CAZyme Information: MGYG000003493_01414

Basic Information

• Species: Prevotella sp002299275
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002299275
• CAZyme ID: MGYG000003493_01414
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
637		71567.32	6.3097

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003493	3028354	MAG	Fiji	Oceania

• Gene Location: Start: 11567; End: 13480 Strand: -

Full Sequence      

MTVVSLMFAGGTMSAQQTFNELTYTKDASSFRLNAPSKAKSVKVHIYKEGVGGEVVKTVK
MKRTGNDLWTADIKGDLKGMFYTFQVETSKQKMNETPGVFAKAVGVNGRRAAIIDMADTN
PDGWCCDKRPLTKQPTDLVIYEMHHRDFSVSPNSGLEHKGKFLALTEPKAVYHLKNLGVN
AIHILPSYDYASVDESKPDVPQYNWGYDPLNYNVPEGSYSTNAECPIARIKEFKQMVQAM
HKAGIRVILDVVYNHTFDVDNSNFNLTYPGYYYRKTADGKISDGSGCGNETASEKPLMRQ
FMIESVLYWAKEYHIDGFRFDLMGIHDIETMNLIRKALDEVDPSIYIYGEGWSAGTCAYP
VEKLAMKANTRQLDRIGAFCDDMRDAIRGPFSDDHKAAFLGAVPGNEESIRFGIAGAIAH
PQIDMSKVNYSKEPWTNSPAQMISYVSCHDDMCLVDRLKASIPGITEDELIRLDLLAQTM
VFTSQGVPFILAGEEMLRDKKGVHNSFKSPDNINQLPWENLEKYPQVFDYYRGLTEMRRN
HPAFRMSDAEMVRTHLEFLKSQENVVAFRLKDNANGDSWKDIIVILNSNKTTQRVNIPDG
TWTSVCEGGQINLAGISEYKGTVVEVAPQEALIIYTK

Enzyme Prediction     

No EC number prediction in MGYG000003493_01414.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	173	495	9.4e-113	0.9896193771626297

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	136	538	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.
TIGR02104	pulA_typeI	0.0	21	611	13	601	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	5.63e-132	2	603	42	661	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	8.41e-120	23	592	131	846	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	8.64e-111	24	599	219	924	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVJ82241.1	0.0	17	635	10	622
ALO49594.1	4.74e-317	11	635	17	639
QUB46864.1	8.70e-317	14	636	19	639
QNT66905.1	1.12e-311	13	637	20	656
ADE82909.1	8.83e-311	35	635	3	597

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	1.43e-174	24	614	45	634	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	2.29e-173	24	614	45	634	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	2.29e-173	24	614	45	634	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	3.86e-162	24	623	322	909	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	3.44e-143	22	637	66	714	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	9.71e-145	24	635	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	9.08e-128	24	599	110	674	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	4.81e-68	24	570	212	852	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2UNG0	1.17e-61	39	597	471	1091	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	1.53e-61	39	597	456	1076	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.638847	0.359606	0.000834	0.000393	0.000157	0.000166

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003493_01414.