6 GO Terms
| Identifier | Name | Description |
|---|---|---|
| GO:0016491 | oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
| GO:0055114 | oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| GO:0003824 | catalytic activity | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. |
| GO:0050660 | flavin adenine dinucleotide binding | Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity | Catalysis of the reaction: UDP-N-acetylmuramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+. |
| GO:0016614 | oxidoreductase activity, acting on CH-OH group of donors | Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. |
34 Blast
12 Domain Motifs
| Analysis | Begin | End | Length | Domain Identifier | Cross Ref | Description | Inter Pro |
|---|---|---|---|---|---|---|---|
| Pfam | 71 | 207 | 137 | PF01565 | "KEGG:00520+1.3.1.98","KEGG:00550+1.3.1.98","MetaCyc:PWY-6386","MetaCyc:PWY-6387","UniPathway:UPA00219" | FAD binding domain | IPR006094 |
| Phobius | 1 | 16 | 16 | SIGNAL_PEPTIDE | none | Signal peptide region | none |
| PANTHER | 1 | 528 | 528 | PTHR32448 | none | none | none |
| ProSiteProfiles | 67 | 241 | 175 | PS51387 | none | PCMH-type FAD-binding domain profile. | IPR016166 |
| Phobius | 1 | 3 | 3 | SIGNAL_PEPTIDE_N_REGION | none | N-terminal region of a signal peptide. | none |
| Phobius | 4 | 12 | 9 | SIGNAL_PEPTIDE_H_REGION | none | Hydrophobic region of a signal peptide. | none |
| Phobius | 13 | 16 | 4 | SIGNAL_PEPTIDE_C_REGION | none | C-terminal region of a signal peptide. | none |
| Phobius | 17 | 528 | 512 | NON_CYTOPLASMIC_DOMAIN | none | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. | none |
| SUPERFAMILY | 18 | 242 | 225 | SSF56176 | none | none | IPR016166 |
| Gene3D | 128 | 242 | 115 | G3DSA:3.30.465.10 | none | none | IPR016169 |
| Pfam | 465 | 522 | 58 | PF08031 | none | Berberine and berberine like | IPR012951 |
| Gene3D | 66 | 126 | 61 | G3DSA:3.30.43.10 | none | none | IPR016167 |
3 Localization
| Analysis | Start | End | Length |
|---|---|---|---|
| SignalP_GRAM_POSITIVE | 1 | 16 | 15 |
| SignalP_EUK | 1 | 16 | 15 |
| SignalP_GRAM_NEGATIVE | 1 | 16 | 15 |
4 Qtllist
| Qtl Name | Chromosome Name | Linkage Group | Prox Marker | Dist Marker | Position QTL | Pos One | Pos Two | Test Type | Test Value | R 2 |
|---|---|---|---|---|---|---|---|---|---|---|
| Bourran1_2004_QTL5_peak_Bud_burst_A4 | Qrob_Chr10 | 10 | s_1C8OKQ_688 | v_12844_707 | 25,6 | 13,9 | 39,9 | lod | 2,7 | 6,1 |
| Bourran2_2002_QTL13_peak_Bud_burst_3P | Qrob_Chr10 | 10 | s_1B1AG7_637 | s_1A3A1N_709 | 19,44 | 0 | 49,44 | lod | 3 | 5,6 |
| Bourran2_2014_vSeqBC_A4 | Qrob_Chr10 | 10 | s_1BAM4E_1326 | s_1C0HD0_1012 | 36,88 | 7,71 | 46,03 | lod | 2,6164 | 7,3 |
| Champenoux_2015_nPriLBD_3P | Qrob_Chr10 | 10 | v_15000_157 | v_15000_310 | 15,68 | 15,9 | 15,91 | lod | 2.4 | 5.5 |
