Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 485786 |
Family | AA5 |
Protein Properties | Length: 543 Molecular Weight: 59741.1 Isoelectric Point: 5.6191 |
Chromosome | Chromosome/Scaffold: 5 Start: 16787477 End: 16789225 |
Description | glyoxal oxidase-related protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA5 | 28 | 540 | 0 |
DLPGTWELIVQDAGIASMHTAVTRFNTVILLDRTNIGPSRKALDRHRCRRDPKDAALKHDCYAHSVLFDLGTNQIRPLMIQTDTWCSSGQFLSDGSLLQT GGDKDGFKKIRKFEPCDPNETCDWVELQDTELITGRWYATNQILPDGSVIIVGGRGTNTVEYYPPRQNGAVPFQFLADVEDKQMDNLYPYVHLLPDDDGG HLFVFANSRAVKYDHRLNTVVREYPPLDGGPRNYPSGGSSAMLAIQGDFTTAEILICGGAQSGAFTARAIDAPAHGTCGRIIATAADPVWVTEEMPFGRI MGDMVNLPTGEILIINGAQAGSQGFEMGSDPCLYPLLYRPDQPIGLRFMTLNPGTVPRMYHSTANLLPDGRILLAGSNPHYFYKFNAEFPTELRIEAFSP EYLSPDRANLRPEIREIPQIVRYGEVFDVFVTVPLPVVEIIQMNWGSAPFATHSFSQGQRLVKLTVAPSVPDGVGRYRIQCTAPPNGAVSPPGYYMAFAV NQGVPSIARWIRI |
Full Sequence |
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Protein Sequence Length: 543 Download |
MAEFVPSYTP GIVLVLQTIL LFSIARADLP GTWELIVQDA GIASMHTAVT RFNTVILLDR 60 TNIGPSRKAL DRHRCRRDPK DAALKHDCYA HSVLFDLGTN QIRPLMIQTD TWCSSGQFLS 120 DGSLLQTGGD KDGFKKIRKF EPCDPNETCD WVELQDTELI TGRWYATNQI LPDGSVIIVG 180 GRGTNTVEYY PPRQNGAVPF QFLADVEDKQ MDNLYPYVHL LPDDDGGHLF VFANSRAVKY 240 DHRLNTVVRE YPPLDGGPRN YPSGGSSAML AIQGDFTTAE ILICGGAQSG AFTARAIDAP 300 AHGTCGRIIA TAADPVWVTE EMPFGRIMGD MVNLPTGEIL IINGAQAGSQ GFEMGSDPCL 360 YPLLYRPDQP IGLRFMTLNP GTVPRMYHST ANLLPDGRIL LAGSNPHYFY KFNAEFPTEL 420 RIEAFSPEYL SPDRANLRPE IREIPQIVRY GEVFDVFVTV PLPVVEIIQM NWGSAPFATH 480 SFSQGQRLVK LTVAPSVPDG VGRYRIQCTA PPNGAVSPPG YYMAFAVNQG VPSIARWIRI 540 VS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam09118 | DUF1929 | 1.0e-29 | 438 | 540 | 104 | + Domain of unknown function (DUF1929). Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase. | ||
cd02851 | E_set_GO_C | 6.0e-33 | 435 | 540 | 107 | + C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. | ||
pfam07250 | Glyoxal_oxid_N | 8.0e-136 | 45 | 286 | 247 | + Glyoxal oxidase N-terminus. This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABA42922.1 | 0 | 24 | 541 | 8 | 522 | glyoxal oxidase [Vitis pseudoreticulata] |
GenBank | ACV49899.1 | 0 | 24 | 541 | 8 | 522 | glyoxal oxidase [Vitis vinifera] |
RefSeq | NP_190963.1 | 0 | 1 | 542 | 1 | 545 | glyoxal oxidase-related [Arabidopsis thaliana] |
RefSeq | XP_002274763.1 | 0 | 24 | 541 | 27 | 541 | PREDICTED: similar to glyoxal oxidase [Vitis vinifera] |
RefSeq | XP_002322929.1 | 0 | 13 | 542 | 3 | 528 | predicted protein [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2eid_A | 3e-18 | 106 | 541 | 221 | 638 | A Chain A, Galactose Oxidase W290g Mutant |
PDB | 2wq8_A | 9e-18 | 106 | 541 | 243 | 660 | A Chain A, Glycan Labelling Using Engineered Variants Of Galactose Oxidase Obtained By Directed Evolution |
PDB | 2eib_A | 3e-17 | 106 | 541 | 221 | 638 | A Chain A, Crystal Structure Of Galactose Oxidase, W290h Mutant |
PDB | 1k3i_A | 3e-17 | 106 | 541 | 238 | 655 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 2vz3_A | 3e-17 | 106 | 541 | 221 | 638 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |