logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002104_01582

You are here: Home > Sequence: MGYG000002104_01582

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 Olsenella_E sp003150175
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Atopobiaceae; Olsenella_E; Olsenella_E sp003150175
CAZyme ID MGYG000002104_01582
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1089 MGYG000002104_18|CGC1 121152.86 4.6058
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002104 2042785 MAG Mongolia Asia
Gene Location Start: 19306;  End: 22575  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002104_01582.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 196 530 2.6e-120 0.9936708860759493
GH77 735 1081 1.3e-107 0.7327935222672065

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14510 PRK14510 4.51e-179 1 1067 1 1191
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11338 AmyAc_CMD 9.11e-170 133 567 2 389
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.
PRK14508 PRK14508 4.77e-158 651 1066 2 472
4-alpha-glucanotransferase; Provisional
pfam02446 Glyco_hydro_77 3.02e-138 661 1066 2 455
4-alpha-glucanotransferase. These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.
PLN02635 PLN02635 3.14e-106 653 1066 27 498
disproportionating enzyme

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOY60572.1 0.0 1 1089 1 1083
ADK68793.1 0.0 1 1089 1 1095
SDS02076.1 0.0 1 1089 3 1113
AKT48087.1 0.0 1 1089 1 1094
QUC03509.1 0.0 1 1089 1 1085

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2X1I_A 5.99e-92 657 1067 8 476
glycosidehydrolase family 77 4-alpha-glucanotransferase from thermus brockianus [Thermus brockianus]
1FP8_A 3.07e-91 652 1067 3 476
StructureOf The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 [Thermus thermophilus],1FP9_A Structure Of Amylomaltase From Thermus Thermophilus Hb8 In Space Group C2 [Thermus thermophilus]
1CWY_A 3.07e-91 652 1067 3 476
CrystalStructure Of Amylomaltase From Thermus Aquaticus, A Glycosyltransferase Catalysing The Production Of Large Cyclic Glucans [Thermus aquaticus],1ESW_A X-Ray Structure Of Acarbose Bound To Amylomaltase From Thermus Aquaticus. Implications For The Synthesis Of Large Cyclic Glucans [Thermus aquaticus]
2OWC_A 6.24e-91 652 1067 6 478
Structureof a covalent intermediate in Thermus thermophilus amylomaltase [Thermus thermophilus],2OWW_A Covalent intermediate in amylomaltase in complex with the acceptor analog 4-deoxyglucose [Thermus thermophilus],2OWX_A THERMUS THERMOPHILUS AMYLOMALTASE AT pH 5.6 [Thermus thermophilus]
5JIW_A 1.50e-88 652 1067 3 476
Crystalstructure of Thermus aquaticus amylomaltase (GH77) in complex with a 34-meric cycloamylose [Thermus aquaticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P36905 7.01e-106 4 626 257 905
Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38939 8.55e-105 4 640 254 917
Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950 2.06e-104 4 640 254 918
Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38536 9.13e-103 4 585 257 852
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
O87172 1.68e-90 652 1067 3 476
4-alpha-glucanotransferase OS=Thermus thermophilus OX=274 GN=malQ 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
1.000046 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002104_01582.