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Conserved domains on  [gi|1010222134|ref|NP_001308471|]
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sphingolipid delta(4)-desaturase DES1 isoform 3 [Homo sapiens]

Protein Classification

sphingolipid delta(4)-desaturase family protein( domain architecture ID 10131397)

sphingolipid delta(4)-desaturase family protein such as sphingolipid delta(4)-desaturase (also called dihydroceramide desaturase) which generates a trans double bond at position 4 of sphinganine bases in sphingolipids

EC:  1.14.19.17
Gene Ontology:  GO:0046872|GO:0016020|GO:0008610|GO:0016717
PubMed:  9767077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 1-279 3.07e-166

The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the integral-membrane enzymes, dihydroceramide Delta-4 desaturase, involved in the synthesis of sphingosine; and the human membrane fatty acid (lipid) desaturase (MLD), reported to modulate biosynthesis of the epidermal growth factor receptor; and other related proteins. These proteins are found in various eukaryotes including vertebrates, higher plants, and fungi. Studies show that MLD is localized to the endoplasmic reticulum. 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, HXXHH, and 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.


:

Pssm-ID: 239585 [Multi-domain]  Cd Length: 289  Bit Score: 462.11  E-value: 3.07e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134   1 MKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGncKAMWNRWFGMFANLPI 80
Cdd:cd03508    12 FGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWNRLFGIFANLPI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  81 GIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTF 160
Cdd:cd03508    90 GVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRLEVINIVVQITF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 161 DILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPL 239
Cdd:cd03508   170 DYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHDFPYIPGTRLPK 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1010222134 240 VRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRH 279
Cdd:cd03508   250 LRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
 
Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 1-279 3.07e-166

The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the integral-membrane enzymes, dihydroceramide Delta-4 desaturase, involved in the synthesis of sphingosine; and the human membrane fatty acid (lipid) desaturase (MLD), reported to modulate biosynthesis of the epidermal growth factor receptor; and other related proteins. These proteins are found in various eukaryotes including vertebrates, higher plants, and fungi. Studies show that MLD is localized to the endoplasmic reticulum. 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, HXXHH, and 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.


Pssm-ID: 239585 [Multi-domain]  Cd Length: 289  Bit Score: 462.11  E-value: 3.07e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134   1 MKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGncKAMWNRWFGMFANLPI 80
Cdd:cd03508    12 FGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWNRLFGIFANLPI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  81 GIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTF 160
Cdd:cd03508    90 GVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRLEVINIVVQITF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 161 DILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPL 239
Cdd:cd03508   170 DYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHDFPYIPGTRLPK 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1010222134 240 VRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRH 279
Cdd:cd03508   250 LRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 1-278 1.44e-141

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 401.04  E-value: 1.44e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134   1 MKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNckAMWNRWFGMFANLPI 80
Cdd:PLN02579   41 FGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLFLAIHELSHNLAFKT--PVYNRWLGIFANLPI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  81 GIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTF 160
Cdd:PLN02579  119 GIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLFFYALRPLFVNPKPPGLWEFINLLTQIAF 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 161 DILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLV 240
Cdd:PLN02579  199 DAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKV 278

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1010222134 241 RKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKR 278
Cdd:PLN02579  279 KEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKR 316
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
1-249 1.37e-21

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 92.10  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134   1 MKPDPNLIWIIIMMVLTQLGAFYIVkdLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNckAMWNRWFGMFANLPI 80
Cdd:COG3239    26 LGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRS--RWLNDLLGRLLGLPL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  81 GIPYSIsFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFI--WVILQPLFYAFRPLFINP------KPITYLEVI 152
Cdd:COG3239   102 GTPYDA-WRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWLLALDFLPlrgrleLKERRLEAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 153 NTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHpISGHFIAEHYMFLKGHE----------TYSYYGPLNLLTFNVGY 222
Cdd:COG3239   181 LLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLL-LGLRFYLEHRGEDTGDGeyrdqllgsrNIRGGRLLRWLFGNLNY 259

                         250       260
                  ....*....|....*....|....*..
gi 1010222134 223 HNEHHDFPNIPGKSLPLVRKIAAEYYD 249
Cdd:COG3239   260 HIEHHLFPSIPWYRLPEAHRILKELCP 286
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 32-256 1.18e-15

Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme.


