CAZyme Information: MGYG000003507_00682

Basic Information

• Species: UBA733 sp900767825
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-826; UBA733; UBA733 sp900767825
• CAZyme ID: MGYG000003507_00682
• CAZy Family: CBM41
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
895	MGYG000003507_14|CGC1	99733.41	4.8095

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003507	1599809	MAG	Fiji	Oceania

• Gene Location: Start: 7989; End: 10676 Strand: +

Full Sequence      

MKKIKTYFVIACASILVSSCGEANGSTSKTDSTGVSTNTGYTFPETPVYDEPSFQIHYLR
NDNDYSPWCLWLWSEDKDGADYEFNGGDATNGAIASYPLSKLGLSESSTLNFIVKKGREG
NWLAKDVDDDREIDLSSLDKDSNDIYHIYLKSGDANVYTSKDYIVPEKISYAKFNSVNNL
TQVILETSLPINKAVLKRDDVVLKELTLSKPKKFVRIEGIEGEVDFLAKYTVEVTFNESN
NVLSKEVSLNSLFGTAEFNAKYEYKGSDLGVTENDGTFTFKVWSPFSSSIEVRIYNSGTP
KSLDESGDDAYTTITLTKGEKGVWSGALKQDLYGKYYTLFVKSKDYKQGIEIVDPYAKGC
GINGLRGMIVDFNAAKPTNWDGFKAPVHDRKSMVVYETHIADITSSSSWTNDAEIRKLEK
TYAGAIKEGTTYQKDGKIIKTGYDSIKDLGVNAVQILPIFDQANDERKENRTFNWGYNPL
NYNCIEGSYSSNPYDGYTRIKEFRELVEKFGSDNMSIIMDVVYNHVNGAKGSNFDVLAPG
YYFRYDGEKLTSKSGCGNDTASDHAMYAHFMRDSVKFLAETYKLSGFRFDLMGLHTLEAM
NEVVEAARSVNPDIVIYGEPWEMEESLGLTMASQKNLASFEGFGAFNDKMRDALIKGGMS
AVDELGFATNPRGGSESDMRSVVYGIEGKTSTISFDPDKTVNYASCHDNYTLYDRAFMAG
IDDEELLKKMPVLANSIVLTSQGTSFILSGEEFLRTKDKVNDDGTHTKDGNSYASSYEVN
ALDYDLKSKNMDVYAIYKKLIYLKTHVDGLALTKEGVTSNLNVAASKGQITYTIKDSLNN
KEYKIVHNDGASTHEAMDFAGYELYLDTIDVNSTRKLTNNEKANRFQTLIGVKSL

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	444	752	1.1e-88	0.9930795847750865
CBM41	55	161	7.7e-18	0.9509803921568627

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	1.68e-168	257	848	1	576	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	2.26e-158	393	801	3	403	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.
TIGR02102	pullulan_Gpos	1.87e-85	49	849	101	947	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 (.
COG1523	PulA	4.21e-81	246	806	45	588	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877	PLN02877	1.86e-74	262	793	209	806	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOS39053.1	8.44e-234	19	894	18	888
QWB95757.1	6.00e-148	56	853	32	849
VEU82346.1	4.43e-146	51	869	28	857
VEU81131.1	9.59e-139	55	895	33	884
QLY39684.1	8.80e-137	56	868	75	892

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	2.89e-98	235	852	29	665	ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A	6.29e-98	256	836	28	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]
7LSR_A	4.04e-97	235	852	29	665	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	4.22e-97	235	852	29	665	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	4.31e-97	235	852	29	665	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	3.98e-91	48	804	17	745	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	2.26e-79	219	806	52	616	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	1.24e-59	55	757	232	935	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	1.29e-59	55	757	247	950	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	1.75e-59	55	757	254	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	1.000031	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003507_00682.