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Conserved domains on  [gi|527498295|ref|NP_001268430|]
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acyl-CoA 6-desaturase isoform 2 precursor [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: ...
 140-390 8.51e-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: 203.64  E-value: 8.51e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 140 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 219
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 220 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPpllipmyfqyqiimtmivhknwvdlawavsyyirffityipfygilGALL 299
Cdd:cd03506   80 SEPAF---GKDQKKRFLHRYQHFYFFPLLA----------------------------------------------LLLL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 300 FLNFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 376
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 527498295 377 IAPLVKSLCAKHGI 390
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: ...
 140-390 8.51e-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: 203.64  E-value: 8.51e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 140 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 219
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 220 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPpllipmyfqyqiimtmivhknwvdlawavsyyirffityipfygilGALL 299
Cdd:cd03506   80 SEPAF---GKDQKKRFLHRYQHFYFFPLLA----------------------------------------------LLLL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 300 FLNFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 376
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 527498295 377 IAPLVKSLCAKHGI 390
Cdd:cd03506  191 VAPLVRELCKKHGL 204
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
124-413 1.14e-42

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 152.19  E-value: 1.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 124 IAWFTVFYFGNGWI-PTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHkFVIGHLKGASANWWNHRHFQHHAKP 202
Cdd:COG3239   41 LALLAALWLLLSWSwLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLG-RLLGLPLGTPYDAWRRSHNRHHAYT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 203 NIFHKDPDvnmlHVFVLGEWQPIeygkkklkylpYNHQHEY-FFLIGPPLLIPMYFQYQIIMTM-IVHKNWVDLAWAVsy 280
Cdd:COG3239  120 NDPGKDPD----IGYGVQAWRPL-----------YLFQHLLrFFLLGLGGLYWLLALDFLPLRGrLELKERRLEALLL-- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 281 yIRFFITYIPFYGILGALLFLNFI---RFLESHWFVWVTQMNHIVMEIDQEAYRDwfssQLTATCNVEQSFFNDWFSGHL 357
Cdd:COG3239  183 -LLFLAALLALLLALGWWAVLLFWllpLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNL 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 527498295 358 NFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGK 413
Cdd:COG3239  258 NYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 48-410 1.95e-39

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 148.30  E-value: 1.95e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  48 DAFRAFHPDLEFvgKFLKPLLIGELAPEEPSQDhgknskITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESiAWF 127
Cdd:PLN03198 154 DAFSSFHAASTW--KILQDFYIGDVDNVEPTPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFA-ASI 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 128 TVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYrKPKWNHLVHKFVIGH-LKGASANWWNHRHFQHHAKPNIFH 206
Cdd:PLN03198 225 AIICCSKSISAVLASACMMALCFQQCGWLSHDFLHNQVF-ETRWLNEVVGYLIGNaVLGFSTGWWKEKHNLHHAAPNECD 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 207 K-----DPDVNMLHVFVLGE--WQPIEyGKKKLKYLPYNH---QHEYFFLIGPPLLIPMYFQYQIIMTMIVhknWVDLAW 276
Cdd:PLN03198 304 QlyqpiDEDIDTLPLIAWSKdiLATVE-NKTFLRILQYQHlffMALLFFARGSWLFWSWRYTSTAKLAPAD---RLLEKG 379

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 277 AVSYYIRFFITyIPFYGILG--ALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAyRDWFSSQLTATCNVEQSFFNDWFS 354
Cdd:PLN03198 380 TILFHYFWFIG-TACYLLPGwkPLVWMAVTELMCGMLLGFVFVLSHNGMEVYNKS-KEFVNAQIVSTRDIKANIFNDWFT 457

