43	709	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	2.78e-113	41	798	19	773	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	9.02e-98	205	769	73	613	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
P07206	1.74e-58	201	752	254	913	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
P07811	1.40e-57	251	752	315	923	Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1
Q8GTR4	2.33e-53	201	750	161	791	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000001	1.000047	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
5	24