CAZyme Information: MGYG000003532_00586

Basic Information

• Species: W0P28-013 sp004557405
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae; W0P28-013; W0P28-013 sp004557405
• CAZyme ID: MGYG000003532_00586
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
662	MGYG000003532_14|CGC2	74410.49	5.9891

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003532	1885895	MAG	Fiji	Oceania

• Gene Location: Start: 135587; End: 137575 Strand: -

Full Sequence      

MKRILNSALCLLATLVCSCNIQPTYTSVDEYPVYEGCDLGATFTPSRTSFRTWSPGAEQV
RLHIYADASSDEPLATYNMRRAKQGTWTYNVQQNLEGKFYTFQIYQNGQWYDETPGIWAK
AVGVNGDRAAIIDFQKTNPENWENDQRPAMAHFTDAVIYEVHMRDFTIDSTSGSHFPGKF
LGLSESGTTSPQGQKTGLDHLKELGITHVQILPSYDYASIDETKLDSNFYNWGYDPENYN
VPEGGYSTNPYDPATRIREMKQMIQTLHANGIRVIMDVVYNHTFVGYESHLNQLVPNYFY
RFYNDSTWGNSSGCGNETASERPMMRQFIVESVKYWATEYHIDGFRFDLMGIHDIETVNA
IRTALDQIDPTISMHGEGWAAGGSPLAEDVRALKQSAPRFYPTAVFSDDIRDALRGNWMD
GNKGGFLVGNGYEESIKFGIVGATAHPQVDLAKIIHSQTAYATTPAQAINYVSCHDDPCV
VDKLKATIPNIKEQELLAMDKLAQTIVFTSQGVPFMYAGEEVFRDKKGVHNSYISPDSIN
AIDWSRKAKYRDLFDYYKNLIALRKAHPAFHITSAEMVAKHLVFDAKTPKNVVAYTLNDN
ANGDTWRTILVIFNGNRKPVSYTLPSGKWTAVCRHGKIDEQGLEQVSGQLKIGASEAVIL
FQ

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	198	521	1.4e-114	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	154	564	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	29	640	2	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.
COG1523	PulA	1.81e-136	29	629	59	662	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	1.91e-108	35	622	124	849	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	7.65e-107	10	625	180	923	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBK90475.1	1.07e-284	14	662	13	664
QUR46980.1	1.07e-284	14	662	13	664
QUT18526.1	2.16e-284	14	662	13	664
QIX66559.1	2.16e-284	14	662	13	664
QKH97022.1	2.16e-284	14	662	13	664

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	1.55e-202	29	629	31	623	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	2.50e-201	29	629	31	623	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	2.50e-201	29	629	31	623	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	1.11e-169	34	662	313	921	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
3WDH_A	1.27e-156	29	629	101	678	Crystalstructure of Pullulanase from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDI_A Crystal structure of Pullulanase complexed with maltotriose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDJ_A Crystal structure of Pullulanase complexed with maltotetraose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	2.12e-171	28	662	216	842	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.97e-141	29	626	98	674	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	7.82e-71	28	628	198	919	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	2.80e-68	29	660	427	1123	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	3.03e-68	29	660	449	1145	Pullulanase A OS=Streptococcus pneumoniae OX=1313 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
0.000000	0.000017	1.000052	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003532_00586.