Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10436303g0010 |
Family | AA5 |
Protein Properties | Length: 586 Molecular Weight: 64898.5 Isoelectric Point: 9.1277 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA5 | 26 | 583 | 0 |
QLHEGRWELLLQNAGVSAMHMTLTHTNKLLIFDQKLAGSSQIVRTDPPCNNATIAASEDCGAHSIEYDIATNRVRPLHLLTDTFCSSXXXXNRVRPLHLL TDTFCSSAAFASNGTLIHTGGWNDGTRVIRYFIPCSDATCNWIESPTRLAANRWYASNQILPDDRVIVVGGRRSFNYEFVPKAPSDRAFQLPLLLKTNTV GEENNLYPFLHLSSDGNLFVFANKDSILFDYKKNQVVKTFPTMPGGGARNYPSSGSSVMLPLESANNFQKVEILVCGGAPNGAFSKAGMNQTFVEALRSC GRMEITSQNPQWQMEDMPGPRVMGDMLILPTAQILIINGAKNGTAGWQFAREPALSPFLYTPTEAMGNRFRVLAPTKIPRMYHSTASVLPDGRILVAGSN SNFGYRFSGVPFPTELRVEAYIPYYLHSHYDPKRVNITAISTREIKYGSKFNVRFFLTNITAISTREIKYGSKFIVRFFLTRRLSVNIDFHAYAPPFTTH SLSMNQRMLSLATTAIVKDKDGYSVGLTAPPSAVVAPSGYYLLTIVNGGVPSKAEWIR |
Full Sequence |
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Protein Sequence Length: 586 Download |
MGELTTLLVQ AVIIVCCCMR LVSGDQLHEG RWELLLQNAG VSAMHMTLTH TNKLLIFDQK 60 LAGSSQIVRT DPPCNNATIA ASEDCGAHSI EYDIATNRVR PLHLLTDTFC SSXXXXNRVR 120 PLHLLTDTFC SSAAFASNGT LIHTGGWNDG TRVIRYFIPC SDATCNWIES PTRLAANRWY 180 ASNQILPDDR VIVVGGRRSF NYEFVPKAPS DRAFQLPLLL KTNTVGEENN LYPFLHLSSD 240 GNLFVFANKD SILFDYKKNQ VVKTFPTMPG GGARNYPSSG SSVMLPLESA NNFQKVEILV 300 CGGAPNGAFS KAGMNQTFVE ALRSCGRMEI TSQNPQWQME DMPGPRVMGD MLILPTAQIL 360 IINGAKNGTA GWQFAREPAL SPFLYTPTEA MGNRFRVLAP TKIPRMYHST ASVLPDGRIL 420 VAGSNSNFGY RFSGVPFPTE LRVEAYIPYY LHSHYDPKRV NITAISTREI KYGSKFNVRF 480 FLTNITAIST REIKYGSKFI VRFFLTRRLS VNIDFHAYAP PFTTHSLSMN QRMLSLATTA 540 IVKDKDGYSV GLTAPPSAVV APSGYYLLTI VNGGVPSKAE WIRFIS |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam09118 | DUF1929 | 4.0e-18 | 484 | 583 | 103 | + 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 | 2.0e-23 | 485 | 583 | 100 | + 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-96 | 44 | 303 | 265 | + 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 |
RefSeq | NP_191321.1 | 0 | 8 | 583 | 8 | 545 | glyoxal oxidase-related [Arabidopsis thaliana] |
RefSeq | XP_001771865.1 | 0 | 46 | 582 | 1 | 489 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002276473.1 | 0 | 29 | 585 | 44 | 570 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002280559.1 | 0 | 17 | 584 | 28 | 552 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002301997.1 | 0 | 30 | 584 | 5 | 523 | 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 | 2eib_A | 4e-17 | 127 | 583 | 225 | 636 | A Chain A, Crystal Structure Of Galactose Oxidase, W290h Mutant |
PDB | 2eid_A | 8e-17 | 127 | 583 | 225 | 636 | A Chain A, Galactose Oxidase W290g Mutant |
PDB | 1k3i_A | 8e-17 | 127 | 583 | 242 | 653 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 2vz3_A | 9e-17 | 127 | 583 | 225 | 636 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 2vz1_A | 9e-17 | 127 | 583 | 225 | 636 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |