CAZyme Information: MGYG000003601_00841

Basic Information

• Species: HGM12713 sp900770605
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; HGM12713; HGM12713 sp900770605
• CAZyme ID: MGYG000003601_00841
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
897	MGYG000003601_95|CGC1	98642.34	4.1612

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003601	1391946	MAG	Fiji	Oceania

• Gene Location: Start: 2552; End: 5245 Strand: -

Full Sequence      

MKKTLRALSIFMLLVMLMAVVLSACTDATSDVTADSTPPTNDQNTDDTDDGGDEGSADEY
NLPLEDGYNQLTLYWTYNGTYENCDIWIWWGDKAGQGYVFHECDYGAKVVVNVPVGVEEV
GFIVRKSCSDPGGSSWGNATKDFEQDRFAVIDGRETKIYLKSGVEDQFYSDDGGKTLTMI
KKFSLAGMMDSQKIQYRITPKTTITSLDQVKVYEGDREIPVKSVSTLGISASSGYITVDE
TFSLSGNYRVEIEGYGDKRIIPTGIFDSAYFAENYHYDGNDLGAFVTGENTVFKLWAPTA
SEVRLNLFEAGNGDEAYKSVEMTLGEKGVWSHTEPCGHGTYYTYSVTTAVGTQEAVDPYA
RAAGVNGERGMVVDLSLTDPEGFDEDASLDTLQSYSDAVIWEVHVRDFSNKIESSEYKGK
YLAFTETGLVNEYGVPVGIDYLKQLGITHVHLLPVYDYASVDEASTEPQFNWGYDPENYN
VPEGSYSTDPYNGEVRINEFKQMVMALHEAGIGVIMDVVYNHTYDANSSFNKIVPYYYYR
YTSSGANSSASGCGNDTASERYMFGKFMVDSTSYWMEEYHLDGFRFDLMGLHDLQTMQEI
ESAVHTLNPNAIIYGEGWTMGSTVDGSAQANQTQISKIVPTGDAIGGIAVFNDVMRDGLK
GSVFEATGKGYINGAPSSANLSKIIFSIRGGVGVGTGWSVTDAMVINYMSAHDNNTLWDK
LLLSCPNSSEDDRNAMNKLGAAILMISKGTPFWQAGEEMLRTKDGDENSYKSSDSINNID
WSVLSTESREYRTMLYYQGLIAMRKAFPIFRDVSATVEYEALGSGIAIVTFDDGNGGRAM
VVINPQNAALPCTIEGEWNLVADGQTASSDVIARESGSITVEEYSVRIYVNDALLNN

Enzyme Prediction     

No EC number prediction in MGYG000003601_00841.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	439	758	3.4e-110	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	397	804	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.
TIGR02104	pulA_typeI	0.0	270	871	1	605	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.
TIGR02103	pullul_strch	3.48e-127	275	890	119	895	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]
COG1523	PulA	3.93e-123	275	889	61	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877	PLN02877	2.78e-117	273	890	207	967	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTE69880.1	0.0	56	886	29	862
QTE73814.1	0.0	56	886	29	862
QUC66538.1	0.0	56	886	29	862
QUA52340.1	0.0	56	880	28	856
QTE67820.1	0.0	56	886	24	856

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	2.37e-155	255	878	14	639	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]
6JHI_A	3.67e-154	255	878	14	639	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	3.67e-154	255	878	14	639	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
2WAN_A	3.85e-147	202	888	243	918	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	2.22e-146	275	893	57	715	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	3.08e-145	74	888	27	839	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	5.32e-122	218	815	42	624	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	7.98e-75	263	785	190	794	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	4.49e-69	273	811	428	1020	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	4.99e-69	273	811	450	1042	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	0.000001	1.000056	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
7	24