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CAZyme Information: PSK36426.1

You are here: Home > Sequence: PSK36426.1

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 [Candida] pseudohaemulonis
Lineage Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] pseudohaemulonis
CAZyme ID PSK36426.1
CAZy Family GH132
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
994 PYFQ01000011|CGC1 111618.62 6.7080
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CpseudohaemuloniiB12108 5285 N/A 151 5134
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in PSK36426.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 104 339 2.3e-47 0.9098039215686274

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
173825 ascorbate_peroxidase 1.39e-118 70 343 2 253
Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
270250 PBP2_PDT_like 7.12e-66 547 708 30 184
Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic binding protein fold. Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
240234 PTZ00027 5.70e-65 359 541 1 182
60S ribosomal protein L6; Provisional
223155 PheA2 8.17e-63 546 769 30 233
Prephenate dehydratase [Amino acid transport and metabolism].
178218 PLN02608 5.15e-57 107 339 33 243
L-ascorbate peroxidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.51e-211 1 358 1278 1635
5.72e-204 56 358 54 356
5.72e-204 56 358 54 356
1.62e-203 56 358 54 356
1.65e-143 76 358 94 372

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.13e-99 359 548 1 190
Chain q, Ribosomal 60S subunit protein L9B [Candida albicans SC5314],7Q0F_q Chain q, Ribosomal 60S subunit protein L9B [Candida albicans SC5314],7Q0P_q Chain q, Ribosomal 60S subunit protein L9B [Candida albicans SC5314]
5.06e-95 65 359 3 294
Structure of isoniazid (INH) bound to cytochrome c peroxidase mutant N184R Y36A [Saccharomyces cerevisiae]
7.55e-95 69 359 9 296
Structure of cytochrome c peroxidase mutant N184R Y36A [Saccharomyces cerevisiae],4A6Z_A Cytochrome c peroxidase with bound guaiacol [Saccharomyces cerevisiae]
1.05e-94 69 359 9 296
cytochrome c peroxidase in complex with phenol [Saccharomyces cerevisiae]
2.42e-94 69 359 4 291
Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M25_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M26_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M27_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M28_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M29_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2A_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2B_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2C_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2D_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2E_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2F_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2G_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2H_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],3M2I_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.71e-137 55 358 59 359
Cytochrome c peroxidase, mitochondrial OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=CCP1 PE=3 SV=1
5.74e-129 62 358 71 364
Cytochrome c peroxidase, mitochondrial OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CCP1 PE=3 SV=2
1.56e-95 63 352 52 336
Cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=CCP1 PE=3 SV=1
1.08e-92 62 359 65 357
Cytochrome c peroxidase, mitochondrial OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=CAGL0K08184g PE=3 SV=1
1.71e-92 62 359 66 361
Cytochrome c peroxidase, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=CCP1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999832 0.000195

TMHMM  Annotations      download full data without filtering help

Start End
19 41