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Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000308649 |
Family | AA5 |
Protein Properties | Length: 774 Molecular Weight: 87934.3 Isoelectric Point: 5.9444 |
Chromosome | Chromosome/Scaffold: 019373418 Start: 3125 End: 8730 |
Description | glyoxal oxidase-related protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA5 | 2 | 385 | 0 |
STQHILPNGNFILVGGRRMFNYEYIPKGGGSNDVYFPLPFLQETTDPFENNLYPFVFLSTDGNILIFANNRSILLNPTTNKIVRELPVLDGGSRNYPASG MAALLPINLSDPNPKAILAEIXICGGADPRAGKLVEXGIFVTALQDCGRIDITDPKSTWQKEMMPTPRTMGDLXILPTGDILIVNGAKEGIAGWNFAQDP NXTPLLYRPDNPTTQRFTELKATTIPRMYGSTSMVLPDGKILVAGSNTNYYYNFTGVKYPTELRVEKFYPPYFDPLLILDRPMITSDYKGKMVKYRGYIV VEFKLKKAEVDQSDLKVTMYSPPFTTHGFSMGQRLLILAIKKLXNVESEFFRVEVVAPPSAEIAPPGFYLIFVVHXXVPSSGIW |
Full Sequence |
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Protein Sequence Length: 774 Download |
FSTQHILPNG NFILVGGRRM FNYEYIPKGG GSNDVYFPLP FLQETTDPFE NNLYPFVFLS 60 TDGNILIFAN NRSILLNPTT NKIVRELPVL DGGSRNYPAS GMAALLPINL SDPNPKAILA 120 EIXICGGADP RAGKLVEXGI FVTALQDCGR IDITDPKSTW QKEMMPTPRT MGDLXILPTG 180 DILIVNGAKE GIAGWNFAQD PNXTPLLYRP DNPTTQRFTE LKATTIPRMY GSTSMVLPDG 240 KILVAGSNTN YYYNFTGVKY PTELRVEKFY PPYFDPLLIL DRPMITSDYK GKMVKYRGYI 300 VVEFKLKKAE VDQSDLKVTM YSPPFTTHGF SMGQRLLILA IKKLXNVESE FFRVEVVAPP 360 SAEIAPPGFY LIFVVHXXVP SSGIWFSGLN TREPSPESLT LNYLLRINEN ELEIDWSKIR 420 HESLAFALYR VVNRNVRERK VVFGYRERVG VGDGIWFDVY LRKEKVLKGV FRKDKRQDWK 480 LECKCVLEGE SVARRSRRLR SAWPWWVWVW VWGWGTMRTL SVASILLYTL LMLSPLQLNV 540 ALSTETQMLI EEANMSGPYL GLVIPNSYEM DPLLQSPNFT SSNLFIDFSG RRFRFGTIAN 600 KPVILVMTGL SMINAAITTQ LLLSQFDIEG VVHYGIAGHA NPSLSLADVV IPQYWSHSAL 660 WSWQRYGNGP EDELPLEKDG DYTREIGYLN VANYTTNVTD GSSYDNLLNN IWFQPEEVFP 720 IDGTPEERQH AFWVAVDPLY YEISQKLEVS MIDHFQEKEP SISLRIYVMI LVLS 780 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01048 | PNP_UDP_1 | 6.0e-13 | 560 | 652 | 94 | + Phosphorylase superfamily. Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase) | ||
pfam09118 | DUF1929 | 6.0e-17 | 282 | 386 | 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-21 | 281 | 385 | 106 | + 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-52 | 1 | 127 | 127 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0009116 | nucleoside metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI28031.1 | 0 | 1 | 395 | 235 | 629 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002280698.1 | 0 | 1 | 385 | 259 | 643 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002281387.1 | 0 | 1 | 385 | 195 | 580 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324431.1 | 0 | 1 | 385 | 132 | 518 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331167.1 | 0 | 1 | 385 | 219 | 605 | 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 | 2vz3_A | 0.0000007 | 154 | 381 | 424 | 630 | A Chain A, Crystal Structure Of The R3 Form Of Pectate Lyase A, Erwinia Chrysanthemi |
PDB | 2vz1_A | 0.0000007 | 154 | 381 | 424 | 630 | A Chain A, Crystal Structure Of The R3 Form Of Pectate Lyase A, Erwinia Chrysanthemi |
PDB | 2jkx_A | 0.0000007 | 154 | 381 | 424 | 630 | A Chain A, Crystal Structure Of The R3 Form Of Pectate Lyase A, Erwinia Chrysanthemi |
PDB | 2eie_A | 0.0000007 | 154 | 381 | 424 | 630 | A Chain A, Crystal Structure Of Galactose Oxidase Complexed With Azide |
PDB | 1goh_A | 0.0000007 | 154 | 381 | 424 | 630 | A Chain A, Crystal Structure Of Galactose Oxidase Complexed With Azide |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GO507509 | 228 | 522 | 748 | 0 |
GO505690 | 226 | 522 | 746 | 0 |
EE076591 | 232 | 517 | 747 | 0 |
EE107991 | 232 | 517 | 747 | 0 |
GO512867 | 221 | 522 | 741 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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