CAZyme Information: MGYG000000195_02378

Basic Information

• Species: Faecalibacterium prausnitzii_E
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii_E
• CAZyme ID: MGYG000000195_02378
• CAZy Family: CBM48
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
649	MGYG000000195_8|CGC1	72545.71	7.1792

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000195	3389403	Isolate	China	Asia

• Gene Location: Start: 30270; End: 32219 Strand: +

Full Sequence      

MKTPAQWKAWFESEEFARQTGYQGPLGAAYSPSGTHLRLWAPTAQSVRVDLYRKGDGGAC
IGSLPLSPWGQGVWGVYLPGDQHGKYYNFNVTTEWGSVTTADPYARAAGVNGARSMIVDL
ARTDPPGWEQDKRPVIPASKRSVWEVNVRDFSQDPASGVRNAWRGKFLAFTQQGTTLNGD
GIHPTCLNYLKRLGVRYVQLMPIFDFGSVDESRPLTRQYNWGYDPANFNVPEGSYSTDPA
RGEVRVRECKQMIQALHAAGIGVVMDVVYNHMYRFDNVLNRAVPLYYFRQNEDGSLSNGS
GCGNEFASERPMARQYFLDSVLYWAQEYHIDGFRFDLMGLYDVETMNLLRAELDKLPGGR
DILMYGEPWQGGSSALHRYEANKNNLAMLNDRIGIFCDDTRDAIKGGCFNAREPGYVEGK
PGSFWDIGGAVAAWCRSDKFPPHTPGQIVSYVSAHDNFTLWDKLLLVRYERPEFGAVDRA
ALAQNRLAAGIYLTCMGLPFWQAGEEFARTKKGQGNSYRSSPALNRLDWKRAEQFHGLVD
YYRGLIGLRNAFPRLGAVDRASPNAIAFFDLEQPLVGWRLPALPGDGAWWGALCVYYNPT
EQEQPIRLPDGRWKLLSDGTSSSLWRGDSRILSGEAVLAPVSATIFGLV

Enzyme Prediction     

No EC number prediction in MGYG000000195_02378.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	187	506	1.8e-105	0.9965397923875432
CBM48	24	108	4.3e-16	0.9210526315789473

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	143	549	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	15	620	1	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	2.31e-121	13	615	54	662	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877	PLN02877	2.78e-106	21	529	210	797	alpha-amylase/limit dextrinase
TIGR02103	pullul_strch	4.41e-101	22	529	121	728	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]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATL90051.1	0.0	2	649	4	651
QIA41780.1	0.0	2	649	4	651
ATO99834.1	0.0	2	649	4	651
CBK98735.1	0.0	1	649	1	649
AXA81915.1	0.0	1	647	1	647

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	1.59e-164	13	624	50	690	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	2.51e-163	13	624	50	690	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	2.66e-163	13	624	50	690	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	2.74e-163	13	624	50	690	ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A	7.60e-142	26	568	41	588	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	4.81e-126	22	645	221	839	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	6.24e-121	2	618	82	683	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	1.00e-73	22	538	204	799	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	5.68e-65	11	608	412	1076	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	8.04e-65	11	608	427	1091	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 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
1.000063	0.000013	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000195_02378.