CAZyme Information: MGYG000004561_00403

Basic Information

• Species: Prevotella sp002480935
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002480935
• CAZyme ID: MGYG000004561_00403
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
650	MGYG000004561_4|CGC2	73073.98	6.5377

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004561	3001921	MAG	France	Europe

• Gene Location: Start: 89164; End: 91116 Strand: -

Full Sequence      

MKKHLLASIFTMLLPLCASAQDINSMSLDYTNPVEYSPSGTTFLLFAPENKQHAPILRLY
HEGVGGKPFKTIRMKPVENYGWKAEVKGNLKDQFYTFDVWGTKRDHKETPGIYARAVGVN
GVRGAVIDMNETNPVGWKDDHRVPTKSAADLVIYELHHRDFSIDASSGLVHKGKYLALTE
KKAINYLKSLGVNAIHILPSFDFASVDEQKPFEPQYNWGYDPLNYNVPEGSYSYDACQPE
RRIMEFKQMVQALHKAGIRVILDVVYNHTFNIEGSSFERTFPKGFYRYTADGKPSNGSGC
GNETASERTLMHQFMLQSVKYWAQEYHIDGFRFDLMGVHDIATMNDIRAELNAIDPNIFV
YGEGWSAGTCAYPTEKLAMKANMQQLKGIAAFCDDMRDALRGPFSDDKKGAFLAGIPGEE
ESLKAGIAGMIDHPQVDYSKVNYSKKAWASEPTQMISYVSCHDDLCLTDRLRAEMPGITT
DELIRLDCLAQTAVFLSQGVPFMLCGEEMLRTKQDVHNSFNSPDSINHLDWNNLKRYPQV
FSYYQQLIKLRHDHPAFRLGSAQLVRKHLDFLAVESPCLVAFRLKEHAGNDQWNNIIVIL
NGNKEAKTVSVPQGNYTVVACDGKIDQAGLDSVQSDKVIVDGQSALILHD

Enzyme Prediction     

No EC number prediction in MGYG000004561_00403.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	184	508	1.4e-108	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	150	551	2	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	0.0	35	632	15	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.
COG1523	PulA	2.09e-132	74	650	102	691	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	2.34e-114	34	615	130	855	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	1.02e-99	30	585	211	860	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUB40566.1	0.0	2	650	4	637
QUB83640.1	0.0	3	650	4	637
QUB92581.1	0.0	1	650	3	637
AXV49297.1	0.0	1	650	3	637
QUB88366.1	0.0	1	650	3	637

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	2.55e-153	36	648	322	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	1.47e-151	36	612	45	618	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	2.33e-150	36	612	45	618	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	2.33e-150	36	612	45	618	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
2E8Y_A	1.95e-123	36	649	110	709	Crystalstructure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Y_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Z_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E8Z_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E9B_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis],2E9B_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	4.68e-135	36	649	229	841	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	5.90e-122	36	649	110	709	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	5.13e-63	30	571	204	864	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2UNG0	6.66e-58	146	574	583	1051	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	8.77e-58	146	574	568	1036	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 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
0.000832	0.666813	0.331498	0.000346	0.000264	0.000217

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004561_00403.