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Conserved domains on  [gi|1931206188|ref|XP_030033583|]
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acyl-CoA Delta(11) desaturase [Manduca sexta]

Protein Classification

acyl-CoA desaturase( domain architecture ID 10131286)

acyl-CoA desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; similar to acyl-CoA delta(9) desaturase and acyl-CoA delta(11) desaturase

EC:  1.14.19.-
Gene Ontology:  GO:0046872|GO:0016020|GO:0006633|GO:0016717
PubMed:  9767077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 60-300 1.22e-73

The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. 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: HXXXXH, HXXHH, and H/QXXHH. These 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. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.


:

Pssm-ID: 239582  Cd Length: 178  Bit Score: 224.74  E-value: 1.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  60 KWQTILAGYIFFIVGGLGITAGSHRLWSHKSFKATKPLQLILMLFQSCANQHSVAHWVRDHRLHHKYSDTDADPHNATRG 139
Cdd:cd03505     1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 140 FFYSHVGWLMVrkhpevvkrgkhidlsdiysnpylkfqndnsfwfipllsfvvptllpvicwsetisiawhvnMLRYALN 219
Cdd:cd03505    81 FWFSHVGWLGG--------------------------------------------------------------LLRIVLV 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 220 LNVTFMVNSVAHMWGYKPYDKNIAPSQSHAVSVVSLGEGYHNFHHVFPYDYRSDeLSNIRLNPTTIFIDLCAKLGLAYDL 299
Cdd:cd03505    99 LHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNG-LKWYQIDPTKWVIRLLEKLGLAWDL 177


                  .
gi 1931206188 300 K 300
Cdd:cd03505   178 K 178
 
Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 60-300 1.22e-73

The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. 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: HXXXXH, HXXHH, and H/QXXHH. These 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. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.


Pssm-ID: 239582  Cd Length: 178  Bit Score: 224.74  E-value: 1.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  60 KWQTILAGYIFFIVGGLGITAGSHRLWSHKSFKATKPLQLILMLFQSCANQHSVAHWVRDHRLHHKYSDTDADPHNATRG 139
Cdd:cd03505     1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 140 FFYSHVGWLMVrkhpevvkrgkhidlsdiysnpylkfqndnsfwfipllsfvvptllpvicwsetisiawhvnMLRYALN 219
Cdd:cd03505    81 FWFSHVGWLGG--------------------------------------------------------------LLRIVLV 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 220 LNVTFMVNSVAHMWGYKPYDKNIAPSQSHAVSVVSLGEGYHNFHHVFPYDYRSDeLSNIRLNPTTIFIDLCAKLGLAYDL 299
Cdd:cd03505    99 LHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNG-LKWYQIDPTKWVIRLLEKLGLAWDL 177


                  .
gi 1931206188 300 K 300
Cdd:cd03505   178 K 178
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
22-309 2.48e-73

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 441008  Cd Length: 286  Bit Score: 227.78  E-value: 2.48e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  22 IVPRAEPRKYKIVCRNIVVFLYYHFAGLYGF-YLCLTAAKWQTILAGYIFFIVGGLGITAGSHRLWSHKSFKATKPLQLI 100
Cdd:COG1398     3 TATPAPPEKGRINWVTVLFFVLLHLLALLAAvPYAGVGFSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 101 LMLFQSCANQHSVAHWVRDHRLHHKYSDTDADPHNA-TRGFFYSHVGWLMVRKHPEVVKRgkhiDLSDIYSNPYLKFQND 179
Cdd:COG1398    83 LAILGALALQGGPLWWVADHRRHHRHSDTEGDPHSPkLRGFWWSHMGWMLREDPTPNDYR----YAPDLAKDPELRWLDR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 180 NsFWFIPL-LSFVVPTLLPVICWSETISIAWHVnMLRYALNLNVTFMVNSVAHMWGYKPYD-----KNIAPsqshaVSVV 253
Cdd:COG1398   159 Y-YLLLQLaLGLLLPALLGGLLGGGWSGLLWGG-FVRTVLLHHGTWFINSLAHVWGYRPFEtrdtsRNNWW-----LALL 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1931206188 254 SLGEGYHNFHHVFPYDYRsdelSNIR---LNPTTIFIDLCAKLGLAYDLKRAPREIVTA 309
Cdd:COG1398   232 TFGEGWHNNHHAFPTSAR----HGLRwweIDPTWWLIRLLEKLGLAWDVRRPPAERIAA 286
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
 53-300 2.08e-29

