CAZyme Information: MGYG000003419_00988

Basic Information

• Species: RF16 sp900766775
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae; RF16; RF16 sp900766775
• CAZyme ID: MGYG000003419_00988
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
690		76412.3	5.5111

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003419	2335712	MAG	Fiji	Oceania

• Gene Location: Start: 8473; End: 10545 Strand: +

Full Sequence      

MKKQILALSLVCTLAGCSVKAPVYESVDDYPVREGALDEMVYSPQKTIFSLWSPAADSVW
LRLYAEGLGGEAQEAVAMRRGKDGTWTCSVRGDLQGKFYTFQVDDMEETPGIFAKAVGVN
GRRGAVIDLRSTDPEGWAEDVRPAFAGAKDAIVYEMHYRDYSIHPSSGVAHKGKFLALTE
KGTQVSPMVRLSTNRDNTSDCTSITQESSKVRPGDRTSLNSATGIEHLKELGVTHVQILP
SYDYGSIDETRLEDNKYNWGYDPVNYNAPEGGYSTNPYDPACRIREMKEMIQALHKAGIR
VVMDVVYNHTFDVAHSNFHNTCPGYFYRYNADGSLGNASGCGNETASERGMMRKFIVESC
RYWLTEYHIDGFRFDLMGIHDIETMRAVRAMMDGIDPTLLLYGEGWAAGAPLLPQEELAM
KANILRIEGVGAFCDDMRDALRGPFSDDHKGAFLAGEKGHEESIKFGIAGCIEHPDVDMS
RVNYSKAAWAAEPTQCISYVSCHDDMMLTDRLKASISLKKGELERLDKLAQTAVLTSQGI
PFLWNGEEILRNKKGVHNSYCSPDSINAIDWSLKAQHEDVFRYYQGLIALRKAHPAFRMG
NADLVRKHLHFLDAPEGVVAYALDGEAVGDDWKTIVVVLNANRKAVEVALPAGAYRLACG
DGECPYSGMRVDEKTTTVSAQSAQILYTKE

Enzyme Prediction     

EC	3.2.1.41	3.2.1.1	3.2.1.-	3.2.1.68

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	225	548	3.8e-112	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	28	664	2	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.
cd11341	AmyAc_Pullulanase_LD-like	0.0	150	591	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.
COG1523	PulA	5.22e-140	48	658	70	663	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	4.23e-112	35	686	113	894	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	1.10e-104	35	652	203	924	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO71194.1	6.02e-289	13	687	15	664
QUT90365.1	8.03e-287	13	687	15	664
ADV44974.1	1.61e-286	13	686	15	663
QRQ50227.1	3.25e-286	13	687	15	664
QUT43839.1	4.61e-286	13	687	15	664

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	2.54e-181	28	652	31	619	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	4.07e-180	28	652	31	619	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	4.07e-180	28	652	31	619	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	3.99e-147	41	657	321	890	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
3WDH_A	2.11e-140	25	657	98	680	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	4.40e-153	25	687	214	841	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.60e-138	28	687	97	709	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	4.11e-65	35	613	196	839	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	4.83e-63	50	650	450	1076	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	6.79e-63	50	650	465	1091	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 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	0.000000	1.000040	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003419_00988.