CAZyme Information: MGYG000001553_02062

Basic Information

• Species: Clostridium_P mediterraneense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_P; Clostridium_P mediterraneense
• CAZyme ID: MGYG000001553_02062
• CAZy Family: CBM48
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
670		78021.24	5.986

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001553	3045114	Isolate	not provided	not provided

• Gene Location: Start: 1703906; End: 1705918 Strand: -

Full Sequence      

MTIEEDLINRKNVLDVDNDFNLIENLYYHNEGLGAIYRKKKTIFKLWSPTAEKVSLVLFS
SDDENAKKKYLDMKKCLEGVWYIELKGDYHRQYYNYRIEKNDEVFEVTDPYCRAINITGD
KSMVINLDKTNPKRWKNSFSPKMSKNPIIYELSIRDFTIDEASGVREEDRGKYKGLTFTD
NEAEIKTGLNHLVELGVTHVQLMPIYDFSSSDKNVLNGEYNWGYNPRNYNVPEGIYSTNP
KDAVLRIRELKEMIMKLHDNGIRVIMDVVYNHTAESINSSFNKIVPKYYYRFNENGEYSN
GSGCGNEIATERRMARKFIIDSMIYWAKEYKIDGFRLDLMGLYDIETVEEIRKELDKIDK
DILLLGEGWKGGESTLSNENSMIKDNIRKIENKRIACFNDNLRDAIKGNVFSDSDRGFVS
GKANLEETIKFGIVGAIEHRDINYSKVIYNKYPWANESFQSINYDSCHDNYTLWDKLSLA
NKDASKEDLIDMNKLSAAIVLTSQGIPFINSGEELLRTKKKENGEYDGNSYKSSDSVNKI
YWNSKKENKDIFDYYRELISLRKNHSVFNIGSKEKINKYLKFIDENKFSEIGNLVAYTIE
CDDIDKYWSKVLVAFNGSNIDKYIELDDKGWEVILDKDKVRESGIEYIDESRVKIKRLGA
FIAVKFKNRI

Enzyme Prediction     

No EC number prediction in MGYG000001553_02062.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	189	514	2.4e-115	0.9965397923875432
CBM48	33	115	7.1e-16	0.8947368421052632

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	23	642	2	603	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	0.0	148	562	4	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	2.46e-143	25	636	59	667	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	2.83e-118	33	618	128	843	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	4.41e-101	23	618	205	914	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASW44111.1	3.42e-227	19	662	2	655
CDM69740.1	2.82e-224	24	665	24	673
AIY78793.1	2.55e-222	22	665	1	650
CDH91884.1	2.55e-222	22	665	1	650
ACD23019.1	2.55e-222	22	665	1	650

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	5.63e-154	28	582	36	578	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	8.89e-153	28	582	36	578	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	8.89e-153	28	582	36	578	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
2WAN_A	5.42e-148	28	648	313	905	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	5.94e-141	28	664	59	712	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	6.44e-146	27	662	219	839	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	4.47e-128	27	618	100	664	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q9F930	8.34e-66	22	607	447	1083	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2ZL64	2.62e-65	20	607	423	1061	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	2.75e-65	22	607	440	1076	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 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
1.000043	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001553_02062.