CAZyme Information: MGYG000001972_00283

Basic Information

• Species: Prevotella sp900315955
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900315955
• CAZyme ID: MGYG000001972_00283
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
675	MGYG000001972_8|CGC1	75523.31	6.8661

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001972	3441323	MAG	Denmark	Europe

• Gene Location: Start: 4184; End: 6211 Strand: -

Full Sequence      

MNFRNIILTALLLPVSLMAMSQNYNFDEVSYTPRHTTFKLIAPDDVKHVVLSLYTKGDEA
TDKKPLATKQMKHVGKNLWSVTVRGNLIGRFYTFNIGKGETPGVFAKAVGVNGRRGAVIN
MKRTDPEGWSSDHILSYASTPNSTSNSTPSSTPNSCLQTPNYTALTVYEMHFRDFSIARN
VNLDPKEFFVKRQSTKYPGKFLALTEPWAINYLKNLGVGAVHILPSFDYASVDETKLDKP
QYNWGYDPLNYNVPEGSYSTDPYDPATRIREFKEMVAALHKAGIRVILDVVYNHTFDLDK
SNFQRTWPNAYYRFTADGKPSNGSGCGNETASDHAVMRQFMLQSVKYWAQEYHIDGFRFD
LMGVHDIETMNEIRRELTAVNPNIFIYGEGWSAGQCAYPTEQLAVKANISRLPGIAAFCD
DLRDALRGPFSDDHQGAFLAGLAGSEESLKAGITGMTSHPQVDYTKVNYSKDPWATEPTQ
CINYVSCHDDLCLVDRLKASVPGITTDELIRLDELAQTVVFTSQGVPFMLSGEEMLRDKK
GVHNSFNSPDSINELNWNNPLRYPQVLSYYKNLIALRNHHPAFRLGKTQLVQKHLEFLTT
ADCLVAYRLKDHAGGDAWNDIIVIFNANKAARQVTVPQGTYTVVCKDGQIDEGGLETVSG
TQVTVHPQSALILHN

Enzyme Prediction     

No EC number prediction in MGYG000001972_00283.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	210	534	1.1e-111	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	28	652	13	603	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	167	577	5	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	7.94e-128	37	673	70	694	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	8.57e-101	29	632	130	847	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	5.70e-91	31	600	219	874	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALO49594.1	1.88e-304	26	674	25	639
QVJ82241.1	1.60e-303	11	675	1	623
QUB40566.1	1.18e-299	26	675	26	637
ATV52787.1	1.68e-299	16	675	17	637
QUB49547.1	3.50e-299	16	675	17	638

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	1.45e-149	24	637	36	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]
6JHH_A	2.28e-148	24	637	36	618	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	2.28e-148	24	637	36	618	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	3.10e-136	31	673	322	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	3.04e-127	29	672	66	710	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	2.57e-131	15	674	210	841	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	2.88e-119	31	656	110	693	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2UNG0	2.06e-63	167	633	590	1088	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	3.61e-63	167	633	575	1073	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	3.80e-63	167	633	597	1095	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
0.000382	0.998923	0.000212	0.000164	0.000155	0.000144

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001972_00283.