CAZyme Information: MGYG000002159_02159

Basic Information

• Species: UMGS403 sp900540865
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS403; UMGS403 sp900540865
• CAZyme ID: MGYG000002159_02159
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
998		109454.68	4.3108

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002159	2536943	MAG	Germany	Europe

• Gene Location: Start: 837; End: 3833 Strand: -

Full Sequence      

MAIVLSLMLIVSVFCVPTVFAAGNYYEEFAAGLDEKAYTGDDLGATYTPEATTFKVWSPT
ASSAKVVLYTKGSDKEDGAAKISTTDMTYNEANGVWSVAIDGDLKNVYYTYLIMNDGKER
EVVDIYAQAVGVDGNRGMVVDLDSTDPEGWENDTYKLVPSQTDANIWEIQIKDFSYNENS
GISKEKRGKYLAFTEKGTTLNGEGKYATGVDYLKQLGVNYVHLNPFYDFGSIQETGSDTQ
FNWGYDPKNYNAPEGSFSSNPYDGNVRINEVKQMVKALHDEGIGVIMDVVYNHTFEGAGS
WFQQTVPNYYYRFSGQNTWSSGSGCGNDTASEHEMFRKYMVDSVTYWAKEYHIDGFRFDL
MGLHDVQTMNAIRASLDEIDPRLLMYGEGWSMATTTDSDAPSLATQINAAKMSDRIGFFN
DQIRDGLKGSVFEAKGQGYIQGVAGSASSVKYGIQGNVISGAWKAKAPTQTVTYASAHDN
NTLYDRLVMSMKGGAKEQFSQRYDDLVAMNKLSAAIVYSSQGIPFILAGEEFARTKFGDE
NSYQSSPEINMLDWSRTVSYKDLVSYYAGMIEIRNNYAPFRDATTDTAKTKMQFATAPSG
VLAYTIYDEAQPWKTVAVAFNNQATDKQVTLTSKGTLPEKWTIIANDQTAGILSLGEVTG
STVTVPAGGALILVDSESFNTADVPSTKGLLTVNHIDKSTGKTLSTTSLQGEIGTLYETE
KNAALAVDYDLDSDSGNTTGKFTEEPIVVNYYYTPYSLKAQDISGDGNVSLDDVLIIQKD
LAKVASMTEEQAKIADANCDGVVSIADVLIYQKNIAKMFVPGVGTVEVNYLDTDTGKPVP
KQSPLVTKARTGESYKAEALTINYYTLDETKLPDNAEGRYTDGKIVVNYYYKYQPATYTV
HVKLMDGQTWTPYLHAWDDGGDLLGGGWPGGEMTLGEDGWFTIDVTCGGSFNWIINDNGQ
GAQTIDMENFSSDIWVVLNVAKPNKGADDVTVYTSKPE

Enzyme Prediction     

No EC number prediction in MGYG000002159_02159.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	211	531	1e-114	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	34	652	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.
cd11341	AmyAc_Pullulanase_LD-like	0.0	162	574	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.
COG1523	PulA	1.88e-138	53	667	70	688	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	5.26e-110	37	667	122	888	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]
PLN02877	PLN02877	2.95e-103	33	555	205	798	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT05892.1	1.00e-275	2	998	6	1042
QCT05893.1	9.19e-273	26	775	32	783
QCT07748.1	1.90e-264	16	998	21	1029
APO32485.1	4.33e-235	26	700	23	693
QCT07019.1	5.01e-216	5	687	17	718

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	1.23e-251	20	756	40	795	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	1.96e-250	20	756	40	795	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	2.10e-250	20	756	40	795	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	2.17e-250	20	756	40	795	ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A	4.28e-156	29	610	26	594	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
O33840	2.52e-142	33	661	216	829	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	8.06e-127	31	618	94	659	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	3.21e-68	33	555	198	791	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	6.14e-60	33	598	425	1037	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	6.44e-60	33	598	440	1052	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA 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
0.000393	0.998964	0.000170	0.000180	0.000149	0.000138

TMHMM  Annotations     

start	end
2	24