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CAZyme Information: GAQ04921.1

You are here: Home > Sequence: GAQ04921.1

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 Aspergillus lentulus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
CAZyme ID GAQ04921.1
CAZy Family CE5
CAZyme Description pdp3-interacting factor 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
493 BCLY01000004|CGC7 55283.20 4.4863
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AlentulusIFM54703 9916 N/A 259 9657
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in GAQ04921.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA11 30 206 5.8e-67 0.9162303664921466

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
226802 MtnX 1.27e-54 203 428 5 217
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid transport and metabolism].
319826 HAD_Pase 4.13e-49 203 423 1 210
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily. Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. Members of this family belong 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.
213629 DKMTPPase-SF 2.29e-26 203 394 3 188
2,3-diketo-5-methylthio-1-phosphopentane phosphatase. This phosphatase is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. With the exception of OMNI|NTL01BS01361 from B. subtilis and GP|15024582 from Clostridium acetabutylicum, the members of this group are all eukaryotic, spanning metazoa, plants and fungi. The B. subtilus gene (YkrX, renamed MtnX) is part of an operon for the conversion of methylthioribose (MTR) to methionine. It works with the enolase MtnW, a RuBisCO homolog. The combination of MtnW and MtnX achieves the same overall reaction as the enolase-phosphatase MtnC. The function of MtnX was shown by Ashida, et al. (2003) to be 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, rather than 2,3-diketo-5-methylthio-1-phosphopentane phosphatase as proposed earlier. See the Genome Property for methionine salvage for more details. In eukaryotes, methionine salvage from methylthioadenosine also occurs. It seems reasonable that members of this family in eukaryotes fulfill a similar role as in Bacillus. A more specific, equivalog-level model is TIGR03333. Note that SP|P53981 from S. cerevisiae, a member of this family, is annotated as a "probable membrane protein" due to a predicted transmembrane helix. The region in question contains the second of the three conserved HAD superfamily catalytic motifs and thus, considering the fold of the HAD catalytic domain, is unlikely to be a transmembrane region in fact. [Central intermediary metabolism, Other]
236562 mtnX 5.56e-19 203 425 5 215
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed
273653 HAD-SF-IB 1.44e-15 207 387 5 177
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like. This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
6.96e-106 4 206 6 208
1.59e-98 11 205 10 204
1.59e-98 11 205 10 204
3.52e-98 3 207 5 209
5.43e-98 11 205 46 240

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.50e-35 20 205 1 201
Structure of Aspergillus oryzae AA11 Lytic Polysaccharide Monooxygenase with Zn [Aspergillus oryzae],4MAI_A Structure of Aspergillus oryzae AA11 Lytic Polysaccharide Monooxygenase with Cu(I) [Aspergillus oryzae]
2.24e-08 270 431 74 223
Crystal structure of MtnX phosphatase from Bacillus Subtilis at 2.00 A resolution [Bacillus subtilis],2FEA_B Crystal structure of MtnX phosphatase from Bacillus Subtilis at 2.00 A resolution [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.29e-49 204 425 9 225
Pdp3-interacting factor 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ptf1 PE=1 SV=1
4.28e-42 203 426 5 229
Polyol phosphate phosphatase PYP1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PYP1 PE=1 SV=1
1.41e-14 204 427 5 216
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase OS=Bacillus mycoides (strain KBAB4) OX=315730 GN=mtnX PE=3 SV=1
3.51e-14 204 427 5 216
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase OS=Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98) OX=315749 GN=mtnX PE=3 SV=1
1.18e-13 262 424 63 214
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase OS=Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 / 255-15) OX=262543 GN=mtnX PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000226 0.999755 CS pos: 19-20. Pr: 0.9504

TMHMM  Annotations      help

There is no transmembrane helices in GAQ04921.1.