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 527498295 355 GHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKK 410
Cdd:PLN03198 458 GGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 135-396 6.89e-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: 6.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  135 GWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFV---IGHLKGASANWWNHRHFQHHAKPNIFHKDPDV 211
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  212 NMLHVFVLGEWQPIeygkkkLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIvHKNWVDLAWAVsYYIRFFITYIPF 291
Cdd:pfam00487  81 APLASRFRGLLRYL------LRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSR-RRRWRLIAWLL-LLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  292 YGILGALLFLNFIRFLESHWFVwvtqmnHIVMEIDQEAYRDWFSSQLTATCNVEQ-SFFNDWFSGHLNFQIEHHLFPTMP 370
Cdd:pfam00487 153 LGLGGLLLLLWLLPLLVFGFLL------ALIFNYLEHYGGDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 527498295  371 RHNLHKIAPLVKSLCAKHGIEYQEKP 396
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: ...
 140-390 8.51e-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: 203.64  E-value: 8.51e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 140 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 219
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 220 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPpllipmyfqyqiimtmivhknwvdlawavsyyirffityipfygilGALL 299
Cdd:cd03506   80 SEPAF---GKDQKKRFLHRYQHFYFFPLLA----------------------------------------------LLLL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 300 FLNFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 376
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 527498295 377 IAPLVKSLCAKHGI 390
Cdd:cd03506  191 VAPLVRELCKKHGL 204
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
124-413 1.14e-42

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 152.19  E-value: 1.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 124 IAWFTVFYFGNGWI-PTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHkFVIGHLKGASANWWNHRHFQHHAKP 202
Cdd:COG3239   41 LALLAALWLLLSWSwLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLG-RLLGLPLGTPYDAWRRSHNRHHAYT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 203 NIFHKDPDvnmlHVFVLGEWQPIeygkkklkylpYNHQHEY-FFLIGPPLLIPMYFQYQIIMTM-IVHKNWVDLAWAVsy 280
Cdd:COG3239  120 NDPGKDPD----IGYGVQAWRPL-----------YLFQHLLrFFLLGLGGLYWLLALDFLPLRGrLELKERRLEALLL-- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 281 yIRFFITYIPFYGILGALLFLNFI---RFLESHWFVWVTQMNHIVMEIDQEAYRDwfssQLTATCNVEQSFFNDWFSGHL 357
Cdd:COG3239  183 -LLFLAALLALLLALGWWAVLLFWllpLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNL 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 527498295 358 NFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGK 413
Cdd:COG3239  258 NYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 48-410 1.95e-39

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 148.30  E-value: 1.95e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  48 DAFRAFHPDLEFvgKFLKPLLIGELAPEEPSQDhgknskITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESiAWF 127
Cdd:PLN03198 154 DAFSSFHAASTW--KILQDFYIGDVDNVEPTPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFA-ASI 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 128 TVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYrKPKWNHLVHKFVIGH-LKGASANWWNHRHFQHHAKPNIFH 206
Cdd:PLN03198 225 AIICCSKSISAVLASACMMALCFQQCGWLSHDFLHNQVF-ETRWLNEVVGYLIGNaVLGFSTGWWKEKHNLHHAAPNECD 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 207 K-----DPDVNMLHVFVLGE--WQPIEyGKKKLKYLPYNH---QHEYFFLIGPPLLIPMYFQYQIIMTMIVhknWVDLAW 276
Cdd:PLN03198 304 QlyqpiDEDIDTLPLIAWSKdiLATVE-NKTFLRILQYQHlffMALLFFARGSWLFWSWRYTSTAKLAPAD---RLLEKG 379

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 277 AVSYYIRFFITyIPFYGILG--ALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAyRDWFSSQLTATCNVEQSFFNDWFS 354
Cdd:PLN03198 380 TILFHYFWFIG-TACYLLPGwkPLVWMAVTELMCGMLLGFVFVLSHNGMEVYNKS-KEFVNAQIVSTRDIKANIFNDWFT 457

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 527498295 355 GHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKK 410
Cdd:PLN03198 458 GGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 35-410 1.08e-38

