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CAZyme Information: MGYG000003466_00593

You are here: Home > Sequence: MGYG000003466_00593

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 Treponema_D sp900767955
Lineage Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900767955
CAZyme ID MGYG000003466_00593
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1143 124139.68 4.9158
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003466 2580548 MAG Fiji Oceania
Gene Location Start: 51523;  End: 54954  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 618 1013 2.8e-108 0.9972222222222222

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09505 malS 1.98e-137 574 1064 185 654
alpha-amylase; Reviewed
cd11339 AmyAc_bac_CMD_like_2 3.93e-38 582 1055 6 342
Alpha amylase catalytic domain found in bacterial 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). This group of CMDs is bacterial. 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.
COG0366 AmyA 6.67e-37 582 1012 4 355
Glycosidase [Carbohydrate transport and metabolism].
cd00551 AmyAc_family 8.86e-31 582 1009 3 253
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.
smart00642 Aamy 6.46e-30 583 710 1 98
Alpha-amylase domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QSI03195.1 6.44e-302 12 1143 17 1106
ADZ82879.1 2.74e-139 573 1124 49 594
QEH68420.1 1.53e-138 573 1124 49 594
CQR56565.1 1.17e-130 574 1124 60 601
BAB04132.1 1.29e-130 574 1120 44 583

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5A2A_A 2.77e-23 575 868 5 200
CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A 4.15e-23 575 868 39 234
CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A 1.21e-20 575 868 6 201
Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
7P4W_A 4.87e-14 576 868 6 216
ChainA, Alpha-amylase [Aspergillus oryzae]
2GUY_A 4.92e-14 576 868 6 216
Orthorhombiccrystal structure (space group P21212) of Aspergillus niger alpha-amylase at 1.6 A resolution [Aspergillus oryzae],2GVY_A Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution [Aspergillus oryzae],2GVY_B Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution [Aspergillus oryzae],3KWX_A Chemically modified Taka alpha-amylase [Aspergillus oryzae],3VX0_A Crystal Structure of alpha-amylase from Aspergillus oryzae [Aspergillus oryzae RIB40],3VX1_A Crystal Structure of alpha-Amylase from Aspergillus oryzae [Aspergillus oryzae RIB40],6TAA_A Structure And Molecular Model Refinement Of Aspergillus Oryzae (Taka) Alpha-Amylase: An Application Of The Simulated-Annealing Method [Aspergillus oryzae],7TAA_A Family 13 Alpha Amylase In Complex With Acarbose [Aspergillus oryzae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P25718 3.36e-96 557 1064 164 647
Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884 8.04e-21 615 933 95 372
Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P21543 1.13e-19 567 708 738 862
Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q8A1G0 3.95e-16 582 711 129 248
Neopullulanase SusA OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=susA PE=3 SV=1
P21567 7.89e-16 568 819 25 239
Alpha-amylase OS=Saccharomycopsis fibuligera OX=4944 GN=ALP1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000055 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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