NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|569008022|ref|XP_006527501|]
View 

acyl-CoA (8-3)-desaturase isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 40-291 1.01e-61

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: 195.17  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  40 ILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPLFFA 119
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 120 LGKVLpvelGREKKKHMPYNHQHKYFFLIGPPALLplyfqwyifYFVvqrkkwvdlawmlsfyarifftympllglkgfl 199
Cdd:cd03506   80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL---------AFL--------------------------------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 200 glffIVRFLESNWFVWVTQMNHIPMHIDH---DRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEHHLFPTMPRHNYH 276
Cdd:cd03506  114 ----VVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189

                        250
                 ....*....|....*
gi 569008022 277 KVAPLVQSLCAKYGI 291
Cdd:cd03506  190 KVAPLVRELCKKHGL 204
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 40-291 1.01e-61

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: 195.17  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  40 ILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPLFFA 119
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 120 LGKVLpvelGREKKKHMPYNHQHKYFFLIGPPALLplyfqwyifYFVvqrkkwvdlawmlsfyarifftympllglkgfl 199
Cdd:cd03506   80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL---------AFL--------------------------------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 200 glffIVRFLESNWFVWVTQMNHIPMHIDH---DRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEHHLFPTMPRHNYH 276
Cdd:cd03506  114 ----VVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189

                        250
                 ....*....|....*
gi 569008022 277 KVAPLVQSLCAKYGI 291
Cdd:cd03506  190 KVAPLVRELCKKHGL 204
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
23-314 9.51e-36

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 131.39  E-value: 9.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  23 VAAWLTLWIFGTSLVPFILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFvIGHLKGAPASWWNHMHFQHHAKP 102
Cdd:COG3239   41 LALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRL-LGLPLGTPYDAWRRSHNRHHAYT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 103 NCFRKDPDINmhplffalgkvlpvelGREKKKHMPYNHQHKY-FFLIGPPALLPLYFQWYIFYF--VVQRKKWVDLAWML 179
Cdd:COG3239  120 NDPGKDPDIG----------------YGVQAWRPLYLFQHLLrFFLLGLGGLYWLLALDFLPLRgrLELKERRLEALLLL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 180 SFYARIF--FTYMPLLGLKGFLGLFFIVRFLesnWFVWVTQMNHIPMHIDHDRNVDwvstQLQATCNVHQSAFNNWFSGH 257
Cdd:COG3239  184 LFLAALLalLLALGWWAVLLFWLLPLLVAGL---LLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGN 256

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569008022 258 LNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKESGQ 314
Cdd:COG3239  257 LNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 43-311 2.07e-30

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 120.57  E-value: 2.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  43 AVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFRK----DPDINMHPLF 117
Cdd:PLN03198 240 ACMMALCFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQLyqpiDEDIDTLPLI 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 118 FALGKVLPVELGREKKKHMPYNHqhkyffligppallpLYFQWYIFYfvvQRKKWVDLAWMLSFYAR------------I 185
Cdd:PLN03198 320 AWSKDILATVENKTFLRILQYQH---------------LFFMALLFF---ARGSWLFWSWRYTSTAKlapadrllekgtI 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 186 FFTYMpllglkgflGLFFIVRFLESNW--FVW--VTQM------------NHIPMHIdHDRNVDWVSTQLQATCNVHQSA 249
Cdd:PLN03198 382 LFHYF---------WFIGTACYLLPGWkpLVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIVSTRDIKANI 451

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569008022 250 FNNWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKE 311
Cdd:PLN03198 452 FNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 35-293 8.22e-16

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: 75.85  E-value: 8.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022   35 SLVPFILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFV---IGHLKGAPASWWNHMHFQHHAKPNCFRKDPDI 111
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  112 NMHPLFFAlgkvlpvelGREKKKHMPYNHQHKY-FFLIGPPALLPLYFQWYIFYFVVQRKKWVDLAWMLSFYARIFFTYM 190
Cdd:pfam00487  81 APLASRFR---------GLLRYLLRWLLGLLVLaWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  191 PLLGLKGFLGLFFI-VRFLESNWFVWVTQMNHIPmhidhdrnVDWVSTQLQATCNVHQ-SAFNNWFSGHLNFQIEHHLFP 268
Cdd:pfam00487 152 FLGLGGLLLLLWLLpLLVFGFLLALIFNYLEHYG--------GDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFP 223

                         250       260
                  ....*....|....*....|....*
gi 569008022  269 TMPRHNYHKVAPLVQSLCAKYGIKY 293
Cdd:pfam00487 224 GVPWYRLPKLHRRLREALPEHGLPY 248
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 40-291 1.01e-61

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: 195.17  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  40 ILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPLFFA 119
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 120 LGKVLpvelGREKKKHMPYNHQHKYFFLIGPPALLplyfqwyifYFVvqrkkwvdlawmlsfyarifftympllglkgfl 199
Cdd:cd03506   80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL---------AFL--------------------------------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 200 glffIVRFLESNWFVWVTQMNHIPMHIDH---DRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEHHLFPTMPRHNYH 276
Cdd:cd03506  114 ----VVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189

                        250
                 ....*....|....*
gi 569008022 277 KVAPLVQSLCAKYGI 291
Cdd:cd03506  190 KVAPLVRELCKKHGL 204
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
23-314 9.51e-36

