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CAZyme Information: CIHG_00344-t26_1-p1

You are here: Home > Sequence: CIHG_00344-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 Coccidioides immitis
Lineage Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides immitis
CAZyme ID CIHG_00344-t26_1-p1
CAZy Family AA2
CAZyme Description D-arabinono-1,4-lactone oxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
579 DS016981|CGC1 65047.78 7.9652
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CimmitisH538-4 10724 396776 186 10538
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 27 235 3.6e-30 0.4606986899563319

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
273751 FAD_lactone_ox 9.66e-144 28 472 7 436
sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
397924 ALO 2.54e-108 195 478 1 258
D-arabinono-1,4-lactone oxidase. This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.
223354 GlcD 5.02e-44 26 471 21 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
215258 PLN02465 4.64e-35 28 475 89 565
L-galactono-1,4-lactone dehydrogenase
396238 FAD_binding_4 2.85e-34 36 171 1 139
FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.35e-09 36 232 59 267
1.66e-09 12 198 107 300
3.34e-09 36 194 62 223
4.19e-09 35 201 212 381
4.30e-09 35 218 48 239

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.60e-28 23 245 110 331
Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea]
3.36e-15 28 255 13 238
Alditol Oxidase from Streptomyces coelicolor A3(2): Native Enzyme [Streptomyces coelicolor A3(2)],2VFS_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Xylitol [Streptomyces coelicolor A3(2)],2VFT_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sorbitol [Streptomyces coelicolor A3(2)],2VFU_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Mannitol [Streptomyces coelicolor A3(2)],2VFV_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sulphite [Streptomyces coelicolor A3(2)]
8.35e-11 36 232 37 245
Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]
1.97e-10 36 196 48 212
Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
1.97e-10 36 196 48 212
Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.67e-203 9 526 24 556
Putative D-arabinono-1,4-lactone oxidase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=alo-1 PE=3 SV=1
1.66e-126 19 472 9 514
D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1
6.46e-109 16 472 10 543
D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1
5.38e-107 23 472 16 513
D-arabinono-1,4-lactone oxidase OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=ALO1 PE=3 SV=1
3.43e-106 28 475 19 516
D-arabinono-1,4-lactone oxidase OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=ALO1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000054 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in CIHG_00344-t26_1-p1.