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CAZyme Information: MGYG000000464_01086

You are here: Home > Sequence: MGYG000000464_01086

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 QHMH01 sp003258795
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; QHMH01; QHMH01 sp003258795
CAZyme ID MGYG000000464_01086
CAZy Family GH57
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
728 MGYG000000464_5|CGC1 85395.27 4.6667
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000464 1534068 MAG Fiji Oceania
Gene Location Start: 36705;  End: 38891  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH57 1 454 5.5e-71 0.8120104438642297

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10796 GH57N_APU 1.67e-79 1 436 7 313
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 6.71e-72 1 527 12 502
Alpha-amylase/alpha-mannosidase, GH57 family [Carbohydrate transport and metabolism].
pfam03065 Glyco_hydro_57 8.08e-31 1 420 6 292
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 2.10e-22 142 436 32 313
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.
cd10792 GH57N_AmyC_like 2.04e-09 138 426 69 401
N-terminal catalytic domain of alpha-amylase ( AmyC ) and similar proteins. Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, EC 3.2.1.1) play essential roles in alpha-glucan metabolism by catalyzing the hydrolysis of polysaccharides such as amylose starch, and beta-limit dextrin. This subfamily is represented by a novel alpha-amylase (AmyC) encoded by hyperthermophilic organism Thermotoga maritime ORF tm1438, and its prokaryotic homologs. AmyC functions as a homotetramer and shows thermostable amylolytic activity. It is strongly inhibited by acarbose. AmyC is composed of a N-terminal catalytic domain, containing a distorted TIM-barrel structure with a characteristic (beta/alpha)7 fold motif, and two additional less conserved domains. There are other two canonical alpha-amylases encoded from T. maritime that lack the sequence similarity to AmyC, and belong to a different superfamily.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AOR38601.1 2.29e-273 1 726 16 740
BAZ67081.1 4.00e-124 2 727 14 743
QSV74130.1 2.43e-122 2 727 14 744
ALT22081.1 4.68e-122 2 727 14 743
QSV56735.1 6.75e-122 2 727 14 744

PDB Hits      help

has no PDB hit.

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
0.999979 0.000082 0.000002 0.000000 0.000000 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000464_01086.