| Basic Information | |
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| Species | Linum usitatissimum |
| Cazyme ID | Lus10041792 |
| Family | AA4 |
| Protein Properties | Length: 538 Molecular Weight: 58707.9 Isoelectric Point: 6.6231 |
| Chromosome | Chromosome/Scaffold: 272 Start: 1783552 End: 1788126 |
| Description | FAD-linked oxidases family protein |
| 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 |
| AA4 | 101 | 278 | 1.5e-21 |
| QKYKGSSRLLLLPKSTNEVSKVLKYCNSRCLAVVPQGGNTGLVGGSVPVFDEVIINMALMNKVISFDETSGILVCEAGCILEDLISYLDNQGFIMPLDLG AKGSCQIGGNVATNAGGLRLVRYGSLHGTVLGLETVLANGDVLDMLGTLRKDNTGYDLKHLFIGSEGSLGIITKVSIL | |||
| Full Sequence |
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| Protein Sequence Length: 538 Download |
| MAEKYRATAP LLRKTSRSFH GGGFTAFGYT DWFEAGRDQC VSYRGCKKRG LWSSARSFAG 60 HCVASPSNFT DRGFTRDYFM GHQRSFGADE RLEAANNDWM QKYKGSSRLL LLPKSTNEVS 120 KVLKYCNSRC LAVVPQGGNT GLVGGSVPVF DEVIINMALM NKVISFDETS GILVCEAGCI 180 LEDLISYLDN QGFIMPLDLG AKGSCQIGGN VATNAGGLRL VRYGSLHGTV LGLETVLANG 240 DVLDMLGTLR KDNTGYDLKH LFIGSEGSLG IITKVSILTP PKLASVNIAF LACEDYLSCQ 300 KLLLEAKRNL GEILSAFEFL DSVAMDVVLN NLDGARNPLA PSKHNFYVLI ETTGSEESYD 360 TEKIEKFLLG SMESGLVSDG VLAQDINQAS AFWHLREGIP ESLQRAGAVY KYDLSLPVEK 420 MYDIVEEMRE RLGDSVKVVG YGHLGDGNLH LNVSALKYDD AILAQIEPFV YEWTSKHHGS 480 ISAEHGVGLM KANKIFYSKS HETLKVTIPG PPGECSLIFP SLSHSWKNAK ATNQTNK* 540 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02805 | PLN02805 | 3.0e-35 | 109 | 491 | 396 | + D-lactate dehydrogenase [cytochrome] | ||
| pfam01565 | FAD_binding_4 | 3.0e-36 | 108 | 244 | 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. | ||
| pfam02913 | FAD-oxidase_C | 5.0e-46 | 282 | 506 | 233 | + FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. | ||
| TIGR00387 | glcD | 1.0e-64 | 111 | 504 | 415 | + 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 | 4.0e-96 | 79 | 494 | 427 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| Gene Ontology | |
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| 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 | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI17437.1 | 0 | 100 | 506 | 1 | 407 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_568003.2 | 0 | 79 | 504 | 106 | 530 | FAD linked oxidase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002268002.1 | 0 | 10 | 506 | 28 | 524 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002310828.1 | 0 | 3 | 506 | 2 | 502 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002521506.1 | 0 | 45 | 506 | 78 | 538 | d-lactate dehydrognease 2, 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 | 3pm9_F | 0 | 65 | 506 | 9 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_E | 0 | 65 | 506 | 9 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_D | 0 | 65 | 506 | 9 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_C | 0 | 65 | 506 | 9 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_B | 0 | 65 | 506 | 9 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| GO838775 | 330 | 113 | 442 | 0 |
| GO839525 | 331 | 102 | 432 | 0 |
| CO071363 | 284 | 95 | 378 | 0 |
| CO071824 | 285 | 95 | 379 | 0 |
| EH723789 | 265 | 210 | 474 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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