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 74.69  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  32 WVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNCKAM--WNRWFGMFANLPIGIPYSiSFKRYHMDHHRYLGADGVDVDIP 109
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNrwLNDLLGRLAGLPLGISYS-AWRIAHLVHHRYTNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 110 T---DFEGWF-----FCTAFRKFIWVILQPLFYAFRPLFINPKPI-------TYLEVINTVAQVTFDILIYYFLGIKSLV 174
Cdd:pfam00487  82 PlasRFRGLLryllrWLLGLLVLAWLLALVLPLWLRRLARRKRPIksrrrrwRLIAWLLLLAAWLGLWLGFLGLGGLLLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 175 YMLAASLLGLGLHPISGHFIAEHYMFLKGHE------TYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLV-RKIAAEY 247
Cdd:pfam00487 162 LWLLPLLVFGFLLALIFNYLEHYGGDWGERPvettrsIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLhRRLREAL 241


                  ....*....
gi 1010222134 248 YDNLPHYNS 256
Cdd:pfam00487 242 PEHGLPYRS 250
 
Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 1-279 3.07e-166

The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the integral-membrane enzymes, dihydroceramide Delta-4 desaturase, involved in the synthesis of sphingosine; and the human membrane fatty acid (lipid) desaturase (MLD), reported to modulate biosynthesis of the epidermal growth factor receptor; and other related proteins. These proteins are found in various eukaryotes including vertebrates, higher plants, and fungi. Studies show that MLD is localized to the endoplasmic reticulum. 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, HXXHH, and 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.


Pssm-ID: 239585 [Multi-domain]  Cd Length: 289  Bit Score: 462.11  E-value: 3.07e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134   1 MKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGncKAMWNRWFGMFANLPI 80
Cdd:cd03508    12 FGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWNRLFGIFANLPI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  81 GIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTF 160
Cdd:cd03508    90 GVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRLEVINIVVQITF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 161 DILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPL 239
Cdd:cd03508   170 DYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHDFPYIPGTRLPK 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1010222134 240 VRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRH 279
Cdd:cd03508   250 LRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 1-278 1.44e-141

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 401.04  E-value: 1.44e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134   1 MKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNckAMWNRWFGMFANLPI 80
Cdd:PLN02579   41 FGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLFLAIHELSHNLAFKT--PVYNRWLGIFANLPI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  81 GIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTF 160
Cdd:PLN02579  119 GIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLFFYALRPLFVNPKPPGLWEFINLLTQIAF 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 161 DILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLV 240
Cdd:PLN02579  199 DAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKV 278

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1010222134 241 RKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKR 278
Cdd:PLN02579  279 KEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKR 316
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
1-249 1.37e-21

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 92.10  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134   1 MKPDPNLIWIIIMMVLTQLGAFYIVkdLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNckAMWNRWFGMFANLPI 80
Cdd:COG3239    26 LGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRS--RWLNDLLGRLLGLPL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  81 GIPYSIsFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFI--WVILQPLFYAFRPLFINP------KPITYLEVI 152
Cdd:COG3239   102 GTPYDA-WRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWLLALDFLPlrgrleLKERRLEAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 153 NTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHpISGHFIAEHYMFLKGHE----------TYSYYGPLNLLTFNVGY 222
Cdd:COG3239   181 LLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLL-LGLRFYLEHRGEDTGDGeyrdqllgsrNIRGGRLLRWLFGNLNY 259

                         250       260
                  ....*....|....*....|....*..
gi 1010222134 223 HNEHHDFPNIPGKSLPLVRKIAAEYYD 249
Cdd:COG3239   260 HIEHHLFPSIPWYRLPEAHRILKELCP 286
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 32-256 1.18e-15

Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme.


