| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10028342 |
| Family | AA4 |
| Protein Properties | Length: 584 Molecular Weight: 64521.9 Isoelectric Point: 6.6984 |
| Chromosome | Chromosome/Scaffold: 413 Start: 194932 End: 199730 |
| Description | FAD-linked oxidases family protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| AA4 | 126 | 327 | 3.1e-23 |
| FKEILGEKNVVQDERLEAANSDWMHKYKGSSRLLLLPKSTDEVSKVLKYCNSRCLAVVPQGGNTGLVGGSVPVFDEVIINMALMNKVISFDEISGILVCE AGCILEDLISYLDNQGFIMPLDLGAKGSCQIGGNVATNAGGLRLVRYGSLHGTVLGLETVLANGDVLDMLGTLRKDNTGYDLKHLFIGSEGSLGIITKVS IL | |||
| Full Sequence |
|---|
| Protein Sequence Length: 584 Download |
| MMTPAMTEKY RAVVRLLRKN PRSFHDRRFI PQEQFSGGGF AAFGYNDWFE AGRDQCVSHR 60 GCQKRGLWNS ARSFAGHCVA PLSNFMDRGF MRDYSMYQRR SFGAVASEIQ RSSKFATLNS 120 DDLLYFKEIL GEKNVVQDER LEAANSDWMH KYKGSSRLLL LPKSTDEVSK VLKYCNSRCL 180 AVVPQGGNTG LVGGSVPVFD EVIINMALMN KVISFDEISG ILVCEAGCIL EDLISYLDNQ 240 GFIMPLDLGA KGSCQIGGNV ATNAGGLRLV RYGSLHGTVL GLETVLANGD VLDMLGTLRK 300 DNTGYDLKHL FIGSEGSLGI ITKVSILTPP KLSSVNIAFL ACEDYLSCQK LLLEAKRNLG 360 EILSAFEFLD SVAMDVVLNN LDGARNPLAP SKHNFYVLIE TTGSEESYDK EKIEKFLLGS 420 MESGLVSDGV LAQDINQASA FWHLREGIPE SLQRAGAVYK YDLSLPVEKM YDIVEEMRAR 480 LGDSVKVVGY GHLGDGNLHL NVSAQRYDDA ILAQIEPFVY EWTSKHRGSI SAEHGVGLMK 540 ANKIFYSKSP ETVQLMASIK KLLDPNTILN PYKVLPHSLM SYN* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01565 | FAD_binding_4 | 8.0e-37 | 157 | 293 | 137 | + FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. | ||
| PLN02805 | PLN02805 | 1.0e-44 | 150 | 576 | 446 | + D-lactate dehydrogenase [cytochrome] | ||
| pfam02913 | FAD-oxidase_C | 1.0e-59 | 331 | 574 | 252 | + FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. | ||
| TIGR00387 | glcD | 6.0e-73 | 160 | 573 | 435 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
| COG0277 | GlcD | 5.0e-108 | 125 | 577 | 465 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
| GO:0016491 | oxidoreductase activity |
| GO:0050660 | flavin adenine dinucleotide binding |
| 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 |
| EMBL | CAB16815.1 | 0 | 96 | 581 | 40 | 523 | actin interacting protein [Arabidopsis thaliana] |
| RefSeq | NP_568003.2 | 0 | 96 | 581 | 72 | 558 | FAD linked oxidase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002268002.1 | 0 | 98 | 581 | 66 | 550 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002310828.1 | 0 | 92 | 583 | 43 | 530 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002521506.1 | 0 | 97 | 582 | 79 | 565 | d-lactate dehydrognease 2, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3pm9_F | 0 | 117 | 575 | 12 | 476 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_E | 0 | 117 | 575 | 12 | 476 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_D | 0 | 117 | 575 | 12 | 476 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_C | 0 | 117 | 575 | 12 | 476 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_B | 0 | 117 | 575 | 12 | 476 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
 | ||||
| Hit | Length | Start | End | EValue |
| GO838775 | 330 | 162 | 491 | 0 |
| CO071824 | 285 | 144 | 428 | 0 |
| CO071363 | 284 | 144 | 427 | 0 |
| GO839525 | 331 | 151 | 481 | 0 |
| HO419275 | 404 | 176 | 578 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
| Phylogeny |
|---|
 |