CAZyme Information: MGYG000000246_00165

Basic Information

• Species: Streptococcus pasteurianus
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus pasteurianus
• CAZyme ID: MGYG000000246_00165
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1159		127874.67	4.0657

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000246	2159802	Isolate	China	Asia

• Gene Location: Start: 166174; End: 169653 Strand: +

Full Sequence      

MLKDTEVLYGKGKSALFWSASLANIVSADQVSAETATELVTNQWEIAEQANEVAQSKTDI
LADMQAEVENTELTISEDDTQTVVTETDMDITLSDFNELGFLLLDESKEGDDAKIQPDNY
SFKDLANHTQIFLKDEDKTIYTNPYFVSTIRLISVQQTSPTEIVAIVSNLADADKDELFE
NVKVTDKDGNLMTISDLVLNPETNQSTIIGDFSQLLAPYTVSYAGDDYQAKTNWQYTDSL
YAYDGELGARVSEEGVRVDLTVWSPSADSVSVVLYDKDDQTKVVGKIAMVKGDKGQWSAA
LTQESGLGVSDYRGYYYHYEITRGDETVLALDPYAKSLAEWNSDLIGTDPSYKVAKAAIV
DTSTIGNQELTYSDISGYTDREDAIIYEAHVRDFTSDIAISDELQHQFGTFAAFVEKIDY
LQELDVTHIQLLPVMSYYYVNELANAERLTDYASSNTNYNWGYDPQSYFALTGMYSEDPT
NPAKRIEEFKNLIAEIHKRGMGVILDVVYNHTADLAILEALEPNYYHFMEADGTVKTSFG
GGRPGTTHYMTRRLVLDSIAYWVDEFKVDGFRFDMMGDLDAETVQMAYDTAKALNPNIIM
LGEGWISYAGDANDSRQPADQTWMSQTDSVASFSDDIRNLLKSGYPSEGAAAFITGGAKD
LQTLFNNIKAQPSNFTADDPGDVIQYIAAHDNLTLHDVIAKSIQKDPAVAENEAEIQRRL
RLGNLIVLTSQGTAFIHSGQEYGRTKQFLDEDYKTPVSADKVPAKSDLLTNADGTPFEYP
YFISDSYDSTDAINHFDWAKATDSEAYPENTQSQTYTKGLIAIRRSTDAFTLKTKEEVDR
NVSLITIPNENGVGQEDLIIAYQTIASNGDIYAVFINADTVARDFVLTDDYRNLLSAEII
ADGKQAGVEAIENPSGVTMTETGLTLEPLTATILRLKKASAETERTLYDEASGVSVILGA
GERDDIKKIKVSHQETNDVKTPEVLKGTDYDLFDIQPTDDFGNVLAITKTVRVILPIDAG
KTVAQVFYLPENGQPQSLVFEEISRTVAGQTLKFVIFDTEHFSQYGIIYAQEAAQSSDMA
TQTSAETGVTPDDQAQASVVETTTTPITVDANLETLTATDTAEILPATGEKDGTLLTFAG
VLSLASIALLELKRRKKSE

Enzyme Prediction     

EC	3.2.1.41	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	409	745	1.9e-121	0.9964788732394366

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1523	PulA	0.0	210	935	35	690	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	0.0	89	936	160	1004	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 (.
cd11341	AmyAc_Pullulanase_LD-like	4.13e-157	382	824	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.
TIGR02104	pulA_typeI	2.19e-129	236	909	1	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.
TIGR02103	pullul_strch	1.42e-78	238	908	116	880	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]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SQI08991.1	0.0	1	1159	1	1159
BAK30402.1	0.0	1	1159	1	1159
QIX74700.1	0.0	84	1159	1	1076
QKI00055.1	0.0	89	1159	1159	2230
ACX81318.1	0.0	89	1159	1159	2230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2YA2_A	0.0	232	938	1	707	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA in complex with an inhibitor. [Streptococcus pneumoniae TIGR4]
2YA0_A	0.0	233	946	1	714	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA1_A	0.0	89	938	163	1013	Productcomplex of a multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
3FAW_A	0.0	113	969	1	846	CrystalStructure of the Group B Streptococcus Pullulanase SAP [Streptococcus agalactiae COH1],3FAX_A The crystal structure of GBS pullulanase SAP in complex with maltotetraose [Streptococcus agalactiae COH1]
6JEQ_A	4.65e-74	238	848	31	582	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0H2ZL64	0.0	89	986	277	1162	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	0.0	89	950	299	1161	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2UNG0	0.0	89	950	292	1154	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
O33840	2.66e-68	241	934	219	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	2.31e-60	238	847	97	636	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX 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	0.000012	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000246_00165.