CAZyme Information: MGYG000001319_01522

Basic Information

• Species: Butyrivibrio_A crossotus
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Butyrivibrio_A; Butyrivibrio_A crossotus
• CAZyme ID: MGYG000001319_01522
• CAZy Family: CBM41
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
874	MGYG000001319_13|CGC2	95944.03	4.4727

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001319	2482799	Isolate	not provided	not provided

• Gene Location: Start: 184247; End: 186871 Strand: -

Full Sequence      

MKKLRKLFAILLVALMVFSMAACGKKKDQGSVETTTPVETESTTDNSNKATELTLNVHYL
REDGVYDGWNVWLWPDGGEDGKAYTFGTDKDEHGVKTTAVFPAGTTTIGFIVRLNEWESK
DIDSDQFITLNGVIAGTVEVYITSGVEGYKLELGEDCVTGLSVLSAELDGDFQTLKITLT
EEYKDNEIKVTDAEGKELAIDSVEKDSGDAKKIIVKLKEKADQFGKYKVMLGNVGYDVTV
PDYYSTSEFEDAYTYDGDDLGASWSKDSTTFKVWAPTAKAVKVNTYKSGVKGTDDLIKSY
DMTLDKNGVWTVKAEGDLNGVFYLYEADFGSSKTEACDPYAKAVGVNGDRAMVIDLSSTD
PDGWDKDTNPNKKLNATDASVYELHIRDLSADSSSGIKNIGKYLGLTETGTTNGSGQATG
LDHIKELGVTHVQIGPMYDYATVDETKLDTKQYNWGYDPKNYNVPEGSYSSDPYNGAARV
SEVKQMVKALHDNGLSVVMDVVYNHTYNTSYCFNELVPDYFYRPGANGSGCGNDVASERA
MVSKFIVDSVVYWAKEYHIDGFRFDLVGLIDMDTIKAIRTELDKIDPSIILYGEGWSMTT
KITKSGVTLATQMYVNKLDRFAMFSDTIRDAIKGSVFNADEKGYVNGNISNTDVIKKAIQ
GKTGWSEKGSQNIVYASCHDNRTLWDEINLSNPNDSMEDKVKQNLLSAAIVYTSQGTPFI
LAGEEILRSKPNGDGTFSSDSYNAGDEVNSIKWSTLSDATYQKVFNYYKGMIAFRKAHAS
LRIMDTASSYYKFTEDTDKGVIAYELTGVKEEVSDSIFVVYNPLSEATTVTLPEGDWTIC
VQGDKAGTDSLGTANGKITVDGISCTILVKGATK

Enzyme Prediction     

EC	3.2.1.41	3.2.1.-	3.2.1.68	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	421	725	8.7e-110	0.9965397923875432
CBM41	54	147	4.3e-18	0.9117647058823529

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	248	850	1	605	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	377	775	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	1.84e-129	236	868	44	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	2.23e-115	250	870	116	896	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	1.91e-108	250	754	206	798	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADL35847.1	2.41e-273	53	871	39	869
BBF44596.1	8.95e-244	243	874	14	652
CBL10489.1	8.05e-228	249	871	14	655
VCV21250.1	1.60e-226	249	870	10	650
CBL13024.1	1.00e-225	249	871	13	654

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	7.07e-165	232	844	10	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]
2WAN_A	2.05e-164	57	868	9	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	5.16e-164	245	872	49	715	ChainA, Pullulanase [Ruminococcus bromii]
6JHI_A	1.11e-163	232	844	10	630	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	1.11e-163	232	844	10	630	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	4.51e-179	52	870	20	842	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.26e-125	224	833	69	673	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	1.88e-71	250	758	199	795	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
P07206	2.87e-65	250	794	292	935	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
P07811	3.29e-64	261	761	315	927	Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000066	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
7	24