delta-9 acyl-lipid desaturase


Pssm-ID: 177866 [Multi-domain]  Cd Length: 299  Bit Score: 114.13  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  53 YLCLTAA---KWQTILAGYIFFIVGGLGITAGSHRLWSHKSFKATKPLQLILMLFQSCANQHSVAHWVRDHRLHHKYSDT 129
Cdd:PLN02220   44 FLCLLAPfnyKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQFTDS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 130 DADPHNATRGFFYSHVGWLMVRKHPeVVKRGKHIDLSDIYSNPYLKFQNDNSFWFIPLLSFVVPTL--LPVICWSETISI 207
Cdd:PLN02220  124 DRDPHSPIEGFWFSHVLWIFDTSYI-REKCGGRDNVMDLKQQWFYRFLRKTIGLHILMFWTLLYLWggLPYLTWGVGVGG 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 208 awhvnmlryALNLNVTFMVNSVAHMWGYKPYDKNIAPSQSHAVSVVSLGEGYHNFHHVFPYDYRSDeLSNIRLNPTTIFI 287
Cdd:PLN02220  203 ---------AIGYHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQG-LEWWQIDITWYLI 272

                         250
                  ....*....|...
gi 1931206188 288 DLCAKLGLAYDLK 300
Cdd:PLN02220  273 RFFEVLGLATDVK 285
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 58-268 3.02e-07

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: 50.81  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  58 AAKWQTILAGYIFFIVGGLGITAGSHRLWShKSFKATKPLQLILMLFQSCANQHSVAHWVRDHRLHHKY-SDTDADPHNA 136
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALF-KKRRLNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYtNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 137 T-----RGFFYSHVGWLMVRKHPEVVKRGKHIDLSDIYSNPYLKFQNDNSFWFIPLLSFVVPT----LLPVICWSETISI 207
Cdd:pfam00487  82 PlasrfRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAwlglWLGFLGLGGLLLL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1931206188 208 AW-HVNMLRYALNLNVTFMVNSVAHMWGYKPY-DKNIAPSQSHAVSVVSLGEGYHNFHHVFPY 268
Cdd:pfam00487 162 LWlLPLLVFGFLLALIFNYLEHYGGDWGERPVeTTRSIRSPNWWLNLLTGNLNYHIEHHLFPG 224
 
Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 60-300 1.22e-73

The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. 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: HXXXXH, HXXHH, and H/QXXHH. These 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. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.


Pssm-ID: 239582  Cd Length: 178  Bit Score: 224.74  E-value: 1.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  60 KWQTILAGYIFFIVGGLGITAGSHRLWSHKSFKATKPLQLILMLFQSCANQHSVAHWVRDHRLHHKYSDTDADPHNATRG 139
Cdd:cd03505     1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 140 FFYSHVGWLMVrkhpevvkrgkhidlsdiysnpylkfqndnsfwfipllsfvvptllpvicwsetisiawhvnMLRYALN 219
Cdd:cd03505    81 FWFSHVGWLGG--------------------------------------------------------------LLRIVLV 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 220 LNVTFMVNSVAHMWGYKPYDKNIAPSQSHAVSVVSLGEGYHNFHHVFPYDYRSDeLSNIRLNPTTIFIDLCAKLGLAYDL 299
Cdd:cd03505    99 LHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNG-LKWYQIDPTKWVIRLLEKLGLAWDL 177


                  .
gi 1931206188 300 K 300
Cdd:cd03505   178 K 178
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
22-309 2.48e-73

