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CAZyme Information: KAB8204772.1

You are here: Home > Sequence: KAB8204772.1

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 parasiticus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus parasiticus
CAZyme ID KAB8204772.1
CAZy Family GH135
CAZyme Description Phosphomevalonate kinase [Source:UniProtKB/TrEMBL;Acc:A0A5N6DI24]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
996 107758.17 6.7169
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AparasiticusCBS117618 14005 N/A 253 13752
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 137 337 4.3e-42 0.3951965065502183

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
398111 P-mevalo_kinase 2.11e-29 608 726 1 111
Phosphomevalonate kinase. Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation of 5-phosphomevalonate into 5-diphosphomevalonate, an essential step in isoprenoid biosynthesis via the mevalonate pathway. This family represents the animal type of the enzyme. The other is the ERG8 type, found in plants and fungi, and some bacteria (see pfam00288).
235028 PRK02304 2.07e-24 803 995 1 175
adenine phosphoribosyltransferase; Provisional
396238 FAD_binding_4 6.26e-20 152 288 4 136
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.
223354 GlcD 1.73e-19 132 589 15 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
177930 PLN02293 9.41e-17 805 977 14 173
adenine phosphoribosyltransferase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.90e-13 150 591 71 491
2.48e-13 128 588 35 483
4.06e-12 150 588 64 482
4.07e-12 151 588 65 482
2.55e-11 113 336 70 290

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.78e-17 804 977 3 166
Crystal Structure of Human APRT wild type in complex with PRPP and Mg2+ [Homo sapiens],6FCH_B Crystal Structure of Human APRT wild type in complex with PRPP and Mg2+ [Homo sapiens],6FCL_A Crystal Structure of Human APRT wild type in complex with AMP [Homo sapiens],6FCL_B Crystal Structure of Human APRT wild type in complex with AMP [Homo sapiens],6HGP_A Crystal Structure of Human APRT wild type in complex with Phosphate ion. [Homo sapiens],6HGP_B Crystal Structure of Human APRT wild type in complex with Phosphate ion. [Homo sapiens],6HGR_A Crystal Structure of Human APRT wild type in complex with IMP [Homo sapiens],6HGR_B Crystal Structure of Human APRT wild type in complex with IMP [Homo sapiens],6HGS_A Crystal Structure of Human APRT wild type in complex with GMP [Homo sapiens],6HGS_B Crystal Structure of Human APRT wild type in complex with GMP [Homo sapiens]
2.84e-17 804 977 4 167
Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_B Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_C Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_D Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6HGQ_A Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_B Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_C Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_D Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens]
2.91e-17 804 977 5 168
Crystal Structure of F173G Mutant of Human APRT [Homo sapiens],4X45_B Crystal Structure of F173G Mutant of Human APRT [Homo sapiens]
2.91e-17 804 977 5 168
Human Adenine Phosphoribosyltransferase [Homo sapiens],1ZN7_A Human Adenine Phosphoribosyltransferase Complexed with PRPP, ADE and R5P [Homo sapiens],1ZN7_B Human Adenine Phosphoribosyltransferase Complexed with PRPP, ADE and R5P [Homo sapiens],1ZN8_A Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution [Homo sapiens],1ZN8_B Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution [Homo sapiens],1ZN9_A Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms [Homo sapiens],1ZN9_B Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms [Homo sapiens]
2.91e-17 804 977 5 168
Crystal Structure of Mutant R89Q of human Adenine phosphoribosyltransferase [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.06e-26 152 587 51 439
FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
4.25e-21 804 994 5 180
Adenine phosphoribosyltransferase OS=Cricetulus griseus OX=10029 GN=APRT PE=3 SV=2
5.78e-21 804 994 5 180
Adenine phosphoribosyltransferase OS=Mastomys natalensis OX=10112 GN=APRT PE=3 SV=1
8.69e-21 808 982 5 166
Adenine phosphoribosyltransferase OS=Roseiflexus castenholzii (strain DSM 13941 / HLO8) OX=383372 GN=apt PE=3 SV=1
1.46e-20 804 994 5 180
Adenine phosphoribosyltransferase OS=Rattus norvegicus OX=10116 GN=Aprt PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000049 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KAB8204772.1.