y
Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra020145 |
Family | AA1 |
Protein Properties | Length: 571 Molecular Weight: 63249.7 Isoelectric Point: 7.0379 |
Chromosome | Chromosome/Scaffold: 02 Start: 5253949 End: 5257348 |
Description | Plant L-ascorbate oxidase |
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 |
AA1 | 312 | 543 | 1.90002e-41 |
TVLNYVTAPSSQLPTSPPPETPRWNDFDRSKNFSKKIFAAMGSPSPPETFDERLILLNTQNLIEGFTKWAINNVSLAVPGTPYLGSVKYNLRTGFNRSSP PKDYPVDYDIMTPPRNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTA LRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEG | |||
AA1 | 76 | 334 | 0 |
IHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSS RPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIY SGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAPSSQLPTSPPPETPR |
Full Sequence |
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Protein Sequence Length: 571 Download |
MGMWWIVAVA ILAHTASAAV REYAWEVEYK FGWPDCKEGM VMAVNGQFPG PTIHALAGDT 60 IVVHLTNKLA TEGLVIHWHG IRQLGSPWAD GAAGVTQCAI SPGETFTYNF TVDKPGTHFY 120 HGHYGMQRSA GLYGSLIIDV AKGKKEPLRY DGEFNLLLSD WWHEDVLSQE IGLSSRPMRW 180 IGEAQSILIN GRGQFNCSLA AQFSSTSLPT CTFKEGDQCA PQRLHVEPNK TYRIRLASST 240 ALASLNFAVQ GHKLVVVEAD GNYITPFTTD DIDIYSGETY SVLLTTDQDP SQNYYITAGV 300 RGRKPNTPPA LTVLNYVTAP SSQLPTSPPP ETPRWNDFDR SKNFSKKIFA AMGSPSPPET 360 FDERLILLNT QNLIEGFTKW AINNVSLAVP GTPYLGSVKY NLRTGFNRSS PPKDYPVDYD 420 IMTPPRNRNA KQGNVSCVFP FNVTVDVILQ NANGLNANAS EIHPWHLHGH DFWVLGYGEG 480 KFKPGVDEKT YNLKNPPLRN TVALYPYGWT ALRFVTDNPG VWFFHCHIEP HLHMGMGVVF 540 AEGLNRIGKV PDEALGCGLT KQFLMNRNNP * 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 5.0e-78 | 36 | 543 | 544 | + 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 | 5.0e-107 | 18 | 555 | 563 | + 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. | ||
PLN02191 | PLN02191 | 0 | 1 | 570 | 572 | + L-ascorbate oxidase | ||
TIGR03388 | ascorbase | 0 | 20 | 560 | 541 | + 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. | ||
PLN02604 | PLN02604 | 0 | 16 | 561 | 548 | + oxidoreductase |
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 | AAF20932.1 | 0 | 4 | 570 | 1 | 574 | AF206722_1 ascorbate oxidase [Brassica juncea] |
GenBank | AAF20933.1 | 0 | 5 | 570 | 1 | 573 | AF206723_1 ascorbate oxidase [Brassica juncea] |
DDBJ | BAA20519.1 | 0 | 6 | 568 | 2 | 565 | ascorbate oxidase [Arabidopsis thaliana] |
DDBJ | BAG50513.1 | 0 | 21 | 570 | 21 | 577 | ascorbic acid oxidase [Brassica rapa subsp. chinensis] |
RefSeq | NP_680176.5 | 0 | 21 | 568 | 38 | 586 | L-ascorbate oxidase/ copper ion binding / oxidoreductase [Arabidopsis thaliana] |
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 | 18 | 566 | 1 | 547 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
PDB | 1asq_A | 0 | 18 | 566 | 1 | 547 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
PDB | 1asp_B | 0 | 18 | 566 | 1 | 547 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
PDB | 1asp_A | 0 | 18 | 566 | 1 | 547 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
PDB | 1aso_B | 0 | 18 | 566 | 1 | 547 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |