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CAZyme Information: EKG10439.1

You are here: Home > Sequence: EKG10439.1

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 Macrophomina phaseolina
Lineage Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
CAZyme ID EKG10439.1
CAZy Family AA2
CAZyme Description Peptidase S10 serine carboxypeptidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
844 AHHD01000518|CGC2 92426.00 6.1612
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MphaseolinaMS6 14712 1126212 906 13806
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EKG10439.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT1 515 843 1.1e-36 0.7460732984293194

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
187557 dTDP_GD_SDR_e 1.03e-139 32 347 1 311
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs. This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
215146 PLN02260 9.83e-129 32 368 7 340
probable rhamnose biosynthetic enzyme
224013 RfbB 7.11e-113 32 360 1 329
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis].
273489 dTDP_gluc_dehyt 1.90e-98 33 354 1 316
dTDP-glucose 4,6-dehydratase. This protein is related to UDP-glucose 4-epimerase (GalE) and likewise has an NAD cofactor. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
182313 PRK10217 1.57e-71 31 354 1 338
dTDP-glucose 4,6-dehydratase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.81e-100 403 842 6 445
1.81e-100 403 842 6 445
8.13e-100 402 844 5 455
9.52e-89 400 844 3 450
6.57e-80 403 844 6 446

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.48e-77 31 347 4 314
X-ray Structure of the R141 Sugar 4,6-dehydratase from Acanthamoeba polyphaga Minivirus [Acanthamoeba polyphaga mimivirus],6VLO_B X-ray Structure of the R141 Sugar 4,6-dehydratase from Acanthamoeba polyphaga Minivirus [Acanthamoeba polyphaga mimivirus],6VLO_C X-ray Structure of the R141 Sugar 4,6-dehydratase from Acanthamoeba polyphaga Minivirus [Acanthamoeba polyphaga mimivirus],6VLO_D X-ray Structure of the R141 Sugar 4,6-dehydratase from Acanthamoeba polyphaga Minivirus [Acanthamoeba polyphaga mimivirus]
5.36e-68 33 354 26 341
Chain A, dTDP-glucose 4,6-dehydratase [Bacillus anthracis str. Ames],6BI4_B Chain B, dTDP-glucose 4,6-dehydratase [Bacillus anthracis str. Ames],6BI4_C Chain C, dTDP-glucose 4,6-dehydratase [Bacillus anthracis str. Ames],6BI4_D Chain D, dTDP-glucose 4,6-dehydratase [Bacillus anthracis str. Ames]
4.49e-63 31 359 1 343
Dtdp-Glucose 4,6-Dehydratase From E. Coli [Escherichia coli],1BXK_B Dtdp-Glucose 4,6-Dehydratase From E. Coli [Escherichia coli]
5.15e-63 33 365 2 329
Crystal Structure of DesIV (dTDP-glucose 4,6-dehydratase) from Streptomyces venezuelae with NAD and TYD bound [Streptomyces venezuelae]
1.02e-62 33 359 2 346
Chain A, DTDP-D-GLUCOSE 4,6-DEHYDRATASE [Salmonella enterica subsp. enterica serovar Typhimurium],1G1A_B Chain B, DTDP-D-GLUCOSE 4,6-DEHYDRATASE [Salmonella enterica subsp. enterica serovar Typhimurium],1G1A_C Chain C, DTDP-D-GLUCOSE 4,6-DEHYDRATASE [Salmonella enterica subsp. enterica serovar Typhimurium],1G1A_D Chain D, DTDP-D-GLUCOSE 4,6-DEHYDRATASE [Salmonella enterica subsp. enterica serovar Typhimurium],1KEU_A Chain A, dTDP-D-glucose 4,6-dehydratase [Salmonella enterica subsp. enterica serovar Typhimurium],1KEU_B Chain B, dTDP-D-glucose 4,6-dehydratase [Salmonella enterica subsp. enterica serovar Typhimurium],1KEW_A Chain A, dTDP-D-glucose 4,6-dehydratase [Salmonella enterica subsp. enterica serovar Typhimurium],1KEW_B Chain B, dTDP-D-glucose 4,6-dehydratase [Salmonella enterica subsp. enterica serovar Typhimurium]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.49e-104 23 368 4 342
Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2 OS=Arabidopsis thaliana OX=3702 GN=RHM2 PE=1 SV=1
4.32e-103 32 368 7 340
Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1 OS=Arabidopsis thaliana OX=3702 GN=RHM1 PE=1 SV=1
1.04e-102 32 368 7 340
Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3 OS=Arabidopsis thaliana OX=3702 GN=RHM3 PE=2 SV=1
2.56e-99 27 365 13 349
dTDP-D-glucose 4,6-dehydratase OS=Mus musculus OX=10090 GN=Tgds PE=2 SV=2
6.81e-97 27 365 13 349
dTDP-D-glucose 4,6-dehydratase OS=Homo sapiens OX=9606 GN=TGDS PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000052 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in EKG10439.1.