CAZyme Information: MGYG000003476_00082

Basic Information

• Species: UBA7642 sp900549915
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-288; UBA7642; UBA7642 sp900549915
• CAZyme ID: MGYG000003476_00082
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
720	MGYG000003476_4|CGC1	83341.2	9.3426

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003476	1713396	MAG	Fiji	Oceania

• Gene Location: Start: 33162; End: 35324 Strand: +

Full Sequence      

MDKQYLSCTAINNQNLAVYVAKKLTSTILTSFRLYIDGKFSLLLKPVSRSESNSALIYNL
KLPSGFSFIPGNRYEVLTPHNFFVPINISFLARTKKFEEKYRYDGELGAIYSKKKTVFRV
FSPFAASRSLILYFKGKWKSFVRQKDSEHGIFEISLDGNYDKAGYLFEAEIFGSRYRVVD
PYAFALSSNSRLGYVIDRNKIKAIPSNRDKLPKFENETHAVIYEAHVRDRTSLTSRRDRG
TFAALSRGGEKNKDGFPLGRDYIASYGFTHVQLRPVRDYQTVNDEAVFDSYNWGYDPRFY
FAPEGSYSTDPMDPYARNRELKELISSFHERGIRVNLDVVYNHVFSQDFNSLGLLCPEYY
FRHNPDNTLSNGAGCGNDLESRNYRVKKLIKDSIRHWIDAFDIDGLRFDLMGILDVETIK
ECYEEAKARKNDFRFYGEGWDLYTNLPGSEKASRNNAYKIPFCGFFNDRFRDVVKGKSNA
SELSVRGYLLGDCNYRDGFKHVRLGSCVPLAFAPLFSSYHQSINYVQCHDDACLYDKIRI
ANPDAKEPEVRKRIKRINVALLFALGVPFFSEGQEIGKSKSFNFNTYNAGDKINGFDYAL
AEKRKDRMNFLTDAIKRKKRFRLRSGNEYEELDKHRDFEDLNSGALKINYHRKDFDFYLI
FNPTKETIRYDFPEDVRMIFSDGGDVSDSRFRVHLAILPGCSVNVFYKEKANGKLSKEDR

Enzyme Prediction     

No EC number prediction in MGYG000003476_00082.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	261	575	5e-90	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	97	675	2	589	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	1.77e-160	218	616	1	404	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	9.70e-103	99	709	59	692	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	2.14e-72	101	690	119	828	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	7.33e-70	85	589	290	823	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
QOS39282.1	1.70e-264	1	710	1	713
QJS20077.1	3.40e-129	14	688	15	692
AIK38209.1	5.52e-128	71	668	68	658
AJI17510.1	5.52e-128	71	668	68	658
QQR24928.1	1.78e-125	71	683	71	681

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WDH_A	9.72e-117	32	598	37	594	Crystalstructure of Pullulanase from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDI_A Crystal structure of Pullulanase complexed with maltotriose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDJ_A Crystal structure of Pullulanase complexed with maltotetraose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11]
2E8Y_A	3.57e-115	86	676	85	676	Crystalstructure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Y_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Z_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E8Z_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E9B_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis],2E9B_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis]
6JEQ_A	1.40e-102	96	673	29	618	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	2.08e-101	96	673	29	618	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	2.08e-101	96	673	29	618	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C0SPA0	1.39e-114	86	676	85	676	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840	1.25e-88	99	674	217	806	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
A0A0H2ZL64	1.78e-56	25	638	349	1005	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	1.83e-56	25	638	364	1020	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	1.84e-56	25	638	371	1027	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
0.999982	0.000047	0.000005	0.000000	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003476_00082.