| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s194_194V6.1 |
| Family | AA1 |
| Protein Properties | Length: 580 Molecular Weight: 64025.2 Isoelectric Point: 6.7013 |
| Chromosome | Chromosome/Scaffold: 194 Start: 828021 End: 830876 |
| 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 | 48 | 412 | 0 |
| GINGGYPGPTIRATQGDTVKVTFENHVVTEGITMHWHGIRQIGSPWADGTAAISQCPILYGESFTYEFIVDRPGTYFYHGHFGCQRAAGFYGPLIVDLPK DKHEPFTYDGEHMIILNDWWHRSIVGQEQGLESINFAWVGEPQSLLLEGRGRYNCSNVPEYKPAGLSCNQSDERCAPHVWSVERGKTYRLRLASVASLSS LNFKIEGHSMKVVEADGHSIEPFWTDNLDLYSGETYSVLVKADKQGDNFHLGLNVRGRNDEQVPTGLGILNYKDKPVQQPTTPAPKGPAWNDFEASKRQA KTYKALQNNPDPTSHPFDASAPVTRTLVLLTTQNKVEGRIKWSINNLTYAPLQTPLLAGLVYNIS | |||
| Full Sequence |
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| Protein Sequence Length: 580 Download |
| MAMKWAGSWV LATVLAVAGL AKAAVVEYHF KVAYMSAAPD CYSKTIIGIN GGYPGPTIRA 60 TQGDTVKVTF ENHVVTEGIT MHWHGIRQIG SPWADGTAAI SQCPILYGES FTYEFIVDRP 120 GTYFYHGHFG CQRAAGFYGP LIVDLPKDKH EPFTYDGEHM IILNDWWHRS IVGQEQGLES 180 INFAWVGEPQ SLLLEGRGRY NCSNVPEYKP AGLSCNQSDE RCAPHVWSVE RGKTYRLRLA 240 SVASLSSLNF KIEGHSMKVV EADGHSIEPF WTDNLDLYSG ETYSVLVKAD KQGDNFHLGL 300 NVRGRNDEQV PTGLGILNYK DKPVQQPTTP APKGPAWNDF EASKRQAKTY KALQNNPDPT 360 SHPFDASAPV TRTLVLLTTQ NKVEGRIKWS INNLTYAPLQ TPLLAGLVYN ISGAYDTTPP 420 PDYPAHGYNI FAPPEPPHTN VGSGMYQFNT GDVVDVIIQN AAALNNVSEI HPWHLHGHDF 480 WILGYGEGQF DPAESPKSYD LKSPPTRNNV ATFPFGWTAV RVHLDNPGAW PFHCHVEWHF 540 HMGMGVVFTH GIDSVRARGI PNSVLGCGLT KQLFSLPSP* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR03390 | ascorbOXfungal | 3.0e-76 | 34 | 551 | 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 | 1.0e-89 | 28 | 548 | 554 | + 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 | 27 | 570 | 551 | + 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 | 28 | 571 | 554 | + oxidoreductase | ||
| PLN02191 | PLN02191 | 0 | 27 | 572 | 552 | + L-ascorbate oxidase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0016491 | oxidoreductase activity |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001751352.1 | 0 | 17 | 576 | 2 | 559 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001763272.1 | 0 | 22 | 572 | 25 | 572 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001771963.1 | 0 | 3 | 576 | 1 | 574 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001775660.1 | 0 | 3 | 579 | 1 | 577 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001781653.1 | 0 | 17 | 572 | 2 | 558 | predicted protein [Physcomitrella patens subsp. patens] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1asq_B | 0 | 23 | 578 | 1 | 550 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
| PDB | 1asq_A | 0 | 23 | 578 | 1 | 550 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
| PDB | 1asp_B | 0 | 23 | 578 | 1 | 550 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
| PDB | 1asp_A | 0 | 23 | 578 | 1 | 550 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
| PDB | 1aso_B | 0 | 23 | 578 | 1 | 550 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
