CAZyme Information: MGYG000002141_01410

Basic Information

• Species: CAG-95 sp900554925
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-95; CAG-95 sp900554925
• CAZyme ID: MGYG000002141_01410
• CAZy Family: CBM41
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
887	MGYG000002141_74|CGC1	100757.21	4.4037

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002141	2542393	MAG	United States	North America

• Gene Location: Start: 4326; End: 6989 Strand: -

Full Sequence      

MKKRVNKIIFFVCAIFLCWIGMPCQSFGQEQSLTVEVHYTRYNEDYEGWNLWLWVDENEG
RSFEFETDGSEVKTEVELSQVSGDSRIGILLRKGDWEEKDVDGDRYLDLTKAKEGRLTIW
LMQGEETVYYSQEKTGVRILDACLDSETEITFRAYCAGTESLSVVDQQGKEYALAHQELS
KDGNIVSGKLTLKEAAALPGTFYLVIGDVKESIRFGGIYDTDAFKDNFVYEGEDLGVICQ
KERSSFCLWSPMAEEVTLKLYEEGTGGSPVKSIPLTRGEKGVWRLTLEGDYRNQYYTYVV
NVQGEEWEVSDPYARSTGLNGERGMLLAHDEGVPEGFLEDTFLTNTAREDVILYEMSVRD
FTSDEVSGVQEKGKFLGLTEKGTVNPSGDSTGLSYLAELGITHVHLLPVQDFGGVDEENP
EEAYNWGYGPVSFFVPEGSYSTDPYHGEVRVEECKRMVQSLHSEQIGVVMDVVYNHTYQN
TDSNLNRIVPGYYYRMKEDGSFSDGSRCGNELATEREMVRKLIMDSLKYWMEEYHIDGFR
FDLMGLIDVETMKEIEEMVYSINPHAVLYGEGWDAGETVYEGVRMESANAWMTPQIGTFN
NVFRRAVQKYICGMTEEESTVLGMQFGFAGAVSYPHIYDRMGSWTDNPLQCINYASCHDG
YTLWDLITLSCPEEGEEMWKQRDRFGAACVLLCQGTPFLHSGEEILRTKTSETNPDVKYG
NSYNAGDYVNKISWESRTENKDVLEYYKGLIAFRKAHEGLRYQTEKELNRKLMSIEELPE
NVIGYYMSEPVNFFVENQICILLNPTSETVEYVPESGTWKIYVDGERAGTECLKEISRGS
SLDVEGVSALAAVRIKVRWERIALVTAGLILVVVVLVIVRKGRHKKV

Enzyme Prediction     

No EC number prediction in MGYG000002141_01410.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	393	704	2.3e-103	0.9965397923875432
CBM41	34	132	1.8e-19	0.9705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	223	831	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.
cd11341	AmyAc_Pullulanase_LD-like	0.0	349	754	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	3.98e-131	166	859	12	697	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	1.25e-102	34	857	113	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 (.
PLN02877	PLN02877	1.39e-102	212	740	198	803	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJS18678.1	4.14e-210	29	873	149	1004
QEH70112.1	3.10e-209	31	856	139	982
ADZ84640.1	1.73e-208	31	856	139	982
AMC08554.1	1.90e-201	29	844	149	970
ADL35847.1	2.57e-182	1	854	1	868

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	1.59e-149	216	826	21	630	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]
6JHH_A	2.45e-148	216	826	21	630	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	2.45e-148	216	826	21	630	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	3.35e-145	32	850	4	917	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
3WDH_A	1.93e-139	213	827	89	686	Crystalstructure of Pullulanase from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDI_A Crystal structure of Pullulanase complexed with maltotriose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDJ_A Crystal structure of Pullulanase complexed with maltotetraose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	3.12e-150	34	843	22	833	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	4.67e-135	210	824	82	683	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	1.29e-74	19	790	213	1056	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	1.45e-74	19	790	228	1071	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	2.02e-74	19	790	235	1078	Pullulanase A OS=Streptococcus pneumoniae OX=1313 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
0.003289	0.976907	0.018819	0.000339	0.000291	0.000311

TMHMM  Annotations     

start	end
7	29
862	879