| Analysis | rpsblast_cdd | Start | 52 |
| End | 172 | Strand | + |
| Length | 121 | Note | Gaps:16 |
| Hit Coverage | 47.30 | Hit Length | 222 |
| Hit Pident | 36.19 | E Val | 4e-11 |
| Hit Description | cd03507 Delta12-FADS-like The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes delta-12 acyl-lipid desaturases oleate 12-hydroxylases omega3 and omega6 fatty acid desaturases and other related proteins found in a wide range of organisms including higher plants green algae diatoms nematodes fungi and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase cytochrome b and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6) omega-3 desaturase (FAD8) omega-6 desaturase (FAD6)) as well as the cyanobacterial thylakoid-bound FADSs require oxygen ferredoxin and ferredoxin oxidoreductase for activity. As in higher plants the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3) respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four and carbons six and seven respectively from the methyl end of fatty acids. As with other members of this superfamily this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH HXX(X)HH and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homologue stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity.. | Hit Pcons | 15.24 |
| Name | Qrob_P0430920.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0430920.2 | Quercus robur | 0.0 | egn | (M=3) PF11960 - Domain of unknown function (DUF3474) | validated |
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