Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_187092g0010 |
Family | AA5 |
Protein Properties | Length: 578 Molecular Weight: 62972.7 Isoelectric Point: 10.0316 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA5 | 67 | 577 | 0 |
AAGPLGTWQVLVKSAGIASMHTAVTRFNTVIMLDRTNIGASNINLPNGKCRVNPADQVLKRDCTAHSVMLSLNNNGIRPLFIQTDTWCSSGQFLPDGTLL QTGGNLDGALKIRRIAPCPSTGTCDWTEDPNMQLAAPRWYATNQLLPDGRVIVIGGRAVFTYEFVPAAGQGTFPLPFLTATNDAENDNYYPFVHLLPNGN LYIFANRDSIELNYNTGTVVRNFPRIPGEPRNYPSAGSSVLLPLDGPSGYKTAEVMVCGGAQLGAFRQPTKQFPTSQTCGRMVITAAAPVWAMSNMPMRR CMGDMIILPSGEVLLINGAGRGSQGFGFASQPVLNPVIYNPGQLSFSVLQATTIPRVYHSTANLLPDGRVLVAGSNTHQFYTFTGAFPTELRVEAFSPPY LAGVWNARRPQITNAPARVRLGQTFTVVFTLTGQLTALEINLLSAPFSTHSFSQGQRMLRLKLAAAVRVGANMYSVAVTAPPNGNIAPAAYYMLFPLTQG IPGQAAWIQVT |
Full Sequence |
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Protein Sequence Length: 578 Download |
MFTMVGHGYT PTKLYLRLQS VNFLSAIRAR SEIVRAQFKM MRANSMRWMF LILLVNSRLW 60 LPAEIQAAGP LGTWQVLVKS AGIASMHTAV TRFNTVIMLD RTNIGASNIN LPNGKCRVNP 120 ADQVLKRDCT AHSVMLSLNN NGIRPLFIQT DTWCSSGQFL PDGTLLQTGG NLDGALKIRR 180 IAPCPSTGTC DWTEDPNMQL AAPRWYATNQ LLPDGRVIVI GGRAVFTYEF VPAAGQGTFP 240 LPFLTATNDA ENDNYYPFVH LLPNGNLYIF ANRDSIELNY NTGTVVRNFP RIPGEPRNYP 300 SAGSSVLLPL DGPSGYKTAE VMVCGGAQLG AFRQPTKQFP TSQTCGRMVI TAAAPVWAMS 360 NMPMRRCMGD MIILPSGEVL LINGAGRGSQ GFGFASQPVL NPVIYNPGQL SFSVLQATTI 420 PRVYHSTANL LPDGRVLVAG SNTHQFYTFT GAFPTELRVE AFSPPYLAGV WNARRPQITN 480 APARVRLGQT FTVVFTLTGQ LTALEINLLS APFSTHSFSQ GQRMLRLKLA AAVRVGANMY 540 SVAVTAPPNG NIAPAAYYML FPLTQGIPGQ AAWIQVTN |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam09118 | DUF1929 | 2.0e-22 | 475 | 576 | 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 | 3.0e-29 | 472 | 576 | 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 | 4.0e-117 | 86 | 326 | 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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001757263.1 | 0 | 65 | 573 | 22 | 536 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001771982.1 | 0 | 42 | 576 | 5 | 546 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001778975.1 | 0 | 60 | 574 | 12 | 530 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001783776.1 | 0 | 72 | 576 | 14 | 524 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784508.1 | 0 | 72 | 576 | 37 | 549 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 1t2x_A | 2e-16 | 149 | 577 | 223 | 638 | A Chain A, Glactose Oxidase C383s Mutant Identified By Directed Evolution |
PDB | 2eic_A | 8e-16 | 149 | 577 | 223 | 638 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
PDB | 2eib_A | 9e-16 | 149 | 577 | 223 | 638 | A Chain A, Crystal Structure Of Galactose Oxidase, W290h Mutant |
PDB | 2vz3_A | 0.000000000000001 | 149 | 577 | 223 | 638 | A Chain A, Crystal Structure Of Galactose Oxidase, W290h Mutant |
PDB | 2vz1_A | 0.000000000000001 | 149 | 577 | 223 | 638 | A Chain A, Crystal Structure Of Galactose Oxidase, W290h Mutant |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EX306064 | 277 | 165 | 441 | 0 |
DV996283 | 270 | 115 | 384 | 0 |
CO164717 | 271 | 140 | 409 | 0 |
CO482484 | 285 | 285 | 569 | 0 |
CF667952 | 272 | 178 | 448 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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