logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003400_03775

You are here: Home > Sequence: MGYG000003400_03775

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 Stenotrophomonas sp003028475
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas sp003028475
CAZyme ID MGYG000003400_03775
CAZy Family GT20
CAZyme Description Trehalose-6-phosphate synthase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
454 MGYG000003400_64|CGC1 50943.99 8.9433
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003400 4365701 MAG United States North America
Gene Location Start: 60966;  End: 62330  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.15

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT20 3 453 9.3e-160 0.968421052631579

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10117 PRK10117 0.0 1 453 1 452
trehalose-6-phosphate synthase; Provisional
TIGR02400 trehalose_OtsA 0.0 3 453 1 455
alpha,alpha-trehalose-phosphate synthase [UDP-forming]. This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is made from two glucose subunits. This model excludes glucosylglycerol-phosphate synthase, an enzyme of an analogous osmoprotectant system in many cyanobacterial strains. This model does not identify archaeal examples, as they are more divergent than glucosylglycerol-phosphate synthase. Sequences that score in the gray zone between the trusted and noise cutoffs include a number of yeast multidomain proteins in which the N-terminal domain may be functionally equivalent to this family. The gray zone also includes the OtsA of Cornyebacterium glutamicum (and related species), shown to be responsible for synthesis of only trace amounts of trehalose while the majority is synthesized by the TreYZ pathway; the significance of OtsA in this species is unclear (see Wolf, et al., ). [Cellular processes, Adaptations to atypical conditions]
cd03788 GT20_TPS 0.0 3 453 1 463
trehalose-6-phosphate synthase. Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain.
COG0380 OtsA 1.66e-176 1 454 14 479
Trehalose-6-phosphate synthase [Carbohydrate transport and metabolism].
pfam00982 Glyco_transf_20 3.72e-164 2 453 1 469
Glycosyltransferase family 20. Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex,.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QGL94151.1 0.0 1 454 1 454
QDL29223.1 0.0 1 454 1 454
VEE54561.1 0.0 1 454 1 454
QPX95348.1 0.0 1 454 1 454
ALA83652.1 0.0 1 454 1 454

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5TVG_A 2.08e-151 3 454 11 463
Crystalstructure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_B Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_C Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_D Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_E Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_F Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_G Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_H Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4]
5UOF_A 1.19e-150 1 454 9 463
Crystalstructure of alpha,alpha-trehalose 6-phosphate sythase from Burkholderia multivorans [Burkholderia multivorans ATCC 17616],5UOF_B Crystal structure of alpha,alpha-trehalose 6-phosphate sythase from Burkholderia multivorans [Burkholderia multivorans ATCC 17616]
5V0T_A 5.19e-150 1 454 9 467
Crystalstructure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_B Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_C Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_D Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_E Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_F Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_G Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_H Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400]
2WTX_A 5.68e-147 1 453 1 452
Insightinto the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase [Escherichia coli K-12],2WTX_B Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase [Escherichia coli K-12],2WTX_C Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase [Escherichia coli K-12],2WTX_D Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase [Escherichia coli K-12]
1UQT_A 7.40e-147 1 453 1 452
Trehalose-6-phosphatefrom E. coli bound with UDP-2-fluoro glucose. [Escherichia coli],1UQT_B Trehalose-6-phosphate from E. coli bound with UDP-2-fluoro glucose. [Escherichia coli],1UQU_A Trehalose-6-phosphate from E. coli bound with UDP-glucose. [Escherichia coli],1UQU_B Trehalose-6-phosphate from E. coli bound with UDP-glucose. [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P55612 7.56e-160 1 452 1 456
Trehalose-6-phosphate synthase OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=otsA PE=3 SV=1
A4WBR1 2.94e-149 1 453 1 452
Trehalose-6-phosphate synthase OS=Enterobacter sp. (strain 638) OX=399742 GN=otsA PE=3 SV=1
A6TB47 5.46e-147 1 453 1 452
Trehalose-6-phosphate synthase OS=Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) OX=272620 GN=otsA PE=3 SV=1
P31677 3.11e-146 1 453 1 452
Trehalose-6-phosphate synthase OS=Escherichia coli (strain K12) OX=83333 GN=otsA PE=1 SV=3
B1LQW0 3.11e-146 1 453 1 452
Trehalose-6-phosphate synthase OS=Escherichia coli (strain SMS-3-5 / SECEC) OX=439855 GN=otsA 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
1.000054 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003400_03775.