| Basic Information | |
|---|---|
| Species | Populus trichocarpa |
| Cazyme ID | Potri.016G064800.5 |
| Family | AA7 |
| Protein Properties | Length: 536 Molecular Weight: 59074.9 Isoelectric Point: 6.7541 |
| Chromosome | Chromosome/Scaffold: 16 Start: 4560132 End: 4569646 |
| Description | FAD-linked oxidases family protein |
| 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 |
| AA7 | 145 | 340 | 5.4e-27 |
| NIPDVVVFPRSEEEVSNIVKSCDKHKVPIVPYGGATSIEGHTLSPHGGVCIDMSLMQNVKALHVEDMDVVVEPGIGWMELNEYLEPHGLFFPLDPGPGAT IGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTVKDAADV | |||
| Full Sequence |
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| Protein Sequence Length: 536 Download |
| MAFTCWVSRL RSSYSKTITN LRSSFFHRLR TRGANTTAIT SPYHFSKQNP FRFTCSNSLL 60 PITLAGSLAI HFQSPPPLCD ASLDSPSRGI GGKGSTEFVV QGSQKHLPQE LIEELKAICQ 120 DNMSMDYDER YFHGKPQHSF HKAVNIPDVV VFPRSEEEVS NIVKSCDKHK VPIVPYGGAT 180 SIEGHTLSPH GGVCIDMSLM QNVKALHVED MDVVVEPGIG WMELNEYLEP HGLFFPLDPG 240 PGATIGGMCA TRCSGSLAVR YGTMRDNVIS LKVVLPNGDV VKTASRARKS AAGYDLTRLV 300 IGSEGTLGVI TEVTLRLQKI PQHSVVAMCN FPTVKDAADV AIATMLSGIQ VSRVELMDEV 360 QVRAINIAND KNLPEFPTLM FEFIGTEAYA REQTLIVQKI ISEHRGSDFV FAEDPEAKKE 420 LWKIRKEALW ACFAMEPKYE AMISDVCVPL SHLAELISRS KKELDASPLV CTVIAHAGDG 480 NFHTVILFDP NQEDHRREAE RLNHFMVHSA LSMEGACCFL VSAISVLVGK RLWNS* 540 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam02913 | FAD-oxidase_C | 1.0e-42 | 320 | 517 | 203 | + FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. | ||
| pfam01565 | FAD_binding_4 | 3.0e-43 | 147 | 283 | 139 | + 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. | ||
| TIGR00387 | glcD | 3.0e-76 | 150 | 515 | 374 | + 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 | 3.0e-103 | 114 | 517 | 418 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| PLN02805 | PLN02805 | 0 | 9 | 517 | 512 | + D-lactate dehydrogenase [cytochrome] | ||
| 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 |
| RefSeq | NP_001142976.1 | 0 | 79 | 517 | 69 | 504 | hypothetical protein LOC100275430 [Zea mays] |
| RefSeq | NP_568170.1 | 0 | 1 | 517 | 1 | 516 | FAD linked oxidase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002267321.1 | 0 | 1 | 517 | 1 | 515 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002322755.1 | 0 | 90 | 518 | 1 | 429 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002524111.1 | 0 | 1 | 517 | 1 | 504 | d-lactate dehydrogenase, 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 | 2e-29 | 98 | 483 | 4 | 395 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_E | 2e-29 | 98 | 483 | 4 | 395 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_D | 2e-29 | 98 | 483 | 4 | 395 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_C | 2e-29 | 98 | 483 | 4 | 395 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_B | 2e-29 | 98 | 483 | 4 | 395 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| Metabolic Pathways | |||
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| Pathway Name | Reaction | EC | Protein Name |
| photorespiration | RXN-969 | EC-1.1.3 | glycolate oxidase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| EX265038 | 322 | 162 | 482 | 0 |
| CN521074 | 270 | 1 | 270 | 0 |
| DY305587 | 298 | 201 | 498 | 0 |
| EX261606 | 289 | 218 | 506 | 0 |
| DT747637 | 285 | 190 | 474 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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