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CAZyme Information: FFUJ_06618-t31_1-p1
You are here: Home > Sequence: FFUJ_06618-t31_1-p1
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 | Fusarium fujikuroi | |||||||||||
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| Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium fujikuroi | |||||||||||
| CAZyme ID | FFUJ_06618-t31_1-p1 | |||||||||||
| CAZy Family | GT90 | |||||||||||
| CAZyme Description | related to 2-haloalkanoic acid dehalogenase | |||||||||||
| CAZyme Property |
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| Genome Property |
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CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 319787 | HAD_L2-DEX | 3.65e-21 | 8 | 234 | 3 | 216 | L-2-haloacid dehalogenase. L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. |
| 130495 | HAD_type_II | 1.23e-18 | 8 | 206 | 4 | 190 | 2-haloalkanoic acid dehalogenase, type II. Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related. |
| 395571 | Hydrolase | 1.73e-14 | 8 | 201 | 4 | 191 | haloacid dehalogenase-like hydrolase. This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Pseudomonas sp. (S)-2-haloacid dehalogenase 1. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria. |
| 340817 | GT1_Gtf-like | 8.44e-11 | 240 | 373 | 227 | 338 | UDP-glycosyltransferases and similar proteins. This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics. |
| 223943 | YigB | 2.40e-08 | 6 | 236 | 5 | 226 | FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 2.23e-280 | 1 | 373 | 1 | 373 | |
| 3.87e-86 | 244 | 373 | 39 | 168 | |
| 3.26e-85 | 235 | 373 | 21 | 159 | |
| 3.26e-85 | 235 | 373 | 21 | 159 | |
| 7.65e-70 | 224 | 373 | 250 | 393 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3.37e-12 | 6 | 239 | 15 | 239 | Crystal Structure analysis of a Dehalogenase [Burkholderia cepacia],2NO4_B Crystal Structure analysis of a Dehalogenase [Burkholderia cepacia] |
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| 2.81e-11 | 6 | 239 | 15 | 239 | Crystal Structure analysis of a Dehalogenase with intermediate complex [Burkholderia cepacia],2NO5_B Crystal Structure analysis of a Dehalogenase with intermediate complex [Burkholderia cepacia] |
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| 1.84e-09 | 8 | 237 | 22 | 236 | Chain A, (S)-2-haloacid dehalogenase [Zobellia galactanivorans],7ARP_B Chain B, (S)-2-haloacid dehalogenase [Zobellia galactanivorans] |
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| 3.64e-08 | 8 | 237 | 22 | 236 | Chain A, (S)-2-haloacid dehalogenase [Zobellia galactanivorans],7ASZ_B Chain B, (S)-2-haloacid dehalogenase [Zobellia galactanivorans] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.53e-11 | 6 | 239 | 6 | 230 | (S)-2-haloacid dehalogenase 4A OS=Burkholderia cepacia OX=292 GN=hdl IVa PE=1 SV=3 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000086 | 0.000000 |