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CAZyme Information: TSTA_099740-t26_1-p1

You are here: Home > Sequence: TSTA_099740-t26_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 Talaromyces stipitatus
Lineage Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
CAZyme ID TSTA_099740-t26_1-p1
CAZy Family GH7
CAZyme Description polysaccharide deacetylase, putative
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
610 EQ962658|CGC17 69876.17 6.6712
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TstipitatusATCC10500 12629 441959 146 12483
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in TSTA_099740-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE4 208 325 4.9e-21 0.8538461538461538

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
213022 CE4_NodB_like_6s_7s 5.17e-40 210 390 1 171
Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.
238385 MoaE 1.16e-30 467 595 1 124
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.
396800 MoaE 4.14e-29 462 575 1 113
MoaE protein. This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.
200575 CE4_ClCDA_like 4.80e-29 205 393 3 191
Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41) from Colletotrichum lindemuthianum (also known as Glomerella lindemuthiana), which is a member of the carbohydrate esterase 4 (CE4) superfamily. ClCDA catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. It consists of a single catalytic domain similar to the deformed (alpha/beta)8 barrel fold adopted by other CE4 esterases, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine), to carry out acid/base catalysis. It possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Unlike its bacterial homologs, ClCDA contains two intramolecular disulfide bonds that may add stability to this secreted protein. The family also includes many uncharacterized deacetylases and hypothetical proteins mainly from eukaryotes, which show high sequence similarity to ClCDA.
200578 CE4_CtAXE_like 1.46e-26 213 348 4 130
Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.48e-52 445 607 599 757
1.07e-20 200 406 31 239
2.23e-20 210 408 67 254
1.47e-19 197 406 59 267
1.47e-19 197 406 59 267

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.56e-19 438 597 1 154
Crystal structure of human molybdopterin synthase complex [Homo sapiens],5MPO_D Crystal structure of human molybdopterin synthase complex [Homo sapiens]
3.23e-19 195 414 25 238
Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
4.44e-19 460 582 10 131
Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B) [Homo sapiens],4AP8_B Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B) [Homo sapiens],4AP8_C Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B) [Homo sapiens],4AP8_D Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B) [Homo sapiens]
1.85e-18 453 585 1 132
Structural analysis of molybdopterin synthases from two mycobacteria pathogens [Mycolicibacterium smegmatis MC2 155],6JC0_D Structural analysis of molybdopterin synthases from two mycobacteria pathogens [Mycolicibacterium smegmatis MC2 155]
7.59e-15 213 407 120 304
Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.39e-65 407 607 8 195
Molybdopterin synthase catalytic subunit OS=Coccidioides immitis (strain RS) OX=246410 GN=cnxH PE=3 SV=2
8.69e-59 446 604 36 195
Molybdopterin synthase catalytic subunit OS=Ajellomyces capsulatus (strain NAm1 / WU24) OX=2059318 GN=cnxH PE=3 SV=2
6.24e-55 445 607 16 174
Molybdopterin synthase catalytic subunit OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=cnxH PE=3 SV=1
3.10e-54 438 607 29 190
Molybdopterin synthase catalytic subunit OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=cnxH PE=3 SV=1
8.58e-54 438 610 20 184
Molybdopterin synthase catalytic subunit OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=cnxH PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000215 0.999766 CS pos: 20-21. Pr: 0.9816

TMHMM  Annotations      download full data without filtering help

Start End
7 24