logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003215_02188

You are here: Home > Sequence: MGYG000003215_02188

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 1XD42-69 sp014287635
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; 1XD42-69; 1XD42-69 sp014287635
CAZyme ID MGYG000003215_02188
CAZy Family CBM34
CAZyme Description Neopullulanase 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
709 MGYG000003215_264|CGC1 82310.54 5.1135
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003215 2655157 MAG United States North America
Gene Location Start: 8992;  End: 11121  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 195 577 1.2e-94 0.9968354430379747
CBM34 40 137 2.1e-18 0.9166666666666666

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11338 AmyAc_CMD 3.93e-163 140 613 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 3.07e-135 39 699 12 596
maltodextrin glucosidase; Provisional
pfam00128 Alpha-amylase 1.32e-56 195 576 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 8.91e-55 141 649 1 438
Glycosidase [Carbohydrate transport and metabolism].
cd11316 AmyAc_bac2_AmyA 9.67e-48 195 611 20 403
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL08719.1 0.0 4 699 5 697
CBL13964.1 0.0 4 699 5 709
VCV23525.1 0.0 4 699 5 727
AWY98996.1 0.0 1 702 1 700
QQQ94235.1 2.86e-317 1 699 1 697

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5Z0T_A 6.37e-106 27 699 11 635
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 9.57e-105 27 699 11 635
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 1.34e-104 27 699 11 635
ChainA, amylase [Thermoactinomyces vulgaris]
1IZK_A 2.64e-104 27 699 11 635
ChainA, amylase [Thermoactinomyces vulgaris]
5Z0U_A 3.89e-104 27 699 11 624
Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) 11 residues (from A363 to N373) deletion mutant (Del11) [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 1.12e-103 27 699 40 664
Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI PE=1 SV=1
P38939 2.46e-81 43 699 270 917
Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P21517 2.79e-79 135 639 117 558
Maltodextrin glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=malZ PE=1 SV=5
P36905 1.88e-78 79 699 317 920
Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P16950 2.66e-78 43 699 270 918
Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu 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
1.000057 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003215_02188.