Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.009G159700.2 |
Family | AA1 |
Protein Properties | Length: 449 Molecular Weight: 50266.8 Isoelectric Point: 8.0545 |
Chromosome | Chromosome/Scaffold: 09 Start: 12339657 End: 12342834 |
Description | Plant L-ascorbate oxidase |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 1 | 431 | 0 |
MQRSAGLYGSLIVDVAEGEKEPFHYDGEFDLLLSDWWHESAHHQEVGLSSRPMRWIGEPQTLLVNGRGQYGCSLAAHYSNNSSLSQCNVTGHEQWAPYIL HVDPNKTYRIRLSSTTALASLNLAIGNHKMLVVEADGNYLQPFETDDLDIYSGESYSVLLKTSQDPSQNYWISFGVRGRKPQTPQALTILNYKTNSASKF PLSPPPVTPRWDDYAHSKAFTNKVKALDHKTIPKPPSTYHRRIILLNTQNKMNGYTKWSINNVSLSLPATPYLGSIRFGLQNGFDQTKPPESFPVQYDVM KPPGNPNTTTGNGVYMLSYYSTVDVILQNANALAENVSEIHPWHLHGHDFWVLGYGEGKFTKDDEKKFNMKNPPYRNSAVIFPYGWTALRFVADNPGVWA FHCHIEPHLHMGMGVVLAEGVQRLPKIPKEA |
Full Sequence |
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Protein Sequence Length: 449 Download |
MQRSAGLYGS LIVDVAEGEK EPFHYDGEFD LLLSDWWHES AHHQEVGLSS RPMRWIGEPQ 60 TLLVNGRGQY GCSLAAHYSN NSSLSQCNVT GHEQWAPYIL HVDPNKTYRI RLSSTTALAS 120 LNLAIGNHKM LVVEADGNYL QPFETDDLDI YSGESYSVLL KTSQDPSQNY WISFGVRGRK 180 PQTPQALTIL NYKTNSASKF PLSPPPVTPR WDDYAHSKAF TNKVKALDHK TIPKPPSTYH 240 RRIILLNTQN KMNGYTKWSI NNVSLSLPAT PYLGSIRFGL QNGFDQTKPP ESFPVQYDVM 300 KPPGNPNTTT GNGVYMLSYY STVDVILQNA NALAENVSEI HPWHLHGHDF WVLGYGEGKF 360 TKDDEKKFNM KNPPYRNSAV IFPYGWTALR FVADNPGVWA FHCHIEPHLH MGMGVVLAEG 420 VQRLPKIPKE ALSCGLTGKK FMTGNNLG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 3.0e-54 | 9 | 420 | 457 | + L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized. | ||
TIGR03389 | laccase | 2.0e-59 | 5 | 434 | 459 | + laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. | ||
PLN02604 | PLN02604 | 1.0e-165 | 1 | 437 | 439 | + oxidoreductase | ||
TIGR03388 | ascorbase | 0 | 1 | 437 | 438 | + L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. | ||
PLN02191 | PLN02191 | 0 | 1 | 445 | 446 | + L-ascorbate oxidase |
Gene Ontology | |
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GO Term | Description |
GO:0005507 | copper ion binding |
GO:0016491 | oxidoreductase activity |
GO:0055114 | oxidation-reduction 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 |
GenBank | ABK96191.1 | 0 | 1 | 448 | 148 | 594 | unknown [Populus trichocarpa] |
RefSeq | XP_002275678.1 | 0 | 1 | 443 | 137 | 576 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299782.1 | 0 | 1 | 448 | 120 | 566 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002312838.1 | 0 | 1 | 448 | 150 | 597 | l-ascorbate oxidase precursor [Populus trichocarpa] |
RefSeq | XP_002530197.1 | 0 | 1 | 445 | 146 | 587 | l-ascorbate oxidase, putative [Ricinus communis] |
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 | 1asq_B | 0 | 1 | 442 | 109 | 546 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asq_A | 0 | 1 | 442 | 109 | 546 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asp_B | 0 | 1 | 442 | 109 | 546 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asp_A | 0 | 1 | 442 | 109 | 546 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1aso_B | 0 | 1 | 442 | 109 | 546 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY305215 | 307 | 133 | 439 | 0 |
FC929669 | 292 | 133 | 424 | 0 |
CA926921 | 227 | 68 | 294 | 0 |
CX044124 | 279 | 164 | 442 | 0 |
DY904134 | 289 | 155 | 443 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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