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Conserved domains on  [gi|527498297|ref|NP_001268431|]
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acyl-CoA 6-desaturase isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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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: ...
 131-381 2.84e-64

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: 204.80  E-value: 2.84e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 131 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 210
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 211 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPpllipmyfqyqiimtmivhknwvdlawavsyyirffityipfygilGALL 290
Cdd:cd03506   80 SEPAF---GKDQKKRFLHRYQHFYFFPLLA----------------------------------------------LLLL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 291 FLNFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 367
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 527498297 368 IAPLVKSLCAKHGI 381
Cdd:cd03506  191 VAPLVRELCKKHGL 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: ...
 131-381 2.84e-64

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: 204.80  E-value: 2.84e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 131 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 210
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 211 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPpllipmyfqyqiimtmivhknwvdlawavsyyirffityipfygilGALL 290
Cdd:cd03506   80 SEPAF---GKDQKKRFLHRYQHFYFFPLLA----------------------------------------------LLLL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 291 FLNFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 367
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 527498297 368 IAPLVKSLCAKHGI 381
Cdd:cd03506  191 VAPLVRELCKKHGL 204
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
115-404 1.15e-42

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 152.19  E-value: 1.15e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 115 IAWFTVFYFGNGWI-PTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHkFVIGHLKGASANWWNHRHFQHHAKP 193
Cdd:COG3239   41 LALLAALWLLLSWSwLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLG-RLLGLPLGTPYDAWRRSHNRHHAYT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 194 NIFHKDPDvnmlHVFVLGEWQPIeygkkklkylpYNHQHEY-FFLIGPPLLIPMYFQYQIIMTM-IVHKNWVDLAWAVsy 271
Cdd:COG3239  120 NDPGKDPD----IGYGVQAWRPL-----------YLFQHLLrFFLLGLGGLYWLLALDFLPLRGrLELKERRLEALLL-- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 272 yIRFFITYIPFYGILGALLFLNFI---RFLESHWFVWVTQMNHIVMEIDQEAYRDwfssQLTATCNVEQSFFNDWFSGHL 348
Cdd:COG3239  183 -LLFLAALLALLLALGWWAVLLFWllpLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNL 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 527498297 349 NFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGK 404
Cdd:COG3239  258 NYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 39-401 5.59e-39

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 146.76  E-value: 5.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  39 DAFRAFHPDLEFvgKFLKPLLIGELAPEEPSQDhgknskITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESiAWF 118
Cdd:PLN03198 154 DAFSSFHAASTW--KILQDFYIGDVDNVEPTPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFA-ASI 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 119 TVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYrKPKWNHLVHKFVIGH-LKGASANWWNHRHFQHHAKPNIFH 197
Cdd:PLN03198 225 AIICCSKSISAVLASACMMALCFQQCGWLSHDFLHNQVF-ETRWLNEVVGYLIGNaVLGFSTGWWKEKHNLHHAAPNECD 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 198 K-----DPDVNMLHVFVLGE--WQPIEyGKKKLKYLPYNH---QHEYFFLIGPPLLIPMYFQYQIIMTMIVhknWVDLAW 267
Cdd:PLN03198 304 QlyqpiDEDIDTLPLIAWSKdiLATVE-NKTFLRILQYQHlffMALLFFARGSWLFWSWRYTSTAKLAPAD---RLLEKG 379

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 268 AVSYYIRFFITyIPFYGILG--ALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAyRDWFSSQLTATCNVEQSFFNDWFS 345
Cdd:PLN03198 380 TILFHYFWFIG-TACYLLPGwkPLVWMAVTELMCGMLLGFVFVLSHNGMEVYNKS-KEFVNAQIVSTRDIKANIFNDWFT 457

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 527498297 346 GHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKK 401
Cdd:PLN03198 458 GGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 126-387 6.71e-22

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: 93.95  E-value: 6.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  126 GWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFV---IGHLKGASANWWNHRHFQHHAKPNIFHKDPDV 202
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  203 NMLHVFVLGEWQPIeygkkkLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIvHKNWVDLAWAVsYYIRFFITYIPF 282
Cdd:pfam00487  81 APLASRFRGLLRYL------LRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSR-RRRWRLIAWLL-LLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  283 YGILGALLFLNFIRFLESHWFVwvtqmnHIVMEIDQEAYRDWFSSQLTATCNVEQ-SFFNDWFSGHLNFQIEHHLFPTMP 361
Cdd:pfam00487 153 LGLGGLLLLLWLLPLLVFGFLL------ALIFNYLEHYGGDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 527498297  362 RHNLHKIAPLVKSLCAKHGIEYQEKP 387
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 131-381 2.84e-64

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: 204.80  E-value: 2.84e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 131 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 210
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 211 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPpllipmyfqyqiimtmivhknwvdlawavsyyirffityipfygilGALL 290
Cdd:cd03506   80 SEPAF---GKDQKKRFLHRYQHFYFFPLLA----------------------------------------------LLLL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 291 FLNFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 367
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 527498297 368 IAPLVKSLCAKHGI 381
Cdd:cd03506  191 VAPLVRELCKKHGL 204
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
115-404 1.15e-42

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 152.19  E-value: 1.15e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 115 IAWFTVFYFGNGWI-PTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHkFVIGHLKGASANWWNHRHFQHHAKP 193
Cdd:COG3239   41 LALLAALWLLLSWSwLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLG-RLLGLPLGTPYDAWRRSHNRHHAYT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 194 NIFHKDPDvnmlHVFVLGEWQPIeygkkklkylpYNHQHEY-FFLIGPPLLIPMYFQYQIIMTM-IVHKNWVDLAWAVsy 271
Cdd:COG3239  120 NDPGKDPD----IGYGVQAWRPL-----------YLFQHLLrFFLLGLGGLYWLLALDFLPLRGrLELKERRLEALLL-- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 272 yIRFFITYIPFYGILGALLFLNFI---RFLESHWFVWVTQMNHIVMEIDQEAYRDwfssQLTATCNVEQSFFNDWFSGHL 348
Cdd:COG3239  183 -LLFLAALLALLLALGWWAVLLFWllpLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNL 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 527498297 349 NFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGK 404
Cdd:COG3239  258 NYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 39-401 5.59e-39

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 146.76  E-value: 5.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  39 DAFRAFHPDLEFvgKFLKPLLIGELAPEEPSQDhgknskITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESiAWF 118
Cdd:PLN03198 154 DAFSSFHAASTW--KILQDFYIGDVDNVEPTPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFA-ASI 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 119 TVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYrKPKWNHLVHKFVIGH-LKGASANWWNHRHFQHHAKPNIFH 197
Cdd:PLN03198 225 AIICCSKSISAVLASACMMALCFQQCGWLSHDFLHNQVF-ETRWLNEVVGYLIGNaVLGFSTGWWKEKHNLHHAAPNECD 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 198 K-----DPDVNMLHVFVLGE--WQPIEyGKKKLKYLPYNH---QHEYFFLIGPPLLIPMYFQYQIIMTMIVhknWVDLAW 267
Cdd:PLN03198 304 QlyqpiDEDIDTLPLIAWSKdiLATVE-NKTFLRILQYQHlffMALLFFARGSWLFWSWRYTSTAKLAPAD---RLLEKG 379

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 268 AVSYYIRFFITyIPFYGILG--ALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAyRDWFSSQLTATCNVEQSFFNDWFS 345
Cdd:PLN03198 380 TILFHYFWFIG-TACYLLPGwkPLVWMAVTELMCGMLLGFVFVLSHNGMEVYNKS-KEFVNAQIVSTRDIKANIFNDWFT 457

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 527498297 346 GHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKK 401
Cdd:PLN03198 458 GGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 39-401 3.73e-38