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 131.39  E-value: 9.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  23 VAAWLTLWIFGTSLVPFILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFvIGHLKGAPASWWNHMHFQHHAKP 102
Cdd:COG3239   41 LALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRL-LGLPLGTPYDAWRRSHNRHHAYT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 103 NCFRKDPDINmhplffalgkvlpvelGREKKKHMPYNHQHKY-FFLIGPPALLPLYFQWYIFYF--VVQRKKWVDLAWML 179
Cdd:COG3239  120 NDPGKDPDIG----------------YGVQAWRPLYLFQHLLrFFLLGLGGLYWLLALDFLPLRgrLELKERRLEALLLL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 180 SFYARIF--FTYMPLLGLKGFLGLFFIVRFLesnWFVWVTQMNHIPMHIDHDRNVDwvstQLQATCNVHQSAFNNWFSGH 257
Cdd:COG3239  184 LFLAALLalLLALGWWAVLLFWLLPLLVAGL---LLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGN 256

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569008022 258 LNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKESGQ 314
Cdd:COG3239  257 LNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 43-311 2.07e-30

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 120.57  E-value: 2.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  43 AVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFRK----DPDINMHPLF 117
Cdd:PLN03198 240 ACMMALCFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQLyqpiDEDIDTLPLI 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 118 FALGKVLPVELGREKKKHMPYNHqhkyffligppallpLYFQWYIFYfvvQRKKWVDLAWMLSFYAR------------I 185
Cdd:PLN03198 320 AWSKDILATVENKTFLRILQYQH---------------LFFMALLFF---ARGSWLFWSWRYTSTAKlapadrllekgtI 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 186 FFTYMpllglkgflGLFFIVRFLESNW--FVW--VTQM------------NHIPMHIdHDRNVDWVSTQLQATCNVHQSA 249
Cdd:PLN03198 382 LFHYF---------WFIGTACYLLPGWkpLVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIVSTRDIKANI 451

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569008022 250 FNNWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKE 311
Cdd:PLN03198 452 FNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 1-309 2.91e-22

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 96.65  E-value: 2.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022   1 MGLMKANHLFFLVYLLHilllDVAAWLT---LWIFGTSLVPFILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHH 77
Cdd:PLN03199 124 MGMFKSNKMFYAYKCLF----NMAIWAAacaLVFYSDRFAMHIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGI 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  78 FVIGHLKGAPASWWNHMHFQHHAKPNCFRK-------DPDINMHPLF-FALGKVLPV-ELGREKK-----KHMPYNHQHK 143
Cdd:PLN03199 200 FWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqdgDPDIDTMPLLaWSLKQAQSFrEINADGKdsgfvKFAIKFQAFF 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 144 YFfligpPALLPLYFQWYIFYF-------------VVQRKK-------------WVDLAWML---SFYARIFFTYmpllg 194
Cdd:PLN03199 280 YF-----PILLLARISWLNESFkcafglgaasenaALELEAkglqypllekagiLLHYAWMFtlsSGFGRFSFAY----- 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 195 lkgflglfFIVRFLESN-----WFVWVTQMNHIPMHI-DHDRNVDWVSTQLQATCNV-----HQSAFNNWFSGHLNFQIE 263
Cdd:PLN03199 350 --------SAFYFFTATascgfFLAIVFGLGHNGMATyDADARPDFWKLQVTTTRNIigghgFPQAFVDWFCGGLQYQVD 421

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 569008022 264 HHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSL 309
Cdd:PLN03199 422 HHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHL 467
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 35-293 8.22e-16

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: 75.85  E-value: 8.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022   35 SLVPFILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFV---IGHLKGAPASWWNHMHFQHHAKPNCFRKDPDI 111
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  112 NMHPLFFAlgkvlpvelGREKKKHMPYNHQHKY-FFLIGPPALLPLYFQWYIFYFVVQRKKWVDLAWMLSFYARIFFTYM 190
Cdd:pfam00487  81 APLASRFR---------GLLRYLLRWLLGLLVLaWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  191 PLLGLKGFLGLFFI-VRFLESNWFVWVTQMNHIPmhidhdrnVDWVSTQLQATCNVHQ-SAFNNWFSGHLNFQIEHHLFP 268
Cdd:pfam00487 152 FLGLGGLLLLLWLLpLLVFGFLLALIFNYLEHYG--------GDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFP 223

                         250       260
                  ....*....|....*....|....*
gi 569008022  269 TMPRHNYHKVAPLVQSLCAKYGIKY 293
Cdd:pfam00487 224 GVPWYRLPKLHRRLREALPEHGLPY 248
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 22-276 1.53e-08

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: 54.15  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  22 DVAAWLTLWIFGTSLVPFILCAvLLSTVQAQAGW----LQHDFGHLSVFGTSTWNHLLHHfVIGHLKGAPASWWNHMHFQ 97
Cdd:cd03507   13 DILLLALLALAASLLLSWWLWP-LYWIVQGLFLTglfvLGHDCGHGSFSDNRRLNDIVGH-ILHSPLLVPYHSWRISHNR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022  98 HHAKPNCFRKdpDINMHPLffalgkvlpvelgrEKKKHMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVVqrkKWVDLAW 177
Cdd:cd03507   91 HHAHTGNLEG--DEVWVPV--------------TEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLLLNVL---LYYLIPY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008022 178 MLSfyarifftympllglkgflglffivrfleSNWFVWVTQMNHIPMHIDHDRNVDWVSTQLQATCNVHQS--AFNNWFS 255
Cdd:cd03507  152 LVV-----------------------------NAWLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDygGWLNWLT 202

                        250       260
                 ....*....|....*....|.
gi 569008022 256 GHLNFQIEHHLFPTMPrhNYH 276
Cdd:cd03507  203 HIIGTHVAHHLFPRIP--HYN 221
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 39-111 1.58e-08

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: 52.09  E-value: 1.58e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569008022  39 FILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFVIGHLkGAPASWWNHMHFQHHAKPNCFRKDPDI 111
Cdd:cd01060    1 LLLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDS 72
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH