dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000004555_00084

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Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA7067;

CAZyme ID

MGYG000004555_00084

CAZy Family

GH13

CAZyme Description

Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
752		82254.35	4.4618

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004555	1866920	MAG	France	Europe

Gene Location

Start: 4501; End: 6759 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.41	3.2.1.-	3.2.1.68	3.2.1.1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	217	532	9.6e-113	0.9930795847750865

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	168	575	1	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.
TIGR02104	pulA_typeI	0.0	44	655	7	605	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.
COG1523	PulA	1.43e-135	59	666	70	686	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	4.74e-117	39	556	115	729	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]
PLN02877	PLN02877	2.82e-114	39	556	205	798	alpha-amylase/limit dextrinase

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT05893.1	1.11e-250	11	712	9	714
APO32485.1	1.49e-249	39	692	30	684
QCT05892.1	2.11e-242	3	692	2	721
QCT07019.1	5.53e-226	28	690	55	720
QCT07748.1	1.77e-211	7	687	5	709

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	1.07e-236	10	689	22	726	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	1.72e-235	10	689	22	726	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	1.83e-235	10	689	22	726	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	1.90e-235	10	689	22	726	ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A	1.35e-158	44	674	313	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.34e-142	44	674	220	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.09e-120	20	636	77	675	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	3.73e-74	39	556	198	791	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
P07206	1.99e-67	50	668	305	1041	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
P07811	3.15e-64	38	626	308	1012	Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000248	0.999032	0.000203	0.000176	0.000169	0.000148

TMHMM Annotations download full data without filtering help

start	end
718	740