Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10012975m |
Family | AA5 |
Protein Properties | Length: 623 Molecular Weight: 68235 Isoelectric Point: 9.814 |
Chromosome | Chromosome/Scaffold: 2 Start: 6743577 End: 6745865 |
Description | glyoxal oxidase-related protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA5 | 66 | 621 | 0 |
GGAPEAQTNWAGKWELFLENSGVSAMHAILMPVINQVQFYDATIWRISKIKLPPGVPCHVVNAKTNRIDCWAHSVLVDVNTGAIKPLSVCIPLITIHNNM ISFGLCMIKYDLHLQLSTDTWCSSGGLTINGTLVSTGGYGGGANTVRYLAACKDCGWVEYPQALAAKRWYSTQATLPDGNFFVIGGRDALNYEYIPAEGQ NNRKLYDSLLLRQTDDPEENNLYPFVWLNTDGNLFIFANNRSILLSPKTNQVIKEFPQLPGGARNYPGSGSSALLPIHLYVKNPKVIPAEVLICGGSKQD AYYRAGKKVFEPALQDCARMRINSAKPRWKTEMMPMPRVMSDTVILPNGDILLVNGGKRGCSGWGYGKDPAFTPILYKPRAARGKRFRELAASTIPRMYH SIAIALPDGKVLVGGSNTNDGYKYNVEFPTELRVEKFSPPYLDPALANLRPKIVNNATPKQIRYGQNFNVKVDLNQKDVTKENLKVHMLAPSFTTHSISM NMRMLFLGIVGVNPAGAGSFEIQTVAPPNGNIAPPGYYLIFAVYKGVPSIGEWIQI |
Full Sequence |
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Protein Sequence Length: 623 Download |
MRASTRVIWT VSVLMLAAVS EAIFPLPFLP FLPGFNNGFR DNNAAVKVAK PVAPGAVGKA 60 GGRRRGGAPE AQTNWAGKWE LFLENSGVSA MHAILMPVIN QVQFYDATIW RISKIKLPPG 120 VPCHVVNAKT NRIDCWAHSV LVDVNTGAIK PLSVCIPLIT IHNNMISFGL CMIKYDLHLQ 180 LSTDTWCSSG GLTINGTLVS TGGYGGGANT VRYLAACKDC GWVEYPQALA AKRWYSTQAT 240 LPDGNFFVIG GRDALNYEYI PAEGQNNRKL YDSLLLRQTD DPEENNLYPF VWLNTDGNLF 300 IFANNRSILL SPKTNQVIKE FPQLPGGARN YPGSGSSALL PIHLYVKNPK VIPAEVLICG 360 GSKQDAYYRA GKKVFEPALQ DCARMRINSA KPRWKTEMMP MPRVMSDTVI LPNGDILLVN 420 GGKRGCSGWG YGKDPAFTPI LYKPRAARGK RFRELAASTI PRMYHSIAIA LPDGKVLVGG 480 SNTNDGYKYN VEFPTELRVE KFSPPYLDPA LANLRPKIVN NATPKQIRYG QNFNVKVDLN 540 QKDVTKENLK VHMLAPSFTT HSISMNMRML FLGIVGVNPA GAGSFEIQTV APPNGNIAPP 600 GYYLIFAVYK GVPSIGEWIQ IV* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam09118 | DUF1929 | 3.0e-27 | 515 | 621 | 108 | + 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 | 1.0e-31 | 512 | 621 | 111 | + 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 | 2.0e-114 | 91 | 361 | 275 | + 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 | AAL84955.1 | 0 | 1 | 622 | 1 | 594 | AT5g19580/T20D1_100 [Arabidopsis thaliana] |
RefSeq | NP_176897.1 | 0 | 1 | 622 | 1 | 615 | glyoxal oxidase-related [Arabidopsis thaliana] |
RefSeq | NP_197459.1 | 0 | 1 | 622 | 1 | 594 | glyoxal oxidase-related [Arabidopsis thaliana] |
RefSeq | XP_002324431.1 | 0 | 77 | 621 | 2 | 521 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331167.1 | 0 | 77 | 621 | 89 | 608 | 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 | 2eic_A | 1e-17 | 184 | 622 | 225 | 638 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
PDB | 1k3i_A | 2e-17 | 184 | 622 | 242 | 655 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 2vz3_A | 2e-17 | 184 | 622 | 225 | 638 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 2vz1_A | 2e-17 | 184 | 622 | 225 | 638 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 2jkx_A | 2e-17 | 184 | 622 | 225 | 638 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |