CAZyme Information: MGYG000002334_01640

Basic Information

• Species: Bifidobacterium thermophilum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium thermophilum
• CAZyme ID: MGYG000002334_01640
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
657	MGYG000002334_1|CGC21	71848.92	4.5723

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002334	2291643	Isolate	not provided	not provided

• Gene Location: Start: 2087513; End: 2089486 Strand: +

Full Sequence      

MSFAEASWPDYAGLLGSQLLDHGTVFTVWSPSAVAVTLRLFSTSDPKDGPSATVALERAQ
DGAWQHRSAERLAGTYYDYLLTFPASAVSNVPSDAIINAAEGTVTIRTADPWAKASGVNG
ERSMVVDLDSTNPDGWLSDRSPDIPASQTVIWETHVGDFSNDPHGGFPKGHRGKFLAFTD
AHTTLDNQPGGFPTGIAYLKRLGVTHVQIMPFYDYGSVDEATGGPYNWGYDPVAYDVPEG
SYSTDPYDGAVRIRECKAMIAALHRAGIRVIMDVVYNHMYENDNEFERMAPGYFCRRDDA
GGFANGSGCGNDMASERPMFSRFIVDSLVYWAREYHVDGFRFDLMGLLDTQTLNRARKEL
DKLPGGESILMYGEPWSADKTNAEPSFTLADKQGRKLLDARIGWFCDESRDSIKGNVMLE
RKPGYVNGQPSEFAELVRHAFNGWRGTEAQGKQVGQIIQYVSAHDDLTLWDKLCLTMRDD
PAHADYDATGDVQDILAANAIAAGLVLTSAGLPFMLSGEEFTRTKYGCDNSFDRSAELNW
LDWGRASRLSSLIEWYRTLIAVRKAHPDFYDGRRIALDSPEGVIAAQVGDDLAVCANPTT
NGVTVELPQNTADATRHWAVIADSTDVAAGSADGRAQVADGTELSVPARTFVVVALQ

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	197	520	3.9e-102	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	150	563	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.
TIGR02104	pulA_typeI	0.0	11	625	8	599	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	5.30e-123	23	657	68	692	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	2.74e-91	15	653	128	893	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	1.45e-84	11	543	211	791	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGH41957.1	0.0	1	657	1	657
AYZ21359.1	6.44e-250	1	655	1	659
ADP38323.1	7.41e-249	4	655	5	659
SDR90778.1	7.41e-249	4	655	5	659
BAQ32759.1	7.41e-249	4	655	5	659

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	2.11e-129	15	653	64	710	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	3.22e-128	15	653	64	710	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	3.40e-128	15	653	64	710	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	3.48e-128	15	653	64	710	ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A	4.10e-123	15	569	41	564	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.17e-104	11	624	221	815	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.89e-104	11	569	102	619	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	3.49e-57	11	547	204	794	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	2.66e-56	11	532	432	942	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	3.67e-56	11	525	454	957	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA 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
1.000066	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002334_01640.