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 74.69  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  32 WVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNCKAM--WNRWFGMFANLPIGIPYSiSFKRYHMDHHRYLGADGVDVDIP 109
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNrwLNDLLGRLAGLPLGISYS-AWRIAHLVHHRYTNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 110 T---DFEGWF-----FCTAFRKFIWVILQPLFYAFRPLFINPKPI-------TYLEVINTVAQVTFDILIYYFLGIKSLV 174
Cdd:pfam00487  82 PlasRFRGLLryllrWLLGLLVLAWLLALVLPLWLRRLARRKRPIksrrrrwRLIAWLLLLAAWLGLWLGFLGLGGLLLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 175 YMLAASLLGLGLHPISGHFIAEHYMFLKGHE------TYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLV-RKIAAEY 247
Cdd:pfam00487 162 LWLLPLLVFGFLLALIFNYLEHYGGDWGERPvettrsIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLhRRLREAL 241


                  ....*....
gi 1010222134 248 YDNLPHYNS 256
Cdd:pfam00487 242 PEHGLPYRS 250
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 32-112 3.64e-10

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.


Pssm-ID: 238511 [Multi-domain]  Cd Length: 122  Bit Score: 56.71  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  32 WVIFGAYAFGSCInhSMTLAIHEIAHNAAFGNckAMWNRWFGMFANLPIGIPYsISFKRYHMDHHRYLGADGVDVDIPTD 111
Cdd:cd01060     1 LLLALLLGLLGGL--GLTVLAHELGHRSFFRS--RWLNRLLGALLGLALGGSY-GWWRRSHRRHHRYTNTPGKDPDSAVN 75


                  .
gi 1010222134 112 F 112
Cdd:cd01060    76 Y 76
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 53-248 2.04e-05

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.


Pssm-ID: 239583 [Multi-domain]  Cd Length: 204  Bit Score: 44.55  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  53 HEIAHNAAFGNCKamWNRWFGMFANLPIGIPYSiSFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPL 132
Cdd:cd03506    19 HDAGHGQVFKNRW--LNKLLGLTVGNLLGASAG-WWKNKHNVHHAYTNILGHDPDIDTLPLLARSEPAFGKDQKKRFLHR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 133 FYAFrpLFInpkPITYLEVI--NTVAQVTFDILIYYFLGikslvymlaasllglglhpisGHFIAEHYmFLKGHETYSYY 210
Cdd:cd03506    96 YQHF--YFF---PLLALLLLafLVVQLAGGLWLAVVFQL---------------------NHFGMPVE-DPPGESKNDWL 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1010222134 211 -----------GP--LNLLTFNVGYHNEHHDFPNIPGKSL----PLVRKIAAEYY 248
Cdd:cd03506   149 erqvlttrnitGSpfLDWLHGGLNYQIEHHLFPTMPRHNYpkvaPLVRELCKKHG 203
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 53-233 6.76e-03

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.


Pssm-ID: 239584 [Multi-domain]  Cd Length: 222  Bit Score: 37.20  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134  53 HEIAHNAAFGNCKamWNRWFGMFANLPIGIPYSiSFKRYHMDHHRYLG-ADGVDVDIPT---DFEGWFFCTAFRKFIWVI 128
Cdd:cd03507    52 HDCGHGSFSDNRR--LNDIVGHILHSPLLVPYH-SWRISHNRHHAHTGnLEGDEVWVPVteeEYAELPKRLPYRLYRNPF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1010222134 129 LQPLFYAFRPLFINpkpitylevintvaqvtfdILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHET-- 206
Cdd:cd03507   129 LMLSLGWPYYLLLN-------------------VLLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADEWNFAQAGLLgt 189

                         170       180
                  ....*....|....*....|....*....
gi 1010222134 207 --YSYYGPLNLLTFNVGYHNEHHDFPNIP 233
Cdd:cd03507   190 vdRDYGGWLNWLTHIIGTHVAHHLFPRIP 218
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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