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CAZyme Information: MGYG000000312_02027

You are here: Home > Sequence: MGYG000000312_02027

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 Eisenbergiella sp900539715
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900539715
CAZyme ID MGYG000000312_02027
CAZy Family GH13
CAZyme Description Neopullulanase 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
713 MGYG000000312_23|CGC1 83476.31 5.721
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000312 2782709 MAG Sweden Europe
Gene Location Start: 14392;  End: 16533  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 190 570 8.4e-92 0.9968354430379747

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11338 AmyAc_CMD 9.77e-156 137 605 1 388
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 7.91e-116 43 635 19 560
maltodextrin glucosidase; Provisional
COG0366 AmyA 2.64e-52 138 593 1 386
Glycosidase [Carbohydrate transport and metabolism].
pfam00128 Alpha-amylase 1.26e-47 190 569 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.
PRK14510 PRK14510 3.12e-40 128 605 105 576
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNM02520.1 0.0 9 695 12 698
AWY98996.1 0.0 10 695 13 700
QQQ94235.1 0.0 10 693 13 698
ANU76656.1 0.0 10 693 13 698
ASU29464.1 0.0 10 693 13 698

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5Z0T_A 1.81e-101 25 655 12 607
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 2.70e-100 25 655 12 607
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 3.78e-100 25 655 12 607
ChainA, amylase [Thermoactinomyces vulgaris]
5Z0U_A 3.98e-100 25 655 12 596
Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) 11 residues (from A363 to N373) deletion mutant (Del11) [Thermoactinomyces vulgaris]
1IZK_A 7.43e-100 25 655 12 607
ChainA, amylase [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 3.10e-99 25 655 41 636
Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI PE=1 SV=1
P38939 9.61e-94 73 620 311 845
Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950 1.42e-89 73 678 311 911
Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
Q08751 1.38e-88 37 692 15 581
Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
P36905 3.19e-84 73 699 314 927
Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2

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
1.000066 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000312_02027.