CAZyme Information: MGYG000000902_01404

Basic Information

• Species: Clostridium neonatale
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium neonatale
• CAZyme ID: MGYG000000902_01404
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
361	MGYG000000902_14|CGC2	40829.55	4.8194

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000902	4770522	MAG	China	Asia

• Gene Location: Start: 27889; End: 28974 Strand: -

Full Sequence      

MARRFIIDSLKYWVNEYHVDGFRFDLMGVYDIYTVKKIRSELDKIDPSIIMYGEGWSGGT
TQLVPENSALKANGPKFGKSQVAMFSDDLRDGLKGHVFTENAPGYINGKEDLEDTIKFGI
VASTQHDGIDYSKVNYSKEAWANEPYQTINYVTSHDNHMLWDRLQLSAPDASESDRLAMN
RLAATIVWTSQGIPFMQAGEEFARTKRDENGNLEGNSYKSPDSVNELDWNRIREYKDLYE
YYVGLIKLRSSHKAFRMDTTKQIQDNLTFLENGKDFKGDNVVAYVLNGKNIGDSWNKIAV
MFNSTDKAVEVQLSSEDWTVVVDGNKAGVETLGKVEGSKVILPAKSSYVLVDTESYNESN
N

Enzyme Prediction     

No EC number prediction in MGYG000000902_01404.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	201	4.6e-53	0.5674740484429066

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	1.80e-129	1	330	295	604	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	3.32e-118	1	249	173	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	4.56e-62	1	350	335	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	2.89e-49	1	351	472	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]
TIGR02102	pullulan_Gpos	1.41e-44	1	337	618	984	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 (.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANF15666.1	2.52e-170	1	359	298	656
ALS18531.1	2.52e-170	1	359	298	656
AOR95608.1	2.52e-170	1	359	298	656
ALP91823.1	2.52e-170	1	359	298	656
QUF82280.1	4.77e-167	1	359	632	990

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	1.66e-86	1	350	598	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	4.70e-72	1	313	326	617	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	6.86e-71	1	313	326	617	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	6.86e-71	1	313	326	617	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
7LSA_A	2.54e-69	1	359	368	720	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.33e-72	1	350	511	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	3.38e-58	1	316	382	675	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2UNG0	8.29e-38	1	337	754	1120	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	1.12e-37	1	337	739	1105	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	1.12e-37	1	337	761	1127	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA 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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000902_01404.