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CAZyme Information: MGYG000002407_02107

You are here: Home > Sequence: MGYG000002407_02107

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 Cohnella sp900169535
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Cohnella; Cohnella sp900169535
CAZyme ID MGYG000002407_02107
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
945 MGYG000002407_18|CGC5 102296.73 4.6884
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002407 6325359 Isolate not provided not provided
Gene Location Start: 185918;  End: 188755  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.98 3.2.1.60 3.2.1.- 3.2.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 36 341 4.3e-116 0.8
CBM26 562 629 1.4e-21 0.9066666666666666

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09505 malS 1.61e-151 37 415 297 678
alpha-amylase; Reviewed
pfam03423 CBM_25 2.86e-21 747 839 4 95
Carbohydrate binding domain (family 25).
cd11338 AmyAc_CMD 1.16e-20 36 383 107 383
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.
pfam16738 CBM26 2.74e-20 563 628 1 66
Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
cd00551 AmyAc_family 1.11e-18 183 337 97 253
Alpha amylase catalytic domain family. 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; and 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 this 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
QMV42547.1 0.0 37 883 158 1093
QQZ60411.1 5.54e-257 36 907 174 1055
CQR56565.1 9.64e-257 36 812 174 961
QMV43648.1 3.80e-251 36 907 163 1049
QKH59997.1 2.88e-250 36 907 159 1108

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2C3G_A 2.55e-27 561 649 7 95
ChainA, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3H_A Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_B Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_C Chain C, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_D Chain D, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_E Chain E, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_F Chain F, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_G Chain G, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_H Chain H, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans]
2LAA_A 6.83e-26 747 839 5 102
SolutionStrucuture of the CBM25-1 of beta/alpha-amylase from Paenibacillus polymyxa [Paenibacillus polymyxa]
2LAB_A 1.74e-25 746 839 4 102
SolutionStrucuture of the CBM25-2 of beta/alpha-amylase from Paenibacillus polymyxa [Paenibacillus polymyxa]
1K85_A 4.26e-21 654 740 2 88
ChainA, CHITINASE A1 [Niallia circulans]
2C3V_B 6.39e-21 750 839 13 101
ChainB, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_A Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_B Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_C Chain C, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_D Chain D, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3X_A Chain A, Alpha-amylase G-6 [Halalkalibacterium halodurans C-125],2C3X_B Chain B, Alpha-amylase G-6 [Halalkalibacterium halodurans C-125]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P25718 2.56e-95 38 415 297 671
Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
A0P8X0 1.55e-64 652 945 811 1290
Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1
P21543 1.36e-21 747 939 459 661
Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P06547 6.33e-21 738 839 453 559
Beta-amylase OS=Niallia circulans OX=1397 PE=3 SV=1
P20533 4.20e-18 645 744 454 553
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 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
1.000071 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002407_02107.