Basic Information | |
---|---|
Species | Aquilegia coerulea |
Cazyme ID | Aquca_009_00849.1 |
Family | AA5 |
Protein Properties | Length: 540 Molecular Weight: 59152.9 Isoelectric Point: 5.0454 |
Chromosome | Chromosome/Scaffold: 9 Start: 5072960 End: 5074579 |
Description | glyoxal oxidase-related protein |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
AA5 | 27 | 535 | 0 |
PGTWELLVPNAGIASMHTAVTHYNTVILLDRTNIGPTRKMLPKGHCRDDPNDRVLKRDCYAHSVEFDPTTNQIRPLTILTDTWCSSGQFLPDGTLLQTGG DLDGLKKIRKFAPCEPDKFCDWLELSDVELATGRWYSTNQILPDGSVIIVGGRAAHSVEYYPPKAAAPVQLPFLAEVEDNQMDNLYPYVHLLPNGHLFIF ANNKAILYDYTTNTIIRDYPPLDGGPRNYPSAGSSVMLALDGDYSTAVIVVCGGAEYGAFIAKDTDTPAHGSCGRIVATDPEPVWVIEDMPFGRIMGDMV MLPTGEVLIINGAQAGSQGFEMASNPCLYPLLYKPNEPTGLRFMTLTPATIPRMYHATANLLPDGRILLAGSNPHYFYKYIAEFPTELRIEAFSPEYLSP DRANLRPVIEVIPETTPYGTNFDIVVSVPLSVVGIIEVNLASAPYATHSFSQGQRLVKLKVTSAVPEPDGVGKYRIGCIAPPDPKIAPPGYYMVFAVNQG VPSIARWVQ |
Full Sequence |
---|
Protein Sequence Length: 540 Download |
MVSSSTWLLV FFISTIIQPF FIHADLPGTW ELLVPNAGIA SMHTAVTHYN TVILLDRTNI 60 GPTRKMLPKG HCRDDPNDRV LKRDCYAHSV EFDPTTNQIR PLTILTDTWC SSGQFLPDGT 120 LLQTGGDLDG LKKIRKFAPC EPDKFCDWLE LSDVELATGR WYSTNQILPD GSVIIVGGRA 180 AHSVEYYPPK AAAPVQLPFL AEVEDNQMDN LYPYVHLLPN GHLFIFANNK AILYDYTTNT 240 IIRDYPPLDG GPRNYPSAGS SVMLALDGDY STAVIVVCGG AEYGAFIAKD TDTPAHGSCG 300 RIVATDPEPV WVIEDMPFGR IMGDMVMLPT GEVLIINGAQ AGSQGFEMAS NPCLYPLLYK 360 PNEPTGLRFM TLTPATIPRM YHATANLLPD GRILLAGSNP HYFYKYIAEF PTELRIEAFS 420 PEYLSPDRAN LRPVIEVIPE TTPYGTNFDI VVSVPLSVVG IIEVNLASAP YATHSFSQGQ 480 RLVKLKVTSA VPEPDGVGKY RIGCIAPPDP KIAPPGYYMV FAVNQGVPSI ARWVQLIVA* 540 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam09118 | DUF1929 | 8.0e-27 | 432 | 536 | 106 | + 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 | 4.0e-33 | 429 | 536 | 109 | + 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 | 1.0e-111 | 42 | 280 | 244 | + 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 | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABA42922.1 | 0 | 24 | 537 | 11 | 522 | glyoxal oxidase [Vitis pseudoreticulata] |
GenBank | ACV49897.1 | 0 | 24 | 537 | 11 | 522 | glyoxal oxidase [Vitis pseudoreticulata] |
GenBank | ACV49898.1 | 0 | 24 | 537 | 11 | 522 | glyoxal oxidase [Vitis vinifera] |
GenBank | ACV49899.1 | 0 | 24 | 537 | 11 | 522 | glyoxal oxidase [Vitis vinifera] |
RefSeq | XP_002274763.1 | 0 | 3 | 537 | 6 | 541 | PREDICTED: similar to glyoxal oxidase [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2eid_A | 9e-20 | 91 | 536 | 206 | 637 | A Chain A, Galactose Oxidase W290g Mutant |
PDB | 1k3i_A | 2e-19 | 91 | 536 | 223 | 654 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 1t2x_A | 2e-19 | 91 | 536 | 206 | 637 | A Chain A, Glactose Oxidase C383s Mutant Identified By Directed Evolution |
PDB | 2wq8_A | 2e-19 | 91 | 536 | 228 | 659 | A Chain A, Glycan Labelling Using Engineered Variants Of Galactose Oxidase Obtained By Directed Evolution |
PDB | 2eib_A | 2e-19 | 91 | 536 | 206 | 637 | A Chain A, Crystal Structure Of Galactose Oxidase, W290h Mutant |