| Basic Information | |
|---|---|
| Species | Fragaria vesca |
| Cazyme ID | mrna14901.1-v1.0-hybrid |
| Family | AA4 |
| Protein Properties | Length: 838 Molecular Weight: 92936.6 Isoelectric Point: 8.6189 |
| Chromosome | Chromosome/Scaffold: 1 Start: 8203310 End: 8211339 |
| Description | FAD-linked oxidases family protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA4 | 112 | 317 | 1.2e-24 |
| ISYFKGVLGEKNVVEDEERLAIANTDWMHKYRGSSKLLLQPRTTEEVSQILKYCDSRSLAVVPQGGNTGLVGGSVPVFDEVVINMSMMNKVISFDKVSGI LVCEAGCILENMITYLDNQGFVMPLDLGAKGSCQIGGNVSTNAGGLRLVRYGSLHGTVLGLEVVLANGDVLDMLGTLRKDNTGYDLKHLFIGSEGSLGIV TKVSIL | |||
| Full Sequence |
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| Protein Sequence Length: 838 Download |
| MEKLRATGRL LRYSPKASIF DRRFSPNSGK SIHSSGSGNR HGLGKKCGDE ISRKWNVRTC 60 FGLYGSQGRN LRDCTERGVV EDLRRIEHRG FGSVAEKVQR NASFSTLNSD DISYFKGVLG 120 EKNVVEDEER LAIANTDWMH KYRGSSKLLL QPRTTEEVSQ ILKYCDSRSL AVVPQGGNTG 180 LVGGSVPVFD EVVINMSMMN KVISFDKVSG ILVCEAGCIL ENMITYLDNQ GFVMPLDLGA 240 KGSCQIGGNV STNAGGLRLV RYGSLHGTVL GLEVVLANGD VLDMLGTLRK DNTGYDLKHL 300 FIGSEGSLGI VTKVSILTPP KLFSVNVAFL ACQDYFSCQK LLVEAKRKLG EILSAFEFLD 360 SHALDLVLNH LDGVRNPLPP TIHNFYVLIE TTGSDETFDR EKLEAFLVHA MEGGLISDGA 420 IAQDINQASA FWYIREGIPE ALMKAGAVYK YDLSLPVEKM YDLVDEMRTR LGDSANVVGY 480 GHLGDGNLHL NVSTPQYDDK TLAQIEPFVY EWTSGHRGSI SAEHGLGLMK ANKIFYSKPT 540 ATVKVMASIK KMLDPKGILN PISPNEAYHQ NWKTEPERFP MDNLSFNQAG IMSPNPKLAI 600 MAARTPGKQG ESKGQVKERH VKRRRCIKVL ALSPMKGHFV KIRGVVKPWP PGPFCFLFLF 660 VNTSSHSLIS LFSLSAMTSS SAASRKILSK IACNRLQKEL LEWQVNPPAG FKHKVTDNLQ 720 RWVIEVTGAP GTLYSNETYQ LQVDFPEHYP MEAPQVIFVP PAPMHPHIYS NGHICLDILY 780 DSWSPAMTVS SICISILSML SSSTAKQRPE DNDRYVKNCR NGRSPKETRW WFHDDKV* 840 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01565 | FAD_binding_4 | 9.0e-37 | 147 | 283 | 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-38 | 112 | 561 | 472 | + D-lactate dehydrogenase [cytochrome] | ||
| pfam02913 | FAD-oxidase_C | 3.0e-57 | 324 | 561 | 246 | + FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. | ||
| TIGR00387 | glcD | 5.0e-71 | 152 | 561 | 419 | + 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 | 1.0e-106 | 114 | 561 | 459 | + 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:0016881 | acid-amino acid ligase activity |
| GO:0050660 | flavin adenine dinucleotide binding |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3pm9_F | 0 | 106 | 561 | 12 | 472 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_E | 0 | 106 | 561 | 12 | 472 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_D | 0 | 106 | 561 | 12 | 472 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_C | 0 | 106 | 561 | 12 | 472 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_B | 0 | 106 | 561 | 12 | 472 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| Hydropathy |
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| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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