CAZyme Information: MGYG000001669_00419

Basic Information

• Species: UBA7642 sp900539865
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-288; UBA7642; UBA7642 sp900539865
• CAZyme ID: MGYG000001669_00419
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
904		102261.31	4.6817

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001669	1366807	MAG	United States	North America

• Gene Location: Start: 60781; End: 63495 Strand: -

Full Sequence      

MKKASKLLVASLLTITLVGCGTQKPPVTESTKPDSSNTPTSDTVDTSVPDSQVEPEPELP
EVDADVGFTIHFDNAKMENGKYLYNLWLWSDDNTMPGEDYQFNGTDSYGAYARYQFVDFP
KTLINSKLGFIVKQNKPWAENPAKDVDGDRFLDFSEIERDKYGYYNIYLKSKDPEIYTTA
DGKIKEKITHFNVDYNAVDGYYILMKTNVAFDDFEITKNGVVIFNMTIGADSLIEESTTM
RLYHIGNDLPDFKDSYHLKVTFENTTLEQEIDYSPLYSSAEFDALYTYQGELGALYTKEK
TTFRVWSPISSSVKLRIYDNGTPASLGGDDLFTEYDMVPGEKGTFEKTLDADMAGKYYTY
VVTNPFFQKEEVVDPYAKSCGLNGLRGMVVDFAQTNPTGWEDVTLHNYDSTQLTVYETHI
ADLTSSKTWNGTSAKAKTYQGFAEEGTTYTKDEVTVKTGFDHIKELAPNAVQLLPIFDQA
NDEREENREFNWGYNPLNYNCLEGSYSSDPSDGYARIKEFKSLVQSYNKAGINIIMDVVY
NHVNGLDDSNFNILMPKYYFRYNQGKASNGSGCGNETASEMPMYRKFMIDSTSFWAKEYK
LGGFRFDLMGLHDLETMNMLTKNLHDNVNPSLTVYGEPWTGGTSALEKPSANQGSIINYQ
GFGQFNDQMRDNLIRGGLSAVTDKGWITDTARVSSIMGMQNGIVGKTLNYKTEPYKTVNY
VTCHDNYTLHDRIQKAGIKDPETIKKMAMLANSVVFTSQGITFMLAGEEFLRTKNGNGNS
YNASYEVNALNYDLKVKNLDMFKNYQKLLALKQKKELFGKTREEIDENIVIHKNKNYSLI
WYDVTDTVNNVTYRIAHTNGVKADDKFVDFAGYELYLDTLNANTVLSDTTPLQNFQTIIA
SKKL

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	461	769	3.2e-96	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	281	846	1	561	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	1.34e-173	411	812	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.
COG1523	PulA	8.99e-95	277	822	52	595	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	9.80e-78	57	866	90	949	pullulanase, extracellular, Gram-positive. 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. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.
PLN02877	PLN02877	1.59e-76	283	792	206	797	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOS39053.1	5.25e-246	59	902	47	887
VEU82346.1	1.83e-165	84	893	45	870
QLY39684.1	4.07e-157	84	863	87	883
VEU81131.1	2.06e-156	84	855	46	824
QWB95757.1	6.97e-154	70	853	32	836

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	9.09e-112	280	825	28	572	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]
6JHH_A	1.33e-110	280	825	28	572	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	1.33e-110	280	825	28	572	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	8.80e-109	286	854	311	866	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	2.13e-108	278	812	49	611	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	4.70e-107	79	829	31	763	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.32e-78	279	793	93	594	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	1.40e-58	85	774	246	935	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	1.45e-58	85	774	261	950	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	1.96e-58	85	774	268	957	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000054	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001669_00419.