CAZyme Information: MGYG000000088_00193

Basic Information

• Species: Streptococcus lutetiensis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus lutetiensis
• CAZyme ID: MGYG000000088_00193
• CAZy Family: CBM41
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2218		246019.53	4.3393

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000088	1947463	Isolate	United Kingdom	Europe

• Gene Location: Start: 193827; End: 200483 Strand: -

Full Sequence      

MKKVSRLSFPEKREYFGIRKLKVGVASVAIATALFWGAGLTSVSADQITAQAATSEVVSE
TSSPDDSSEALLESEKAVDVNQTIETVNASDVVDNSESQSTEPESPVVEETEPESQPQEV
ISQTQEVQGTAATAEIADVKTVTSAENSNQVNLLKSSQPDNQVSNPPIAEDTIRMHFQAV
TDDNYTQYDLWTWGAVAEPSDGNNWPAAATPFSANQKDDFGYYIDVRQAASHGDIGYLLL
KNGEKTSDSDQSIKPLSKDVNEVWVTSDFMTYSYKLLADDRIIRINYKRDDGNYDGWGLW
AWGDVAGQFGAWPSDALDFTQEGAYGRYIDLPLSKLLDSNIGFLLVNQNDPEKAGNKTLD
MSFSDRDIHSQIFLHNDDATVYTNPYYIATVTGQDFSKATPGVHNISVSASSYRPFNYNE
TDLIDVTVTNPENVEITRMQIDTAQIGGGVIEISPELNRVTITATSDTQPGTYDLPVRVF
DKDNGYYDTTVSVTVTKRVKQAGEVDWDEQVIYFMLTDRFYNGDPSNDNPYHQDYAGAVN
QAGVYKGGDFKGVTAKLDYLKQLGVTSIWVTPIVDNIPQDVSTEAGKEYYAYHGYWADDF
EKLNPHLGTLDDFHELIDQADERGINIIVDVVLNHSGYGTEDKFTGMVRTPEEDKGDDIQ
GSQSGLPDFKTEDAAVREQLVAWQTAWLEKSTTAKGNRIYAFRVDTVKHVDDTTWQYFKN
ELALKDADFHLVGESWGANYKDTKGDLGTGSMDSLLDFGFKDIAKLLVNGRLKEANDELI
ARNDVLTSAYTLAQFLGSHDEDGFLYSIGGDLNKLKLTATLLLTAKGQPVIYYGEELGQS
GANNWPYYDNRYEFDWDDVAGNAILEHYQKLLAFRRDNSELLARGSHSTVAVNDSQGWLL
AKRANDSDAAYILYNLKDQSQKLHLLLSEAATVTDYYTGTTYQALLGQDGQYYLDIEAPA
ISKGGTMLLKVSAGAIIQAFIAQTEEEPIAENTLRVHFKTLPSDDLASLGLWTWEDVEHP
SESWPNGAINLSNLKHDAYGYYIDVKLVNGNRHKVGLLINNTSGENVSGEKVVNLISQDM
NEVWFDEDYNANYYAPLEKGKIRINYYRSDGNYKNLAIWLWGSADSSITSRLGSWPDGVD
FENFGKYGAYIDVPLADFNEIGFLLLDESKEGDAAKIQPDNYTFKDLANQTQIFLKDEDK
TIYTNPYFVSTIRLTSAQQISQSELVAIISNLADADKAELLENLKVTDKAGNVVAITDIT
LDKASNKVIIEGDFSSDGLYTVSYNGDQYQAQQSWQYTDSKYAYDGDLGARVFDNGVRVD
LTVWSPNADNVSVVLYDKNDQTKVVGKIAMTKGDKGQWSASLTSSLGLGISDYRGYYYHY
EITRGKETVLALDPYAKSLAEWNSDLIGTDPSYKVAKAAIVDTSAIGNQDLTYANIKGYK
DREDAIIYEAHVRDFTSDTAISEELRNQFGTFAAFAEKLDYLQSLGVTHIQLLPVMSYYY
VNEVMNNKRLTDYASSNTNYNWGYDPQSYFALTGMYSENPADPAKRIEEFKNLINEIHKR
GMGVILDVVYNHTADLAILEDLEPNYYHFMEADGKAKTSFGGGRPGTTHYMTRRMVLDSI
AYWTKEFKVDGFRFDMMGDLDAETVQMAYDKAKALNPNVIMLGEGWITYAGDANDSRQPA
DQTWMAHTDSVASFSDDIRNLLKSGYPSEGAPCFITGGVKNLQELFNSIKAQPNNFTADD
PGDVIQYIAAHDNLTLHDIIAKSIHKDPSVAENEAEILRRQRLGNLIILTSQGTAFIHSG
QEYGRTKQFRDEAYKTPVATDQVPAKSDLLTNADGTLFVYPYFISDSYDSTDAINHFDWA
KATDGKVYPENAKTQAYTKGLIALRRSTDAFTLKTKADVDSKVKLITIPNENGVGQEDLI
IAYQTQASNGDIYAVFVNADSKARDFVLSDDYKALLNAEVLADADTAGVDAILNPKGVAF
TENSITLNPLTATILRLRKANAETERTLYDQASGVSVILAPGEREEITQIEVHHKETNDS
QTSSVLQGKDYDLYDIEPEDAYGYVVSTTQKDQVILPIDAGKAVAEVFYLPENAQPQLLA
FREVSKLVAGQVVKFVIFDVDHLSQYGIVYQDQVAKTEVPANSNQVAKVTAPTQTQTGVW
NQAASRVLSDLQKVAVTENSTVALPETGQKDSNTLTFVGLLSLASLAVLEVKRRQKSH

Enzyme Prediction     

EC	3.2.1.41	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1470	1806	1.1e-123	0.9964788732394366
GH13	548	842	2.1e-104	0.9931972789115646
CBM41	283	386	4.6e-24	0.9705882352941176
CBM41	1101	1207	5e-22	0.9803921568627451
CBM41	992	1096	4.3e-20	0.9803921568627451

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02102	pullulan_Gpos	0.0	989	1997	1	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 (.
COG1523	PulA	0.0	1239	1998	3	692	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	2.06e-154	1443	1885	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	7.38e-123	1299	1970	3	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	1.03e-77	1299	1995	116	894	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
AEZ62583.1	0.0	1	2218	1	2218
QGZ27537.1	0.0	1	2218	1	2218
QGX00907.1	0.0	1	2218	1	2218
QIM45704.1	0.0	1	2218	1	2208
QGX47250.1	0.0	1	2217	1	2217

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FAW_A	0.0	1176	1999	2	815	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	1294	2007	1	714	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA1_A	0.0	990	1997	5	1011	Productcomplex of a multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA2_A	0.0	1294	1997	2	705	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA in complex with an inhibitor. [Streptococcus pneumoniae TIGR4]
2J44_A	4.72e-73	991	1209	1	215	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	986	2011	115	1139	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	0.0	986	2011	137	1161	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2UNG0	0.0	986	2011	130	1154	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
O33840	1.80e-70	1102	1906	23	766	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.11e-63	1299	1908	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
0.087585	0.892804	0.018204	0.000705	0.000372	0.000321

TMHMM  Annotations     

start	end
21	43