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CAZyme Information: AKAW_11344-t41_1-p1

You are here: Home > Sequence: AKAW_11344-t41_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 Aspergillus luchuensis
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
CAZyme ID AKAW_11344-t41_1-p1
CAZy Family GT61
CAZyme Description phosphoribosyl transferase domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1161 127124.44 6.9402
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AluchuensisIFO4308 11755 1033177 267 11488
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 310 513 2.3e-38 0.4017467248908297

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
235028 PRK02304 2.69e-27 968 1158 4 173
adenine phosphoribosyltransferase; Provisional
223577 Apt 1.70e-24 970 1147 5 169
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism].
398111 P-mevalo_kinase 1.16e-20 771 879 1 104
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).
396238 FAD_binding_4 1.15e-17 313 444 2 129
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.
395104 Pribosyltran 4.42e-17 992 1132 1 120
Phosphoribosyl transferase domain. This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7, Hypoxanthine-guanine-xanthine phosphoribosyl-transferase, Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10, Uracil phosphoribosyl-transferase EC:2.4.2.9, Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, at the very N-terminus of this domain is the P-Loop NTPase domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.94e-16 313 748 49 461
1.10e-15 310 754 57 484
4.10e-15 313 751 49 464
9.57e-15 313 748 49 461
1.00e-14 313 748 58 470

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.07e-18 969 1142 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]
7.25e-18 969 1142 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]
7.43e-18 969 1142 5 168
Crystal Structure of F173G Mutant of Human APRT [Homo sapiens],4X45_B Crystal Structure of F173G Mutant of Human APRT [Homo sapiens]
7.43e-18 969 1142 5 168
Crystal Structure of Mutant R89Q of human Adenine phosphoribosyltransferase [Homo sapiens]
7.43e-18 969 1142 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.48e-25 316 750 52 439
FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
5.13e-19 969 1158 5 179
Adenine phosphoribosyltransferase OS=Cricetulus griseus OX=10029 GN=APRT PE=3 SV=2
6.99e-19 969 1158 5 179
Adenine phosphoribosyltransferase OS=Dipodillus campestris OX=41199 GN=APRT PE=3 SV=1
1.31e-18 968 1119 17 159
Adenine phosphoribosyltransferase OS=Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) OX=391904 GN=apt PE=3 SV=1
1.79e-18 960 1119 9 159
Adenine phosphoribosyltransferase OS=Bifidobacterium longum (strain NCC 2705) OX=206672 GN=apt PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000051 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in AKAW_11344-t41_1-p1.