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 441008  Cd Length: 286  Bit Score: 227.78  E-value: 2.48e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  22 IVPRAEPRKYKIVCRNIVVFLYYHFAGLYGF-YLCLTAAKWQTILAGYIFFIVGGLGITAGSHRLWSHKSFKATKPLQLI 100
Cdd:COG1398     3 TATPAPPEKGRINWVTVLFFVLLHLLALLAAvPYAGVGFSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 101 LMLFQSCANQHSVAHWVRDHRLHHKYSDTDADPHNA-TRGFFYSHVGWLMVRKHPEVVKRgkhiDLSDIYSNPYLKFQND 179
Cdd:COG1398    83 LAILGALALQGGPLWWVADHRRHHRHSDTEGDPHSPkLRGFWWSHMGWMLREDPTPNDYR----YAPDLAKDPELRWLDR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 180 NsFWFIPL-LSFVVPTLLPVICWSETISIAWHVnMLRYALNLNVTFMVNSVAHMWGYKPYD-----KNIAPsqshaVSVV 253
Cdd:COG1398   159 Y-YLLLQLaLGLLLPALLGGLLGGGWSGLLWGG-FVRTVLLHHGTWFINSLAHVWGYRPFEtrdtsRNNWW-----LALL 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1931206188 254 SLGEGYHNFHHVFPYDYRsdelSNIR---LNPTTIFIDLCAKLGLAYDLKRAPREIVTA 309
Cdd:COG1398   232 TFGEGWHNNHHAFPTSAR----HGLRwweIDPTWWLIRLLEKLGLAWDVRRPPAERIAA 286
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
 53-300 2.08e-29

delta-9 acyl-lipid desaturase


Pssm-ID: 177866 [Multi-domain]  Cd Length: 299  Bit Score: 114.13  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  53 YLCLTAA---KWQTILAGYIFFIVGGLGITAGSHRLWSHKSFKATKPLQLILMLFQSCANQHSVAHWVRDHRLHHKYSDT 129
Cdd:PLN02220   44 FLCLLAPfnyKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQFTDS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 130 DADPHNATRGFFYSHVGWLMVRKHPeVVKRGKHIDLSDIYSNPYLKFQNDNSFWFIPLLSFVVPTL--LPVICWSETISI 207
Cdd:PLN02220  124 DRDPHSPIEGFWFSHVLWIFDTSYI-REKCGGRDNVMDLKQQWFYRFLRKTIGLHILMFWTLLYLWggLPYLTWGVGVGG 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 208 awhvnmlryALNLNVTFMVNSVAHMWGYKPYDKNIAPSQSHAVSVVSLGEGYHNFHHVFPYDYRSDeLSNIRLNPTTIFI 287
Cdd:PLN02220  203 ---------AIGYHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQG-LEWWQIDITWYLI 272

                         250
                  ....*....|...
gi 1931206188 288 DLCAKLGLAYDLK 300
Cdd:PLN02220  273 RFFEVLGLATDVK 285
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 64-146 3.53e-11

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: 59.79  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  64 ILAGYIFFIVGGLGITAGSHRLwSHKSFKATKPLQLILMLFQSCANQHSVAHWVRDHRLHHKYSDTD-ADPHNAtrGFFY 142
Cdd:cd01060     1 LLLALLLGLLGGLGLTVLAHEL-GHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPgKDPDSA--VNYL 77


                  ....
gi 1931206188 143 SHVG 146
Cdd:cd01060    78 EHYG 81
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 58-268 3.02e-07

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: 50.81  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188  58 AAKWQTILAGYIFFIVGGLGITAGSHRLWShKSFKATKPLQLILMLFQSCANQHSVAHWVRDHRLHHKY-SDTDADPHNA 136
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALF-KKRRLNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYtNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206188 137 T-----RGFFYSHVGWLMVRKHPEVVKRGKHIDLSDIYSNPYLKFQNDNSFWFIPLLSFVVPT----LLPVICWSETISI 207
Cdd:pfam00487  82 PlasrfRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAwlglWLGFLGLGGLLLL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1931206188 208 AW-HVNMLRYALNLNVTFMVNSVAHMWGYKPY-DKNIAPSQSHAVSVVSLGEGYHNFHHVFPY 268
Cdd:pfam00487 162 LWlLPLLVFGFLLALIFNYLEHYGGDWGERPVeTTRSIRSPNWWLNLLTGNLNYHIEHHLFPG 224
 
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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