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 145.57  E-value: 1.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  35 HPASA---GHPITGQQDAFRAFHPdlEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFF 111
Cdd:PLN03199  57 HPGGAvifTHAGDDMTDIFAAFHA--PGSQALMKKFYIGDLIPESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFY 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 112 LLLLAHIIALESIAWFTVFYFGNGWIpTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWW 191
Cdd:PLN03199 135 AYKCLFNMAIWAAACALVFYSDRFAM-HIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWW 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 192 NHRHFQHHAKPNIFHK-------DPDVNMLHVFVLGEWQPIEY------GKKK--LKYLPYNHQHEYFfligPPLLIPMY 256
Cdd:PLN03199 214 KNKHNGHHAVPNLHCSsadaqdgDPDIDTMPLLAWSLKQAQSFreinadGKDSgfVKFAIKFQAFFYF----PILLLARI 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 257 ----------------------------FQYQII--MTMIVHKNWVDLA------WAVSYYIRFFITYIPFYGILGALLF 300
Cdd:PLN03199 290 swlnesfkcafglgaasenaaleleakgLQYPLLekAGILLHYAWMFTLssgfgrFSFAYSAFYFFTATASCGFFLAIVF 369

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 301 lnfirfleshwfvwvtQMNHIVMEI-DQEAYRDWFSSQLTATCNVE-----QSFFNDWFSGHLNFQIEHHLFPTMPRHNL 374
Cdd:PLN03199 370 ----------------GLGHNGMATyDADARPDFWKLQVTTTRNIIgghgfPQAFVDWFCGGLQYQVDHHLFPMLPRHNI 433

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 527498295 375 HKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKK 410
Cdd:PLN03199 434 AKCHALVESFCKEWGVKYHEADLVDGTMEVLHHLGK 469
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 135-396 6.89e-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: 6.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  135 GWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFV---IGHLKGASANWWNHRHFQHHAKPNIFHKDPDV 211
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  212 NMLHVFVLGEWQPIeygkkkLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIvHKNWVDLAWAVsYYIRFFITYIPF 291
Cdd:pfam00487  81 APLASRFRGLLRYL------LRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSR-RRRWRLIAWLL-LLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295  292 YGILGALLFLNFIRFLESHWFVwvtqmnHIVMEIDQEAYRDWFSSQLTATCNVEQ-SFFNDWFSGHLNFQIEHHLFPTMP 370
Cdd:pfam00487 153 LGLGGLLLLLWLLPLLVFGFLL------ALIFNYLEHYGGDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 527498295  371 RHNLHKIAPLVKSLCAKHGIEYQEKP 396
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 140-215 3.10e-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: 3.10e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527498295 140 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLkGASANWWNHRHFQHHAKPNIFHKDPD--VNMLH 215
Cdd:cd01060    2 LLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDsaVNYLE 78
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 124-374 6.49e-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: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 124 IAWFTVFYFGNGWIPTLITAFVLATSQAQAGW----LQHDYGHLSVYRKPKWNHLVhkfviGHLKGASA----NWWNHRH 195
Cdd:cd03507   14 ILLLALLALAASLLLSWWLWPLYWIVQGLFLTglfvLGHDCGHGSFSDNRRLNDIV-----GHILHSPLlvpyHSWRISH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 196 FQHHAKPNifHKDPDVnmlhvfvlgEWQPIEygkkKLKYLPYNHQHEYFFLIGPPLLIPmyfqyqiimtmivhknwvdLA 275
Cdd:cd03507   89 NRHHAHTG--NLEGDE---------VWVPVT----EEEYAELPKRLPYRLYRNPFLMLS-------------------LG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 276 WAVSYYIRFFITYipfygiLGALLFLNFirfleshWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSF--FNDWF 353
Cdd:cd03507  135 WPYYLLLNVLLYY------LIPYLVVNA-------WLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDYggWLNWL 201

                        250       260
                 ....*....|....*....|.
gi 527498295 354 SGHLNFQIEHHLFPTMPRHNL 374
Cdd:cd03507  202 THIIGTHVAHHLFPRIPHYNL 222
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 124-217 1.31e-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: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498295 124 IAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPN 203
Cdd:cd03510    6 AAAVALALAWPNWLAYLLAVLLIGARQRALAILMHDAAHGLLFRNRRLNDFLGNWLAAVPIFQSLAAYRRSHLKHHRHLG 85

                         90
                 ....*....|....
gi 527498295 204 IfHKDPDVNMLHVF 217
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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