dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000001761_01325

You are here: Home > Sequence: MGYG000001761_01325

Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Gemmiger;

CAZyme ID

MGYG000001761_01325

CAZy Family

GH13

CAZyme Description

Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
642		70891.2	4.9149

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001761	2495136	MAG	Finland	Europe

Gene Location

Start: 2382; End: 4310 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001761_01325.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	183	502	3.3e-105	0.9965397923875432

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	139	547	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.
TIGR02104	pulA_typeI	0.0	11	620	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	1.58e-127	17	639	67	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	8.18e-103	14	526	125	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	2.68e-92	8	525	207	797	alpha-amylase/limit dextrinase

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADD61669.1	0.0	1	642	1	641
ADD61743.1	0.0	1	642	1	640
CBL01352.1	3.89e-220	11	613	27	625
AXB27559.1	1.57e-219	11	613	27	625
ATL90051.1	1.11e-218	6	638	19	647

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	9.82e-161	12	640	59	712	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	1.54e-159	12	640	59	712	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	1.64e-159	12	640	59	712	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	1.68e-159	12	640	59	712	ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A	2.77e-133	12	622	313	903	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	3.06e-129	11	642	219	843	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.23e-109	11	612	101	683	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	2.26e-58	8	525	200	790	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
P07811	2.80e-53	18	525	315	920	Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1
P07206	4.08e-52	5	525	297	910	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000031	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001761_01325.