CAZyme Information: MGYG000000937_01516

Basic Information

• Species: UMGS403 sp900541975
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS403; UMGS403 sp900541975
• CAZyme ID: MGYG000000937_01516
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
761	MGYG000000937_14|CGC1	83950.39	4.4535

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000937	2265948	MAG	Germany	Europe

• Gene Location: Start: 13109; End: 15394 Strand: +

Full Sequence      

MLKKLIAGAVAFMLTFSAVGVTREAHAQEDYTSQARQLDKLAYEGDDLGAVYSPENTVFK
VWAPTASKVELKLYKTGSDQEKNAGLIAQSPMEYNPENGVWTVTKQGDLNGVYYTYLVTV
EGKTNETADIYAKAAGVNGERSMVVDLDVTDPDNWENDRHILFDHQTQATVWEVHIKDFS
SSPSSGVSQDNRGKYLAFTEEGTTLNGEGEVPTCVDYLKALGVNCVQINPFYDFGSVDES
KTDDQEAFNWGYDPKNYNLPEGSYSSNPYDGAVRIREAKQMIQALHDAGIAVVMDVVYNH
TYTGEDSFFNKTVPNYYYRFHEDGSWANGSGCGNDTASERAMYRKFMVDSVAYWVEEYHI
DGFRFDLMGLHDVETMNAIREKLDSFENGEKLIMYGEAWEMAQATDATMACQDNMHLLNE
RIGAFNDGMRDILKGDNFQAADIGFIQGRGAPSLVKKGIKAATDEWARQPSQTVSYMSCH
DNMTLYDKLVASVLGEKEDYRARNEQLVQMNKLGACALLTSQGIAFMLAGEEMARSKDGD
HNSYQSSVQLNQIDWNNLALYGDLAAYYMGLLAIRNNFAPFTQDDNTSVAHMVFYENTDK
HVVAYTLENTVTNATQWDAVTVLLNSNTDKDVTVQLEGAAANKDWVIVADGQSAGLTSLG
EITDGKAVLPRSSAMVLVDKESFARVKLDADLSLQQVLQNAAGTVEEDASQAQASSTAQQ
QTGAGAQFFTGHGVLWLLGAAAAAVVAIAGFVFYKKRKNKK

Enzyme Prediction     

No EC number prediction in MGYG000000937_01516.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	216	532	1.8e-110	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	167	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	38	658	3	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	8.92e-127	30	677	36	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	2.23e-109	38	678	115	895	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	4.64e-101	38	555	205	797	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT05893.1	1.98e-248	2	683	3	682
APO32485.1	3.95e-239	30	683	22	672
QCT05892.1	3.05e-230	10	704	14	730
QCT07019.1	5.38e-223	10	685	26	712
QCT07748.1	2.40e-211	11	683	10	702

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	6.34e-230	21	683	36	717	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	1.02e-228	21	683	36	717	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	1.09e-228	21	683	36	717	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	1.13e-228	21	683	36	717	ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A	9.56e-153	19	609	2	592	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	7.12e-133	38	677	216	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	2.27e-118	39	629	98	666	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	8.54e-68	38	556	198	791	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
P07206	7.77e-65	42	677	298	1073	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
P07811	1.09e-64	20	598	287	996	Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000271	0.999008	0.000190	0.000179	0.000176	0.000154

TMHMM  Annotations     

start	end
732	754