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CAZyme Information: KID65241.1

You are here: Home > Sequence: KID65241.1

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 Metarhizium anisopliae
Lineage Ascomycota; Sordariomycetes; ; Clavicipitaceae; Metarhizium; Metarhizium anisopliae
CAZyme ID KID65241.1
CAZy Family GH18
CAZyme Description phosphoribosyl transferase domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1150 AZNF01000007|CGC11 124282.44 7.3500
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_ManisopliaeARSEF549 10891 1276135 0 10891
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 310 504 9.5e-39 0.37554585152838427

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
235028 PRK02304 1.06e-26 957 1123 1 154
adenine phosphoribosyltransferase; Provisional
398111 P-mevalo_kinase 3.11e-26 774 892 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).
223577 Apt 6.19e-21 957 1109 3 144
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism].
396238 FAD_binding_4 1.16e-19 314 456 1 136
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.
177930 PLN02293 3.53e-18 959 1123 14 165
adenine phosphoribosyltransferase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.01e-14 308 758 55 479
7.57e-14 314 511 70 243
2.28e-13 314 754 63 482
8.46e-13 313 504 120 290
1.15e-11 293 754 35 483

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.00e-18 959 1131 4 166
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]
7.00e-18 959 1131 4 166
Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 14 hours post crystallization [Homo sapiens],6FD4_B Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 14 hours post crystallization [Homo sapiens],6FD5_A Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 14 days post crystallization (with AMP and PPi products partially generated) [Homo sapiens],6FD5_B Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 14 days post crystallization (with AMP and PPi products partially generated) [Homo sapiens],6FD6_A Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 30 days post crystallization (with AMP and PPi products fully generated) [Homo sapiens],6FD6_B Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 30 days post crystallization (with AMP and PPi products fully generated) [Homo sapiens]
7.17e-18 959 1131 5 167
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]
7.35e-18 959 1131 6 168
Crystal Structure of F173G Mutant of Human APRT [Homo sapiens],4X45_B Crystal Structure of F173G Mutant of Human APRT [Homo sapiens]
7.35e-18 959 1131 6 168
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.68e-22 314 751 48 437
FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
3.70e-20 962 1132 8 164
Adenine phosphoribosyltransferase OS=Mycobacterium sp. (strain JLS) OX=164757 GN=apt PE=3 SV=1
3.70e-20 962 1132 8 164
Adenine phosphoribosyltransferase OS=Mycobacterium sp. (strain MCS) OX=164756 GN=apt PE=3 SV=1
3.70e-20 962 1132 8 164
Adenine phosphoribosyltransferase OS=Mycobacterium sp. (strain KMS) OX=189918 GN=apt PE=3 SV=1
8.85e-20 962 1131 5 161
Adenine phosphoribosyltransferase OS=Roseiflexus castenholzii (strain DSM 13941 / HLO8) OX=383372 GN=apt PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000064 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KID65241.1.