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 143.64  E-value: 3.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  39 DAFRAFHPdlEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESIAWF 118
Cdd:PLN03199  73 DIFAAFHA--PGSQALMKKFYIGDLIPESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLFNMAIWAAACA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 119 TVFYFGNGWIpTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHK 198
Cdd:PLN03199 151 LVFYSDRFAM-HIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCS 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 199 -------DPDVNMLHVFVLGEWQPIEY------GKKK--LKYLPYNHQHEYFfligPPLLIPMY---------------- 247
Cdd:PLN03199 230 sadaqdgDPDIDTMPLLAWSLKQAQSFreinadGKDSgfVKFAIKFQAFFYF----PILLLARIswlnesfkcafglgaa 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 248 ------------FQYQII--MTMIVHKNWVDLA------WAVSYYIRFFITYIPFYGILGALLFlnfirfleshwfvwvt 307
Cdd:PLN03199 306 senaaleleakgLQYPLLekAGILLHYAWMFTLssgfgrFSFAYSAFYFFTATASCGFFLAIVF---------------- 369

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 308 QMNHIVMEI-DQEAYRDWFSSQLTATCNVE-----QSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGI 381
Cdd:PLN03199 370 GLGHNGMATyDADARPDFWKLQVTTTRNIIgghgfPQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGV 449

                        410       420
                 ....*....|....*....|
gi 527498297 382 EYQEKPLLRALLDIIRSLKK 401
Cdd:PLN03199 450 KYHEADLVDGTMEVLHHLGK 469
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 126-387 6.71e-22

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: 93.95  E-value: 6.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  126 GWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFV---IGHLKGASANWWNHRHFQHHAKPNIFHKDPDV 202
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  203 NMLHVFVLGEWQPIeygkkkLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIvHKNWVDLAWAVsYYIRFFITYIPF 282
Cdd:pfam00487  81 APLASRFRGLLRYL------LRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSR-RRRWRLIAWLL-LLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297  283 YGILGALLFLNFIRFLESHWFVwvtqmnHIVMEIDQEAYRDWFSSQLTATCNVEQ-SFFNDWFSGHLNFQIEHHLFPTMP 361
Cdd:pfam00487 153 LGLGGLLLLLWLLPLLVFGFLL------ALIFNYLEHYGGDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 527498297  362 RHNLHKIAPLVKSLCAKHGIEYQEKP 387
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 131-206 3.02e-09

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: 54.78  E-value: 3.02e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527498297 131 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLkGASANWWNHRHFQHHAKPNIFHKDPD--VNMLH 206
Cdd:cd01060    2 LLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDsaVNYLE 78
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 115-365 6.97e-07

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: 49.92  E-value: 6.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 115 IAWFTVFYFGNGWIPTLITAFVLATSQAQAGW----LQHDYGHLSVYRKPKWNHLVhkfviGHLKGASA----NWWNHRH 186
Cdd:cd03507   14 ILLLALLALAASLLLSWWLWPLYWIVQGLFLTglfvLGHDCGHGSFSDNRRLNDIV-----GHILHSPLlvpyHSWRISH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 187 FQHHAKPNifHKDPDVnmlhvfvlgEWQPIEygkkKLKYLPYNHQHEYFFLIGPPLLIPmyfqyqiimtmivhknwvdLA 266
Cdd:cd03507   89 NRHHAHTG--NLEGDE---------VWVPVT----EEEYAELPKRLPYRLYRNPFLMLS-------------------LG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 267 WAVSYYIRFFITYipfygiLGALLFLNFirfleshWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSF--FNDWF 344
Cdd:cd03507  135 WPYYLLLNVLLYY------LIPYLVVNA-------WLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDYggWLNWL 201

                        250       260
                 ....*....|....*....|.
gi 527498297 345 SGHLNFQIEHHLFPTMPRHNL 365
Cdd:cd03507  202 THIIGTHVAHHLFPRIPHYNL 222
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 115-208 1.05e-03

This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in Bradyrhizobium japonicum USDA110, and other related proteins. Dihydrorhizobitoxine desaturase is reported to be involved in the final step of rhizobitoxine biosynthesis. 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, 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 homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239587 [Multi-domain]  Cd Length: 175  Bit Score: 39.57  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498297 115 IAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPN 194
Cdd:cd03510    6 AAAVALALAWPNWLAYLLAVLLIGARQRALAILMHDAAHGLLFRNRRLNDFLGNWLAAVPIFQSLAAYRRSHLKHHRHLG 85

                         90
                 ....*....|....
gi 527498297 195 IfHKDPDVNMLHVF 208
Cdd:cd03510   86 T-EDDPDLALYLLL 98
 
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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