Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.006G011600.1 |
Family | AA1 |
Protein Properties | Length: 573 Molecular Weight: 64069.2 Isoelectric Point: 8.3832 |
Chromosome | Chromosome/Scaffold: 06 Start: 5782362 End: 5788641 |
Description | Plant L-ascorbate oxidase |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 23 | 546 | 0 |
RVRHYRFDVEYMMRKPDCLEHVVMGINGQFPGPTIRAEVGDTLHIALTNKLFTEGTVIHWHGIRQVGTPWADGTAAISQCAINPGETFHYRFIVERPGTY FYHGHHGMQRSAGLYGSLIVDLPKGQKEAFHYDGEFNLLLSDFWHTSSHEQEVGLSSIPLKWIGEPQSLLINGRGQFNCSLAAKFINTTLPECQFKGGEE CAPQILHVEPNKTYRIRVASTTSLAALNLAISNHKLVVVEADGNYVTPFVIDDMDIYSGETYSVLLRTDQDPKKNYWLSIGVRGRKPNTTQGLTILNYKT ISASVFPTSPPPLTPLWNDFERSKAFTKKIIAKMGTPQPPKRSDRTIFLLNTQNRVDGFTKWSINNVSLTLPPTPYLGSIKFKLNDAFDQTPPPVTFPQD YDIFNPPVNPNSTIGNGVYKFNLNEVVDVILQNANQLSGNGSEIHPWHLHGHDFWVLGYGEGKFKQGDEKKFNLTHAPLRNTAVIFPYGWTALRFKADNP GVWAFHCHIEPHLHMGMGVIFAEG |
Full Sequence |
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Protein Sequence Length: 573 Download |
MGLKAVLVWC IWLGLIQYSV GGRVRHYRFD VEYMMRKPDC LEHVVMGING QFPGPTIRAE 60 VGDTLHIALT NKLFTEGTVI HWHGIRQVGT PWADGTAAIS QCAINPGETF HYRFIVERPG 120 TYFYHGHHGM QRSAGLYGSL IVDLPKGQKE AFHYDGEFNL LLSDFWHTSS HEQEVGLSSI 180 PLKWIGEPQS LLINGRGQFN CSLAAKFINT TLPECQFKGG EECAPQILHV EPNKTYRIRV 240 ASTTSLAALN LAISNHKLVV VEADGNYVTP FVIDDMDIYS GETYSVLLRT DQDPKKNYWL 300 SIGVRGRKPN TTQGLTILNY KTISASVFPT SPPPLTPLWN DFERSKAFTK KIIAKMGTPQ 360 PPKRSDRTIF LLNTQNRVDG FTKWSINNVS LTLPPTPYLG SIKFKLNDAF DQTPPPVTFP 420 QDYDIFNPPV NPNSTIGNGV YKFNLNEVVD VILQNANQLS GNGSEIHPWH LHGHDFWVLG 480 YGEGKFKQGD EKKFNLTHAP LRNTAVIFPY GWTALRFKAD NPGVWAFHCH IEPHLHMGMG 540 VIFAEGVHKV GKIPREALTC GLTGKKLVEN GH* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 1.0e-82 | 48 | 546 | 530 | + 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 | 9.0e-94 | 22 | 558 | 565 | + 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. | ||
TIGR03388 | ascorbase | 0 | 24 | 563 | 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. | ||
PLN02191 | PLN02191 | 0 | 5 | 571 | 571 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 0 | 1 | 563 | 572 | + 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 |
DDBJ | BAH28261.1 | 0 | 4 | 572 | 5 | 573 | ascorbate oxidase [Pisum sativum] |
EMBL | CAA75577.1 | 0 | 3 | 562 | 4 | 564 | L-ascorbate oxidase [Medicago truncatula] |
EMBL | CAN82127.1 | 0 | 20 | 570 | 4 | 554 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002275678.1 | 0 | 6 | 570 | 13 | 577 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002312838.1 | 0 | 3 | 568 | 16 | 591 | l-ascorbate oxidase precursor [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 | 1asq_B | 0 | 23 | 570 | 2 | 548 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asq_A | 0 | 23 | 570 | 2 | 548 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_B | 0 | 23 | 570 | 2 | 548 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_A | 0 | 23 | 570 | 2 | 548 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1aso_B | 0 | 23 | 570 | 2 | 548 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |