CAZyme Information: MGYG000001157_00738

Basic Information

• Species: Gemmiger sp900540775
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Gemmiger; Gemmiger sp900540775
• CAZyme ID: MGYG000001157_00738
• CAZy Family: CBM48
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
643		71013.48	5.5567

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001157	2792015	MAG	Austria	Europe

• Gene Location: Start: 15746; End: 17677 Strand: -

Full Sequence      

MNWQQACELPYYGGSDLGANPAAEETVFKLWAPTACGVVVCLYATGTDAEPGAGERGVHE
LHREADGVWAITLPGNLHGTYYLYRVYFPDGRMQEVVDPYARSAGANGQRGMVLDLTRAA
PEGWDADARPAIPPHARSVWEVHVADFSADARSGVRPEWRGKFMGFTQPDTTLDGDGAHP
TCLNYLKGLGVSHVQLQPIFDYATVDETRPDGGYNWGYDPQNYNVPEGSFATDPFHGEVR
VRECRAMVAALHRAGLGVIMDVVYNHTYYSESCLERTVPGYWNRRWPNDSMTNGSGCGCD
LASERPMVRKFIVDSVLYWAKTYHIDGFRFDLMALEDVDTMNAIRAALDSLPGGESILMY
GEPWMGGGTNLEGGARPADKRALDALSDRIGFFCDDTRDCIKGNVFDAANAGYVNGAPQH
GYDVIHSISAWHNGAHGFWPRRAGQVVQYVSAHDNYTLWDKLAAVARRGDYDWPDADMLA
QNRMTAGIYLTCQGLPFMQAGEEWGRTKYGDHNSYKGPLSTNRLDWARAHRPEFAALTAF
YRGMLAIRRAYPRLSGAAGEPEPFLLALPGWLIGFVPEHDDTAAKGQLAVYYNPERTRQW
ASLPAGTWRKLSDGVHAGVTPFGPRFRDALELAPTSVTVLVAE

Enzyme Prediction     

No EC number prediction in MGYG000001157_00738.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	183	503	5.8e-102	0.9965397923875432
CBM48	16	104	4e-16	0.9078947368421053

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	139	548	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	10	621	5	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	6.20e-120	17	641	20	688	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	5.69e-104	14	558	125	794	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	6.16e-100	8	527	207	798	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADD61669.1	0.0	1	643	1	641
ADD61743.1	0.0	1	643	1	640
CBL01352.1	1.79e-231	11	642	27	654
AXB27559.1	2.36e-229	11	642	27	654
ATL90051.1	1.65e-223	6	639	19	647

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	5.40e-154	12	623	59	694	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	8.46e-153	12	623	59	694	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	8.95e-153	12	623	59	694	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	9.21e-153	12	623	59	694	ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A	1.60e-132	8	616	32	631	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	2.27e-120	11	643	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	5.28e-108	11	558	101	625	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	7.63e-65	8	527	200	791	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
P07206	1.27e-55	18	527	305	911	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
P07811	2.60e-54	18	552	315	977	Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA 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
1.000027	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001157_00738.