Protein : Qrob_P0279720.2 Q. robur
Protein Identifier  ? Qrob_P0279720.2 Organism . Name  Quercus robur
Score  96.6 Score Type  egn
Protein Description  (M=1) 1.3.1.35 - Phosphatidylcholine desaturase. Code Enzyme  EC:1.3.1.35
Gene Prediction Quality  validated Protein length 

Sequence

Length: 383  
Kegg Orthology  K10256
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0 Synonyms

3 GO Terms

Identifier Name Description
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:0006629 lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
GO:0016717 oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced to two molecules of water.

30 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100258789 1 382 + 382 Gaps:6 100.00 376 83.78 0.0 omega-6 fatty acid desaturase endoplasmic reticulum isozyme 2-like
blastp_kegg lcl|rcu:RCOM_0503360 1 382 + 382 Gaps:1 100.00 383 80.42 0.0 omega-6 desaturase endoplasmic reticulum (EC:1.14.99.33)
blastp_kegg lcl|sot:102580407 1 382 + 382 Gaps:1 99.74 384 79.37 0.0 omega-6 fatty acid desaturase endoplasmic reticulum-like
blastp_kegg lcl|pop:POPTR_0001s04990g 1 382 + 382 none 100.00 382 79.06 0.0 POPTRDRAFT_639715 microsomal omega-6 desaturase family protein
blastp_kegg lcl|sly:101250481 1 382 + 382 Gaps:1 99.74 384 79.11 0.0 omega-6 fatty acid desaturase endoplasmic reticulum-like
blastp_kegg lcl|sot:102593159 1 382 + 382 Gaps:1 100.00 383 78.85 0.0 omega-6 fatty acid desaturase endoplasmic reticulum isozyme 2-like
blastp_kegg lcl|gmx:100805040 1 382 + 382 Gaps:1 100.00 383 80.68 0.0 omega-6 fatty acid desaturase endoplasmic reticulum isozyme 2-like
blastp_kegg lcl|tcc:TCM_040384 11 382 + 372 none 98.67 377 80.91 0.0 Microsomal oleic acid desaturase isoform 1
blastp_kegg lcl|csv:101222623 1 382 + 382 Gaps:2 100.00 382 80.63 0.0 omega-6 fatty acid desaturase endoplasmic reticulum isozyme 2-like
blastp_kegg lcl|tcc:TCM_024902 1 382 + 382 Gaps:5 100.00 383 79.37 0.0 Microsomal oleic acid desaturase
blastp_uniprot_sprot sp|P48631|FD6E2_SOYBN 1 382 + 382 Gaps:1 100.00 383 79.90 0.0 Omega-6 fatty acid desaturase endoplasmic reticulum isozyme 2 OS Glycine max GN FAD2-2 PE 2 SV 1
blastp_uniprot_sprot sp|P48630|FD6E1_SOYBN 1 381 + 381 Gaps:3 97.67 387 78.04 0.0 Omega-6 fatty acid desaturase endoplasmic reticulum isozyme 1 OS Glycine max GN FAD2-1 PE 2 SV 1
blastp_uniprot_sprot sp|P46313|FAD6E_ARATH 1 382 + 382 Gaps:1 100.00 383 73.37 0.0 Omega-6 fatty acid desaturase endoplasmic reticulum OS Arabidopsis thaliana GN FAD2 PE 2 SV 1
blastp_uniprot_sprot sp|Q39287|FAD6E_BRAJU 1 382 + 382 Gaps:2 100.00 384 73.96 0.0 Omega-6 fatty acid desaturase endoplasmic reticulum OS Brassica juncea PE 2 SV 1
blastp_uniprot_sprot sp|O81931|FAD12_CREAL 1 380 + 380 Gaps:6 99.73 375 59.89 2e-170 Delta(12) fatty acid dehydrogenase OS Crepis alpina PE 2 SV 2
blastp_uniprot_sprot sp|P59668|FAD12_MORIS 28 369 + 342 Gaps:18 89.50 400 44.13 4e-97 Delta(12) fatty acid desaturase OS Mortierella isabellina PE 2 SV 1
blastp_uniprot_sprot sp|Q9Y8H5|FAD12_MORAP 28 369 + 342 Gaps:18 89.50 400 44.13 5e-97 Delta(12) fatty acid desaturase OS Mortierella alpina PE 1 SV 2
blastp_uniprot_sprot sp|P48626|FAD3E_TOBAC 1 342 + 342 Gaps:24 86.54 379 39.33 3e-67 Omega-3 fatty acid desaturase endoplasmic reticulum OS Nicotiana tabacum GN FAD3 PE 2 SV 1
blastp_uniprot_sprot sp|P48623|FAD3E_ARATH 14 342 + 329 Gaps:34 81.61 386 41.90 7e-66 Omega-3 fatty acid desaturase endoplasmic reticulum OS Arabidopsis thaliana GN FAD3 PE 2 SV 1
blastp_uniprot_sprot sp|P48624|FAD3E_BRANA 3 342 + 340 Gaps:24 85.12 383 38.96 2e-63 Omega-3 fatty acid desaturase endoplasmic reticulum OS Brassica napus GN FAD3 PE 2 SV 1
rpsblast_cdd gnl|CDD|178121 1 382 + 382 Gaps:3 100.00 381 79.79 0.0 PLN02505 PLN02505 omega-6 fatty acid desaturase.
rpsblast_cdd gnl|CDD|178114 24 342 + 319 Gaps:24 67.78 450 39.02 1e-56 PLN02498 PLN02498 omega-3 fatty acid desaturase.
rpsblast_cdd gnl|CDD|58173 46 328 + 283 Gaps:65 100.00 222 47.75 6e-56 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..
rpsblast_cdd gnl|CDD|33051 19 342 + 324 Gaps:35 86.01 343 27.12 5e-30 COG3239 DesA Fatty acid desaturase [Lipid metabolism].
rpsblast_cdd gnl|CDD|178208 29 342 + 314 Gaps:41 69.60 421 26.62 9e-23 PLN02598 PLN02598 omega-6 fatty acid desaturase.
rpsblast_cdd gnl|CDD|201259 80 342 + 263 Gaps:20 96.81 251 25.10 3e-22 pfam00487 FA_desaturase Fatty acid desaturase.
rpsblast_cdd gnl|CDD|58177 59 329 + 271 Gaps:27 85.61 285 24.59 1e-11 cd03511 Rhizopine-oxygenase-like This CD includes the putative hydrocarbon oxygenase MocD a bacterial rhizopine (3-O-methyl-scyllo-inosamine 3-O-MSI) oxygenase and other related proteins. It has been proposed that MocD MocE (Rieske-like ferredoxin) and MocF (ferredoxin reductase) under the regulation of MocR act in concert to form a ferredoxin oxygenase system that demethylates 3-O-MSI to form scyllo-inosamine. This domain family appears to be structurally related to the membrane fatty acid desaturases and the alkane hydroxylases. They all share in common 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 HXXHH and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs stearoyl CoA desaturase and alkane hydroxylase..
rpsblast_cdd gnl|CDD|58170 82 189 + 108 Gaps:12 93.44 122 28.95 9e-11 cd01060 Membrane-FADS-like The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs alkane hydroxylases beta carotene ketolases (CrtW-like) hydroxylases (CrtR-like) and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme iron-containing oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H HXX(X)HH and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase..
rpsblast_cdd gnl|CDD|58172 80 342 + 263 Gaps:68 98.53 204 24.38 2e-07 cd03506 Delta6-FADS-like The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4 delta-5 delta-6 delta-8 delta-8-sphingolipid and delta-11 desaturases found in vertebrates higher plants fungi and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs) which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria plants and fish the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid plant endoplasmic reticulum (ER) and plastid and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. 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 the residues: HXXXH HXX(X)HH and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog stearoyl CoA desaturase..
rpsblast_kog gnl|CDD|39433 61 359 + 299 Gaps:30 67.67 430 21.31 3e-08 KOG4232 KOG4232 KOG4232 Delta 6-fatty acid desaturase/delta-8 sphingolipid desaturase [Lipid transport and metabolism].

