CAZyme Information: MGYG000002982_00483

Basic Information

• Species: Streptococcus rubneri
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus rubneri
• CAZyme ID: MGYG000002982_00483
• CAZy Family: CBM41
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1249		139345.2	4.8409

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002982	1039311	MAG	United States	North America

• Gene Location: Start: 34; End: 3783 Strand: +

Full Sequence      

MKRNTQANDEKVLRYSLRKYKLGLASVTIGAIFLSFSAVQVVKADEAVSTLESSTQVEPA
DSSLTTSGLVTETPAAPVTAESTSVSKVNEPVSLPEENTSRTKTTKLTETSENTPKTVST
NNSQALTNASEDPIAEGTIRLHFQELPSQDKSSLGLWTWDDVEKPSENWPTGAQSFKDAK
TDDYGYYLDVKLKNEQAKKISFLINNVKGDNITGDKSIELLSPEMNEAWLDEKFKVYSYQ
PQAEGTVRVNYYRTDGNYDKKSLWYWGDVENPSSAAWPDGTDFTATGKYGRYIDIPLKAV
AKEFGFLLLDESKSGDDVKIRQEDYKFADLKNHSQIFLRDDDPTVYTNPYYVNDIRMTGA
QHVGKEKIEASFSTLAGAQKEELLKRTKITDAQGNPVTISDLLLDEAGKKVTYTGDFSQV
DQSYTVQYDNDRFTTKMNWRLKDEAYSYDGTLGAHLHEAGKKVDLTLWSPSADKVSVVIY
DKNDSEKLVGRVALEKGDRGTWKQTLSADSGLDIQDYTGYFYQYEIERQGKTFTVLDPYA
KSLAAWNSELAKTDDVHKVAKAAFVDPSRLGPSDLTYASIPNFKKREDAIIYEAHVRDFT
SDPALASELKSQFGTFASFVEKLDYLKDLGVTHVQLLPVLSYYHVNELKNSERLLEYASS
NSNYNWGYDPQNYFALSGMYSTDPSNPQKRIEEFKNLVNEIHKRGMGVVLDVVYNHTANV
DIFEDIEPNYYHFMDADGTPRTSFGGGRLGTTHYMSKRILVDSIKYLVDTYKVDGFRFDM
MGDHDAASIEEAYKAARALNPNLIMLGEGWVTYAGDENSPVQPADQSWMKKTDTVAVFSD
DVRNNLKSGYPNEGQPAFITNGKRKIATIFKNLIAQPTNFEADSPGDVIQYIAAHDNLTL
FDIIAQSIKKDPSIPANNAEIHRRLRLGNLLVLTAQGTPFLHSGQEYGRTKQFKDPAYRT
PVSDDKVPNKSHLLVDENGKPFDYPYFIHDSYDSSDAINHFDWGKATNEDLYPENTRSRA
FTKGLIALRKSTDAFRMDNMDEVKSRVKLLTIPGENGVEEEDQVIGYQITASNGDVYLVL
VNADTKARDFALGTDFERFRKADVLVDGERAGISNLTDPKGISWTETGLRLDALTATVLR
LSAKEEVENPALPDRSEYHTPVSPSLAKVLPSQTAKPTPQLLAQKNEEPEVQDLAPHHEF
VSVENGEEASPARTLPETGEASSNLTSLAGLLLLGGLGLGMAKKGRKED

Enzyme Prediction     

EC	3.2.1.41	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	614	950	1.1e-124	0.9964788732394366
CBM41	246	350	6e-26	0.9803921568627451
CBM41	138	241	4.6e-23	0.9803921568627451

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02102	pullulan_Gpos	0.0	134	1229	1	1093	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	0.0	380	1142	1	697	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	7.12e-167	587	1029	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	8.78e-140	443	1113	3	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.
TIGR02103	pullul_strch	3.99e-80	443	1097	116	859	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
SQH66992.1	0.0	131	1249	114	1232
AYF94045.1	0.0	131	1249	114	1232
AGY38741.1	0.0	131	1249	114	1232
AGY40221.1	0.0	131	1249	128	1246
VED67760.1	0.0	1	1249	1	1239

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FAW_A	0.0	318	1148	1	825	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]
2YA0_A	0.0	438	1142	1	705	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA1_A	0.0	135	1142	5	1012	Productcomplex of a multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA2_A	0.0	438	1142	2	706	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA in complex with an inhibitor. [Streptococcus pneumoniae TIGR4]
2J44_A	1.68e-119	139	354	4	217	Alpha-glucanbinding by a streptococcal virulence factor [Streptococcus pneumoniae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0H2ZL64	0.0	3	1249	2	1256	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	0.0	3	1142	2	1148	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2UNG0	0.0	3	1142	2	1141	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
O33840	1.34e-83	243	1139	19	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	2.24e-60	443	1052	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.020495	0.977167	0.001464	0.000400	0.000238	0.000213

TMHMM  Annotations     

start	end
20	42