CAZyme Information: MGYG000001828_00988

Basic Information

• Species: UBA4951 sp900542595
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-826; UBA4951; UBA4951 sp900542595
• CAZyme ID: MGYG000001828_00988
• CAZy Family: CBM41
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
864		96157.83	4.3023

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001828	1066613	MAG	Denmark	Europe

• Gene Location: Start: 1275; End: 3869 Strand: +

Full Sequence      

MKSRLKLSFILLSFVLPFGLAACDTGGGGGKQSASLPGDEEGVAIHYHRADGMYDNWALW
LWEAPSGEGAQYAFNGEDDYGAYCVLPFSTWENVPEAQLGFIVKAVDSWTKDIDADRFLD
FTALKKEGNLYHAYLESGDENIYLSPDKEMLEIITTCSFLTNGNLNVQTTLPFNNVKVYK
DGKLIIDQAVNNLQTYNVLMDGENTADFKAVYEAEVTFSESGNTARKTASNYGLYRTENF
DNNYTYDGELGAIYTPAQTTFRVWSPVADKITLNVYNNGTPKNVNATLGSDEKESYEMRL
QDRGVYEYVLSGDQAGKYYTYTVYSREYPNGKEIVDPYAKSAGVNGVRGMIVDFSKTNPV
GWDDVKPLPYDRKELVVYELHVADLTSDDTWGGTKEYAKTFKGFYEEGTKYTEGNTTVST
GFDHIKEMGVNAVQILPFYDQQNDEVNTSFNWGYNPQNYNVLEGSYSTDPYDGYQRIKEF
KELVKAYNENDINIIMDVVYNHVSGAAGSNFDVLMPGYYFRYNSDGTLNNGTGVGNVCAT
EMPMMHKFVVESATFWAEEYKLGGFRFDLMGNIDMETMEAVVTSCEEVNPDIVIYGEPWT
GGTDVLDQTLRAVQANGNRWVGYGGFNDQIRDGLIRGGLSAPSEVGWVANDKTMVGKNDL
NRITYGARGIVYSNGLTYCNPDSTVNYVTCHDNYTIYDRFVYGNEITDEARVKKMVLLSE
AAALLTQGTSFMQGGEEFLRSKGGNSNSYDAGYDVNAFKYDLKVKHLDLVNMMKEIIKVK
TTNPLLHLDQDGTSEMMTATFNPEGNVVTYEVNNPSGSALKIAMANGLQGDTTVDFTGYN
LAFNSVNSTSVTTLEPYQVVVGLK

Enzyme Prediction     

No EC number prediction in MGYG000001828_00988.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	423	737	4.4e-92	0.9930795847750865
CBM41	43	146	5.4e-21	0.9607843137254902

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	240	784	2	530	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	1.25e-169	376	780	4	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	4.73e-97	244	840	61	648	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	6.91e-81	37	742	108	814	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	1.78e-74	241	752	206	789	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOS39053.1	3.11e-228	36	864	50	887
VEU82346.1	1.36e-174	43	833	31	842
VEU81131.1	1.46e-167	35	834	24	846
QLY39684.1	8.46e-167	43	833	73	893
CCV65706.1	9.06e-160	39	814	29	821

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	2.19e-115	43	814	7	858	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	3.06e-115	240	788	30	566	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]
6JHI_A	4.54e-114	240	788	30	566	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	4.54e-114	240	788	30	566	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
7LSA_A	2.68e-103	238	814	51	647	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.84e-124	40	788	20	753	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	2.77e-82	208	788	59	621	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	6.39e-60	43	742	231	935	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	6.73e-60	43	742	253	957	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2UNG0	8.91e-60	43	742	246	950	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000006	0.004772	0.995256	0.000002	0.000003	0.000002

TMHMM  Annotations     

start	end
7	29