17 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 272 382 111 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
Phobius 87 104 18 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 176 195 20 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 242 246 5 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 76 86 11 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
PANTHER 11 381 371 PTHR32100:SF0 none none none
Phobius 137 175 39 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Pfam 82 342 261 PF00487 none Fatty acid desaturase IPR005804
Phobius 54 75 22 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Pfam 21 61 41 PF11960 "UniPathway:UPA00658" Domain of unknown function (DUF3474) IPR021863
PANTHER 11 381 371 PTHR32100 none none none
Phobius 247 271 25 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 196 221 26 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
Phobius 105 115 11 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
Phobius 116 136 21 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 222 241 20 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 1 53 53 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none

5 Localization

Analysis Start End Length
TMHMM 222 244 22
TMHMM 54 76 22
TMHMM 249 271 22
TMHMM 173 195 22
TMHMM 81 103 22

9 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_QTL1_peak_Bud_burst_A4 Qrob_Chr01 1 s_1AMVCC_444 s_1BE1VC_321 4 0 31 lod 3,2 7,4
Bourran2_2003_QTL8_peak_Bud_burst_A4 Qrob_Chr01 1 s_1AH7I_610 s_1BE1VC_321 4,6 0 28 lod 3,5 7,4
Bourran2_2007_QTL6_peak_Bud_burst_3P Qrob_Chr01 1 s_1BE1VC_321 s_1A5JRZ_890 5 0 25 lod 2,4 6
Bourran2_2014_nEpiBC_3P Qrob_Chr01 1 v_1588_550 s_1AZJRA_1600 30,48 9,48 43,98 lod 2,3642 6,3
Bourran2_2014_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran2_2015_rEpiBC_3P Qrob_Chr08 8 s_A9TNV_543 v_11837_70 9,93 9,83 11,15 lod 3.3 7.3
Bourran2_2014_nSeqBC*_A4 Qrob_Chr01 1 s_1CFE4C_2114 s_1BDNCB_819 15,25 2 28,5 lod 2,9903 8,3

0 Targeting