CAZyme Information: MGYG000001523_03000

Basic Information

• Species: Gracilibacillus massiliensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_D; Amphibacillaceae; Gracilibacillus; Gracilibacillus massiliensis
• CAZyme ID: MGYG000001523_03000
• CAZy Family: CBM41
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1962	MGYG000001523_13|CGC10	221063.7	3.9797

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001523	4207224	Isolate	not provided	not provided

• Gene Location: Start: 517863; End: 523751 Strand: -

Full Sequence      

MKKKKQVLVFFMIGVMFLSLFSGIAPLPDVSAEQSELEEVEEGFLRIHYDHGDNDTSEIG
AWLWGDVTTPSDETSDWPNGTWFEEGGIDDYGVYIDVPLEEGAETVGLKINNRAGDDVTN
DISIDILADEMKEVWLSSEGIVYYYKPIEFEENIVRVHFQTDEASHEPWGIWTWGDVATP
SNGENWPMDAHPFLDDVVGEYGAYVDIQLNDNPSNIGFLLAERIEDGDQTGDFSFDDLDN
HRQIFLEEGNEEVYTNPYFISTEKDEDLPDEYEGEQDIKVEANVNQSFNYNEHAVLSVDI
TNNSELGIRTIYADTTALGGTERLHISPELNEVTLTVQHEITAGEKTIPVTAVDEEGGTY
TTEVTATVSPREIGEATTDWDESIIYFMLTDRFYDGDPSNNDPYDLNYDGYDNPRGTYQG
GDFKGVMEQLDYLDELGVNTIWITPIVENVGYDVNYDASEGSYFAYHGYWAKDFEELNPH
LGTLDEFHALIDAAAEREIQIMADVVLNHAGYGLKQDDDLSIDGPAGYPTDEDRSRFDGM
LRDKSGSGDEGMELSGLPDFKTEKSNVREQLVAWQKNWVEKSTTDNGNSLASYRVDTVKH
VDGTTWQHFRNELTKLKPDFQLIGEAWGAGKSDDQGYLGSGMMDSLLDFEFKGTARNFVD
GSLESANEALTIRNETIDNTRLLGQFLGSHDEDGFLYSLDGDEGKYKVASSLQLTAKGQP
VLYYGEELGQSGANNWPEYDNRYNLDWNNIKDNDILEHYQKVIGFRNDFSDVFAKGSRQQ
IAGSDQDQYLMFERSFQNENIYVALNVAESKQTVSVNVENADVSITDHYQGVTYEVNQTN
EENYQITLDLPARSEGGTALLTSSGGAILSEATNVEVPEVTEIPENHLRVHFPGNEHDFD
ELGLWVWEDVASPSESAGGWPNAALNFDETNQTEYGRFVDIELAENPEKIGFLINHANGD
NLSGDLFVNLLTKEMNEVWLTDNYEVYLYPPLKKEDGKLRVNFYQNEESYNNIGLWTWGD
VAEATTDWPDGAHFLSDQRLGLNGSYFDLPLAEDPNQINFLFLNKETGWQSGDLSFDKFD
EHTQIFVRSGDDTVYTNPYFVTEEGILSGEVISDQKLELRFNSVAELDQEKLAEELEVTD
KEGDIVEFTSISISEENNNVIVHGTFDLEKAPFTITHNGREAIATIGWRLKDEMFGYDGD
LGLTLHDETNATLKLWSPSADKVSVILYNKNDQKQIVKDDIEMTKGDKGVWQVELNKETT
GIDSITGYYYHFAIEREGETVLALDPYAKSMAAWNSDNDEYDIGKAAIVDPSAIGPELEY
ADIEGFEKREDAIIYEIHVRDFTSDPSIDEELEAEFGTFASFVEKLDYIEDLGVTHVQLL
PVMSYYFANELNKDERLIGWSALENNYNWGYDPQSYFSLTGMYSEDPNDPAKRIEEFKNL
INEIHDRDMGVILDVVYNHTAQVHLFEDLEPNYYHFMDSDGSSRESFGGGRLGTTHKMAR
RILVDSITYWLDEFKVDGFRFDMMGDHDAESIQIAYDQAKALNPNIIMIGEGWRTFAGDE
NYPNVQPADQDWMEHTDSVASFSDEFRNELKSGFGSEGEPRFITGGARNIESIFNNITAN
PGNFTADDPGDVVPYIAAHDNLTLHDVIAQSIKKDPKDHEKEIHQRIRLGNLMVLTSQGT
PFIHAGQEYGRTKQFRAEEFKTEVAEPPYKSTFLTDENGEPFEYPYFIHDSYDSTDAINM
FDWEKATNSADYPIHTTTRAYTKGLINLRRSTDAFRLATMKDVNEKVTLIDAPEIADEDL
IIGYRAENSTSDEAYYVFVNADNQSRSLTLTEDLTGGEVVVDARQAGVETIEEPQGVSIT
DNGLDIDALTSVVIRVADKTEQSNGENPSSPGSEKETEERSENLEEGNHQKTSTPKGGDQ
NSLDNDNESELPDTATNMYLQLVMGLIMIAIAFGLLVVRRKK

Enzyme Prediction     

EC	3.2.1.41	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1357	1692	1.2e-121	0.9964788732394366
GH13	421	733	4.1e-112	0.9931972789115646
CBM41	154	258	2.2e-23	0.9803921568627451
CBM41	886	991	4.6e-21	0.9901960784313726
CBM41	45	146	8.2e-21	0.9607843137254902

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02102	pullulan_Gpos	0.0	883	1962	1	1110	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	1.45e-173	1195	1876	61	696	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	5.27e-153	1330	1769	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	2.09e-135	1192	1849	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	3.47e-75	1178	1873	100	893	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
QGH37050.1	0.0	16	1962	1	1941
BAM47868.1	0.0	6	1962	9	1964
ADH98514.1	0.0	1	1876	5	1872
AOM81713.1	0.0	11	1876	13	1867
QFQ60721.1	0.0	15	1879	13	1872

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2YA1_A	0.0	885	1877	6	1012	Productcomplex of a multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA0_A	6.36e-291	1188	1877	2	705	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA2_A	2.83e-290	1188	1877	3	706	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA in complex with an inhibitor. [Streptococcus pneumoniae TIGR4]
3FAW_A	1.68e-286	1070	1876	4	813	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	1.46e-73	1192	1847	31	638	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	862	1877	102	1126	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	0.0	847	1877	93	1141	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	0.0	838	1877	91	1148	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
O33840	2.24e-73	986	1874	10	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-67	1192	1794	97	638	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
0.002284	0.888494	0.107979	0.000565	0.000367	0.000283

TMHMM  Annotations     

start	end
7	26
1939	1958