CAZyme Information: MGYG000003511_01014

Basic Information

• Species: SFVR01 sp900769035
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae; SFVR01; SFVR01 sp900769035
• CAZyme ID: MGYG000003511_01014
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663	MGYG000003511_197|CGC1	74787.28	4.6751

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003511	2091537	MAG	Fiji	Oceania

• Gene Location: Start: 13594; End: 15585 Strand: -

Full Sequence      

MKTKIFLLVTLVTLSMISCSEKPQKYASCDEYPIYEGDDLGVTYSTESSVFKAWSPEAEE
VRLNLYEDGVTGAPYATYDMKYDKDGVWKYTVKEDLIGKFFTFQIKQNDKWLGTTPGIWA
KAVGCNGDRAAIIDWSTTNPEGWESDKRPEMKSFTDAIIYEVHMRDFTISPTSGSNYPGK
FLGLCEAGTTSPEGEKTGLDHLVDLGITHVQILPMYDYGSIDETKLEQNNYNWGYDPKNY
NVPEGGYSTDPYNPSVRIIELKTMIQKLHEAGIRVIMDVVYNHTFVGADSHLNLMVPGYF
YRMNADSTWSNGSGCGNETASERPMMRRFMVESVKYWINEYHIDGFRFDLMGIHDIETMK
AIRAAIDEIDPTISIHGEGWTGGECALPESERAIKQNAAQFAPIAVFSDNIRDGLRGNWV
DGDKGGFLVGNDLDETIKFGIVGATKHPQVDYSNIIHANAPYATTPAQVINYVSCHDDPC
VVDKLKATRPEATMDEIIKMDLLAQTVIFTSQGVPFIFAGEEVLRDKKMVHNSYNSPDSI
NEINWSNKATYNNVYQFYRSLIQLRKSHPAFRMNTAESVTENLQFIETEPGIIAYTINAK
ECGDTWSKIMVIFNRNKETKTLNLNGETWNICLKDETFMTDQAQKASNFITINPTTAIIL
FQE

Enzyme Prediction     

No EC number prediction in MGYG000003511_01014.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	199	522	2.9e-116	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	30	641	2	604	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	155	565	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.
COG1523	PulA	1.61e-131	50	663	70	692	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	3.50e-124	36	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	1.57e-111	30	647	206	939	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBK90475.1	2.76e-285	12	663	10	665
QUT95748.1	5.55e-285	12	663	10	665
QCY55926.1	5.55e-285	12	663	10	665
QUT18526.1	5.55e-285	12	663	10	665
QIX66559.1	5.55e-285	12	663	10	665

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	8.71e-197	27	624	28	617	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	1.40e-195	27	624	28	617	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	1.40e-195	27	624	28	617	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	1.29e-161	35	631	313	890	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
3WDH_A	7.24e-153	30	662	101	709	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	2.29e-161	30	663	217	843	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	3.30e-129	27	661	94	709	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	5.63e-75	30	614	199	905	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	1.87e-73	30	624	427	1076	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	2.10e-73	30	624	449	1098	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
0.000204	0.169300	0.830276	0.000067	0.000084	0.000074

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003511_01014.