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CAZyme Information: MGYG000001874_02108

You are here: Home > Sequence: MGYG000001874_02108

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 QAMI01 sp900554095
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; QAMI01; QAMI01 sp900554095
CAZyme ID MGYG000001874_02108
CAZy Family GH57
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
743 87024.82 5.5071
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001874 2081057 MAG Denmark Europe
Gene Location Start: 2894;  End: 5125  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001874_02108.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH57 11 466 9.3e-82 0.8198433420365535

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10796 GH57N_APU 1.91e-99 10 449 1 312
N-terminal catalytic domain of thermoactive amylopullulanases; glycoside hydrolase family 57 (GH57). Pullulanases (EC 3.2.1.41) are capable of hydrolyzing the alpha-1,6 glucosidic bonds of pullulan, producing maltotriose. Amylopullulanases (APU, E.C 3.2.1.1/41) are type II pullulanases which can also degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch, producing oligosaccharides. This subfamily includes GH57 archaeal thermoactive APUs, which show both pullulanolytic and amylolytic activities. They have an acid pH optimum and the presence of Ca2+ might increase their activity, thermostability, and substrate affinity. Besides GH57 thermoactive APUs, all mesophilic and some thermoactive APUs belong to glycoside hydrolase family 13 with catalytic features distinct from GH57. This subfamily also includes many uncharacterized proteins found in bacteria and archaea.
COG1449 COG1449 7.99e-82 6 562 2 521
Alpha-amylase/alpha-mannosidase, GH57 family [Carbohydrate transport and metabolism].
pfam03065 Glyco_hydro_57 2.39e-39 11 424 1 282
Glycosyl hydrolase family 57. This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes.
cd01022 GH57N_like 8.59e-28 176 450 62 313
N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57. Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
COG1543 COG1543 5.46e-10 181 528 112 474
Predicted glycosyl hydrolase, contains GH57 and DUF1957 domains [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AOR38601.1 0.0 1 742 1 740
ACI20270.1 2.19e-151 8 716 3 673
QDZ40903.1 1.61e-144 8 732 5 730
QGZ90793.1 1.26e-143 8 742 5 745
ACB51797.1 4.26e-143 8 741 33 775

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2B5D_X 1.77e-07 159 496 93 464
Crystalstructure of the novel alpha-amylase AmyC from Thermotoga maritima [Thermotoga maritima MSB8]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000025 0.000008 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001874_02108.