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CAZyme Information: MGYG000002765_01593

You are here: Home > Sequence: MGYG000002765_01593

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
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella;
CAZyme ID MGYG000002765_01593
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1098 124063.77 4.526
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002765 1830842 MAG Netherlands Europe
Gene Location Start: 384;  End: 3680  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002765_01593.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 194 524 1.2e-121 0.9936708860759493
GH77 729 1089 1.2e-101 0.7591093117408907

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14510 PRK14510 0.0 1 1095 1 1217
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11338 AmyAc_CMD 1.84e-175 133 563 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 7.49e-153 647 1081 2 485
4-alpha-glucanotransferase; Provisional
pfam02446 Glyco_hydro_77 7.91e-139 657 1070 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.
PRK10785 PRK10785 4.55e-100 127 603 116 568
maltodextrin glucosidase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ATP53560.1 0.0 1 1098 1 1098
QIA33253.1 0.0 1 1098 1 1098
AZH69620.1 0.0 1 1098 1 1098
AEB07182.1 0.0 1 1094 1 1094
QOY60572.1 0.0 1 1093 1 1083

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2OWC_A 3.40e-88 648 1071 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]
1CWY_A 8.52e-88 648 1071 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]
1FP8_A 8.52e-88 648 1071 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]
5JIW_A 3.02e-86 648 1071 3 476
Crystalstructure of Thermus aquaticus amylomaltase (GH77) in complex with a 34-meric cycloamylose [Thermus aquaticus]
2X1I_A 1.53e-85 653 1088 8 491
glycosidehydrolase family 77 4-alpha-glucanotransferase from thermus brockianus [Thermus brockianus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P36905 2.41e-97 3 647 256 931
Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P16950 1.59e-95 3 647 253 929
Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38939 1.57e-93 3 647 253 928
Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P38536 2.31e-91 3 592 256 870
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P0A3Q0 2.18e-90 652 1093 6 494
4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 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
1.000068 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002765_01593.