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CAZyme Information: MGYG000000037_00993

You are here: Home > Sequence: MGYG000000037_00993

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Turicibacter sp001543345
Lineage Bacteria; Firmicutes; Bacilli; Haloplasmatales_A; Turicibacteraceae; Turicibacter; Turicibacter sp001543345
CAZyme ID MGYG000000037_00993
CAZy Family CBM68
CAZyme Description Pullulanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
711 MGYG000000037_10|CGC1 81502.39 4.7579
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000037 2730783 Isolate United Kingdom Europe
Gene Location Start: 59284;  End: 61419  Strand: +

Full Sequence      Download help

MRKLQTFEAY  LDTFETITAY  LNKSYYQGES  QSFRLKDETS  TTTLLNILET  VDEGEYMKYI60
LETPILELGK  NYKVIDDHNL  AVPLQYGYVV  RTKEFDEAFY  YDGHDLGVTY  TKEASTFKVW120
SPIATQVKVE  VQTKDGIETY  DLTKGDEGVW  SITISKDLEL  ASYIYLVKVN  GTWNQATDPY180
AIASTPNHQR  TVIVDPEKIK  IDSKRELAPE  VKSYTDAIIY  EMHVRDFSVH  KNSGIKHVGK240
FLGVVEEGTR  TSRGTLTGLD  YLVDLGVTHI  QLLPTYDFGS  VDELNQFETY  NWGYDPVQYN300
VPEGSYSTDV  HNPYSRIIEM  KQMIAKLHEK  GFRVIMDVVY  NHMFDRQTSS  FENIVPNYYF360
KLGENGEISN  GSFCGNDVDS  LRPMCRQFII  DSCKMWVKEY  GFDGFRFDLM  GILDTETMNQ420
IADECQAIDA  SVMVYGEGWN  MPSIMPEEAK  AMMYNNKKMP  KIAHFNDRFG  RGIKGSPFET480
EMSDIGYGLG  YTGDINRAMN  VVAGSCTDIG  MEALFVEPTM  TLNYVECHDN  MTLFDKIMLS540
NRCESLETRL  KRQKMITALI  LVSQGIAFLH  AGQEFNRTKD  GDHNSYMSPD  SVNQLDWDRK600
DEYIETVEFV  KGFINLRKEL  KALRLNTAEE  IKQHVTVNKL  DDRVIEYTIS  NVKAYGPYEE660
IKIFINPTHE  PFNINLEKEY  LIVADQSGLL  KQHLKSDQIT  INAIELKVLA  I711

Enzyme Prediction      help

EC 3.2.1.41 2.4.1.25 3.2.1.33 3.2.1.1

CAZyme Signature Domains help

Created with Snap3571106142177213248284319355391426462497533568604639675259574GH13597CBM68
Family Start End Evalue family coverage
GH13 259 574 9.8e-110 0.9965397923875432
CBM68 5 97 1.3e-20 0.9787234042553191

CDD Domains      download full data without filtering help

Created with Snap357110614217721324828431935539142646249753356860463967594685pulA_typeI215617AmyAc_Pullulanase_LD-like40686PulA96636PLN0287796601pullul_strch
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02104 pulA_typeI 0.0 94 685 1 597
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 0.0 215 617 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 3.81e-138 40 686 1 669
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877 PLN02877 3.55e-101 96 636 206 870
alpha-amylase/limit dextrinase
TIGR02103 pullul_strch 2.36e-96 96 601 116 732
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]

CAZyme Hits      help

Created with Snap35711061421772132482843193553914264624975335686046396751710AMC09634.1|CBM48|CBM68|GH13_141710QJS20077.1|CBM48|CBM68|GH13_145689QPA30409.1|CBM48|CBM68|GH13_147679ADK07283.1|CBM48|CBM68|GH13_147679ANC21752.1|CBM48|CBM68|GH13_14
Hit ID E-Value Query Start Query End Hit Start Hit End
AMC09634.1 0.0 1 710 1 710
QJS20077.1 0.0 1 710 1 710
QPA30409.1 5.01e-216 5 689 6 694
ADK07283.1 1.17e-215 7 679 8 675
ANC21752.1 1.88e-214 7 679 8 675

PDB Hits      download full data without filtering help

Created with Snap357110614217721324828431935539142646249753356860463967536633WDH_A56882E8Y_A876766JEQ_A876766JHI_A876766JHH_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WDH_A 3.01e-200 3 663 7 660
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]
2E8Y_A 9.07e-167 5 688 6 686
Crystalstructure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Y_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Z_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E8Z_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E9B_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis],2E9B_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis]
6JEQ_A 1.35e-166 87 676 22 617
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]
6JHI_A 2.13e-165 87 676 22 617
Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A 2.13e-165 87 676 22 617
Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]

Swiss-Prot Hits      download full data without filtering help

Created with Snap35711061421772132482843193553914264624975335686046396755688sp|C0SPA0|PULA_BACSU51678sp|O33840|PULA_THEMA96676sp|A0A0H2UNG0|PULA_STRPN96676sp|A0A0H2ZL64|PULA_STRP296676sp|Q9F930|PULA_STREE
Hit ID E-Value Query Start Query End Hit Start Hit End Description
C0SPA0 1.40e-165 5 688 6 686
Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840 2.25e-129 51 678 175 799
Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
A0A0H2UNG0 2.03e-67 96 676 442 1091
Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64 2.58e-67 96 676 427 1076
Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930 2.79e-67 96 676 449 1098
Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000058 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000037_00993.