CAZyme Information: MGYG000000515_01879

Basic Information

• Species: UBA2882 sp900549665
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA2882; UBA2882 sp900549665
• CAZyme ID: MGYG000000515_01879
• CAZy Family: CBM48
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
410	MGYG000000515_11|CGC1	45966.61	4.1004

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000515	2818145	MAG	Fiji	Oceania

• Gene Location: Start: 54914; End: 56146 Strand: -

Full Sequence      

MTIETKRYMILFEGNDYPIIMSTIYSTEKFEKEFTYSDRDLGATYTPEKTTFRVWAPTAD
TVTLNLYGSGTPGTDDLVEQLPMTTDVNGTWITEKEGDLNGTYYTYLVSVGGNENEACDP
YARTTGVNGKRAMILDLASTDPDGWENDTNPNAGMAYNDAVIYELHVRDLSSDESSGIQN
TGKFLGLTETGTTTASGIPTGLDHMKDLGITHVHLLPIYDYASVDETQSDKPQFNWGYDP
ENYNVPEGSYSTDPYNGAVRVAEMKQMVKVLHDNQISVIMDVVYNHVYNASDFCVNQIVP
GYFSRVNEDGTYSNGSDCGNDTASERSMVRKYIVDSVKYWAGEYHIDGFRFDLVGLIDTE
TINEVVTEVHKTHPDVIFYGEGWTMDTAGQFRIEKDDLIEFVKNSAFWSE

Enzyme Prediction     

EC	3.2.1.41	3.2.1.-	3.2.1.68	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	202	388	1.2e-87	0.6401384083044983
CBM48	40	125	1.8e-16	0.9078947368421053

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	4.84e-173	30	388	2	355	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.
cd11341	AmyAc_Pullulanase_LD-like	1.93e-143	158	395	1	240	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.
PLN02877	PLN02877	5.13e-91	34	383	209	598	alpha-amylase/limit dextrinase
TIGR02103	pullul_strch	1.72e-89	41	383	128	527	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]
COG1523	PulA	4.56e-87	51	383	70	384	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADL35847.1	9.27e-190	4	387	209	592
BCN30228.1	5.55e-156	31	383	22	370
VCV21250.1	1.95e-153	30	407	10	399
CBL10489.1	6.24e-153	30	407	14	403
CBL13024.1	1.21e-152	30	407	13	402

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	8.21e-137	29	388	29	386	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]
6JHI_A	8.21e-137	29	388	29	386	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	1.30e-135	29	388	29	386	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
7LSA_A	4.19e-111	14	383	37	423	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	6.40e-110	14	383	37	423	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	6.20e-106	36	383	220	566	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	9.92e-90	14	387	80	441	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	1.56e-59	3	390	171	598	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
P07206	5.75e-58	51	393	314	725	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
P07811	1.47e-57	42	393	315	735	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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000515_01879.