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CAZyme Information: MGYG000000142_01867

You are here: Home > Sequence: MGYG000000142_01867

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 Blautia_A massiliensis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A massiliensis
CAZyme ID MGYG000000142_01867
CAZy Family CBM34
CAZyme Description Neopullulanase 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
705 MGYG000000142_6|CGC1 81906.61 5.0681
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000142 3538467 Isolate United Kingdom Europe
Gene Location Start: 24768;  End: 26885  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1 3.2.1.41

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 192 572 2e-95 0.9968354430379747
CBM34 39 130 2.1e-21 0.8666666666666667

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11338 AmyAc_CMD 6.01e-170 139 608 1 389
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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.
PRK10785 PRK10785 2.66e-137 37 638 11 561
maltodextrin glucosidase; Provisional
pfam00128 Alpha-amylase 6.73e-58 192 571 1 334
Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
COG0366 AmyA 6.40e-54 140 648 1 496
Glycosidase [Carbohydrate transport and metabolism].
PRK14510 PRK14510 1.75e-46 134 607 109 576
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL21300.1 0.0 1 705 1 705
QCU02839.1 0.0 1 705 1 705
AWY98996.1 0.0 7 696 8 697
QMW79818.1 0.0 3 696 3 697
QIB57400.1 0.0 3 696 3 697

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5Z0T_A 2.17e-110 25 648 10 598
Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris],5Z0T_B Thermoactinomyces vulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris]
1JI1_A 1.67e-109 25 648 10 598
CrystalStructure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1JI1_B Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1UH3_A Thermoactinomyces vulgaris R-47 alpha-amylase/acarbose complex [Thermoactinomyces vulgaris]
1IZJ_A 2.34e-109 25 648 10 598
ChainA, amylase [Thermoactinomyces vulgaris]
1IZK_A 4.61e-109 25 648 10 598
ChainA, amylase [Thermoactinomyces vulgaris]
2D0F_A 9.10e-109 25 648 10 598
ChainA, alpha-amylase I [Thermoactinomyces vulgaris]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q60053 1.98e-108 25 648 39 627
Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI PE=1 SV=1
Q08341 1.60e-91 46 697 23 583
Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P38939 9.15e-86 34 673 261 909
Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
Q08751 1.37e-84 25 650 4 549
Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
P38940 2.06e-84 43 692 19 579
Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT 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
1.000056 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000142_01867.