CAZyme Information: MGYG000003389_03624

Basic Information

• Lineage: Bacteria; Bdellovibrionota; Bdellovibrionia_A; CAIPTA01; CAIPTA01
• CAZyme ID: MGYG000003389_03624
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
775		86086.62	5.2906

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003389	3878302	MAG	United States	North America

• Gene Location: Start: 72; End: 2399 Strand: +

Full Sequence      

MLVVSDAGGNEIDRTYFQTGALLDAIYRYDGCLGVCIEGGQPVLRVWAPTARSVRVLWVT
PGRAPQVQDAAVMTAGAGGSFQLAGTTAWFGRNYLFEVEVFSPLTGKVEKFRVTDPYSVG
LALDSASSVLLDLGDSRWKPVGWDSTPRPALASRNDSVLYEVHVRDFSARDASVPPGLRG
TYRAFTLDGTDGDRELRALAGAGITHVHLMPTFDFASVEEDPSLRREPSVAPNLPPDSPL
PQEAVNRFRSFDSFNWGYDPFHYLTPEGSYAQSPEGGSRTLEFREMIQALHRRGLRVVLD
MVFNHTYAAGLADESVLDKVVPGYYHRLDGEGQVRKSSCCSDTASERWMMEKLMRDGLEL
WRSQYHVDGFRFDLMNFHSIATMGRLRDFERAKDPSLLFYGEAWSFGSLLETDPAGAFTQ
PRSYGEKIGVFNDRLRDAIRGGTTDSKGKSDPGWVTGLFYDFNQEPANRDTPVDLGQQRD
KLLWLGDVVRVGLAGNLRDYEFTDHRGNRIRGGDLQFNGGPTGFAQDPEETVNYVSAHDG
YTLWDALAAKLPFHTKSRSPDTATLQERVDRQLLALGLVAVSQGMPFFDEGSELLRSKSG
DQNSYDSGDWFNAVDWTGSANNWGLGLPPLFSNPDDWPFWRPRLADPLLAPGPAEIAAVR
AGFLDLLRLRRSTPLLRLRSGEEIRRRVRFLEADLGPMEPPGLIVMEIRDDARNLDPQWS
RLIIAANALNDSQVFPHASLGHGSLTRLYGKGDSRLAPTPQLVLPPRSLTVWGEK

Enzyme Prediction     

No EC number prediction in MGYG000003389_03624.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	196	594	4.8e-125	0.9944598337950139

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02103	pullul_strch	0.0	2	746	94	859	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	0.0	6	746	188	931	alpha-amylase/limit dextrinase
cd11341	AmyAc_Pullulanase_LD-like	1.49e-174	155	622	1	392	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	2.19e-139	27	736	6	585	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	6.49e-104	26	771	60	688	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDK36759.1	2.08e-233	12	766	103	854
QLY24848.1	1.03e-225	12	742	129	855
AHZ86446.1	9.63e-225	2	741	97	832
QDK47558.1	1.01e-223	12	742	77	803
CAE79132.1	4.23e-223	2	741	107	842

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Y4S_A	1.52e-168	2	722	96	813	BarleyLimit Dextrinase In Complex With Beta-Cyclodextrin [Hordeum vulgare],2Y5E_A BARLEY LIMIT DEXTRINASE IN COMPLEX WITH ALPHA-CYCLODEXTRIN [Hordeum vulgare],4AIO_A Crystal structure of the starch debranching enzyme barley limit dextrinase [Hordeum vulgare],4CVW_A Structure of the barley limit dextrinase-limit dextrinase inhibitor complex [Hordeum vulgare],4CVW_B Structure of the barley limit dextrinase-limit dextrinase inhibitor complex [Hordeum vulgare]
4J3S_A	2.74e-168	2	722	117	834	Crystalstructure of barley limit dextrinase soaked with 300mM maltotetraose [Hordeum vulgare],4J3T_A Crystal structure of barley Limit dextrinase co-crystallized with 25mM maltotetraose [Hordeum vulgare],4J3U_A Crystal structure of barley limit dextrinase in complex with maltosyl-S-betacyclodextrin [Hordeum vulgare],4J3U_B Crystal structure of barley limit dextrinase in complex with maltosyl-S-betacyclodextrin [Hordeum vulgare],4J3V_A Crystal structure of barley limit dextrinase in complex with a branched thio-linked hexasaccharide [Hordeum vulgare]
4J3W_A	2.14e-167	2	722	117	834	Crystalstructure of barley limit dextrinase (E510A mutant) in complex with a branched maltohexasaccharide [Hordeum vulgare],4J3X_A Crystal structure of barley limit dextrinase (E510A mutant) in complex with a branched maltoheptasaccharide [Hordeum vulgare]
6J33_A	2.67e-138	3	762	234	1020	ChainA, pullulanase [Klebsiella pneumoniae],6J33_B Chain B, pullulanase [Klebsiella pneumoniae],6J34_A Chain A, Pullulanase [Klebsiella pneumoniae]
6J35_A	7.34e-138	3	762	234	1020	ChainA, Pullulanase [Klebsiella pneumoniae],6J35_B Chain B, Pullulanase [Klebsiella pneumoniae],6J4H_A Chain A, Pullulanase [Klebsiella pneumoniae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8GTR4	3.57e-168	2	740	177	918	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
P07206	5.83e-139	12	733	280	1027	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
P07811	1.74e-132	34	710	315	1011	Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1
C0SPA0	1.57e-72	14	616	82	593	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840	2.55e-72	27	727	219	794	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2

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
1.000066	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003389_03624.