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Conserved domains on  [gi|2787114989|ref|WP_370264278|]
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acyl-CoA desaturase [Limnobacter sp.]

Protein Classification

acyl-CoA desaturase( domain architecture ID 10787615)

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

EC:  1.14.19.-
Gene Ontology:  GO:0046872|GO:0016020|GO:0006633|GO:0016717|GO:0016717|GO:0006636
PubMed:  9767077|15189125

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
9-284 3.05e-124

Fatty-acid desaturase [Lipid transport and metabolism];


:

Pssm-ID: 441008  Cd Length: 286  Bit Score: 359.52  E-value: 3.05e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989   9 PVHWPAAITLYGTSLAALVLLPTYAWFNdFSAAAWGSFVVLAVLCGLSITAGYHRLWAHRTYEAHWVVRFVLMVFGTMTV 88
Cdd:COG1398    13 RINWVTVLFFVLLHLLALLAAVPYAGVG-FSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYLLAILGALAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  89 QNSILVWASGHRTHHRHVDDvDHDPYSAK-RGFWFSHMGWMLRQYPSgRDDFSNAPDLLKDPMVMFQHKHYTALALGLNF 167
Cdd:COG1398    92 QGGPLWWVADHRRHHRHSDT-EGDPHSPKlRGFWWSHMGWMLREDPT-PNDYRYAPDLAKDPELRWLDRYYLLLQLALGL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 168 TLPFILGYLLGDVWGVVLLGGLARLVWCHQTTFFINSLAHIWGRRPYTDENTARDNDLLAVFTYGEGYHNYHHLFQYDYR 247
Cdd:COG1398   170 LLPALLGGLLGGGWSGLLWGGFVRTVLLHHGTWFINSLAHVWGYRPFETRDTSRNNWWLALLTFGEGWHNNHHAFPTSAR 249

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2787114989 248 NGIKWYHIDPTKWLIAGLSVVGLTKNLKRCDKFAIEK 284
Cdd:COG1398   250 HGLRWWEIDPTWWLIRLLEKLGLAWDVRRPPAERIAA 286
 
Name Accession Description Interval E-value
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
9-284 3.05e-124

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 441008  Cd Length: 286  Bit Score: 359.52  E-value: 3.05e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989   9 PVHWPAAITLYGTSLAALVLLPTYAWFNdFSAAAWGSFVVLAVLCGLSITAGYHRLWAHRTYEAHWVVRFVLMVFGTMTV 88
Cdd:COG1398    13 RINWVTVLFFVLLHLLALLAAVPYAGVG-FSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYLLAILGALAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  89 QNSILVWASGHRTHHRHVDDvDHDPYSAK-RGFWFSHMGWMLRQYPSgRDDFSNAPDLLKDPMVMFQHKHYTALALGLNF 167
Cdd:COG1398    92 QGGPLWWVADHRRHHRHSDT-EGDPHSPKlRGFWWSHMGWMLREDPT-PNDYRYAPDLAKDPELRWLDRYYLLLQLALGL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 168 TLPFILGYLLGDVWGVVLLGGLARLVWCHQTTFFINSLAHIWGRRPYTDENTARDNDLLAVFTYGEGYHNYHHLFQYDYR 247
Cdd:COG1398   170 LLPALLGGLLGGGWSGLLWGGFVRTVLLHHGTWFINSLAHVWGYRPFETRDTSRNNWWLALLTFGEGWHNNHHAFPTSAR 249

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2787114989 248 NGIKWYHIDPTKWLIAGLSVVGLTKNLKRCDKFAIEK 284
Cdd:COG1398   250 HGLRWWEIDPTWWLIRLLEKLGLAWDVRRPPAERIAA 286
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 39-275 3.10e-74

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: 228.21  E-value: 3.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  39 SAAAWGSFVVLAVLCGLSITAGYHRLWAHRTYEAHWVVRFVLMVFGTMTVQNSILVWASGHRTHHRHVDDvDHDPYSAKR 118
Cdd:cd03505     1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDT-DGDPHSPKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 119 GFWFSHMGWMlrqypsgrddfsnapdllkdpmvmfqhkhytalalglnftlpfilgyllgdvwgvvllGGLARLVWCHQT 198
Cdd:cd03505    80 GFWFSHVGWL----------------------------------------------------------GGLLRIVLVLHA 101

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2787114989 199 TFFINSLAHIWGRRPYTDENTARDNDLLAVFTYGEGYHNYHHLFQYDYRNGIKWYHIDPTKWLIAGLSVVGLTKNLK 275
Cdd:cd03505   102 TWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDLK 178
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
 12-275 1.62e-35

delta-9 acyl-lipid desaturase


Pssm-ID: 177866 [Multi-domain]  Cd Length: 299  Bit Score: 131.85  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  12 WPAAITLYGTSLAALVLLPTYAWFNdFSAAAWGSFVVLAVLCGLSITAGYHRLWAHRTYEAHWVVRFVLMVFGTMTVQNS 91
Cdd:PLN02220   28 WTRLDVVRASAVGTVHFLCLLAPFN-YKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  92 ILVWASGHRTHHRHVDDvDHDPYSAKRGFWFSHMGWM-----LRQYPSGRDdfsNAPDLLKDPMVMFQHKHYTALALGLn 166
Cdd:PLN02220  107 PIDWVSTHRFHHQFTDS-DRDPHSPIEGFWFSHVLWIfdtsyIREKCGGRD---NVMDLKQQWFYRFLRKTIGLHILMF- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 167 FTLPFILGYLLGDVWGVVLLGGLArlvwcHQTTFFINSLAHIWGRRPYTDENTARDNDLLAVFTYGEGYHNYHHLFQYDY 246
Cdd:PLN02220  182 WTLLYLWGGLPYLTWGVGVGGAIG-----YHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSA 256

                         250       260
                  ....*....|....*....|....*....
gi 2787114989 247 RNGIKWYHIDPTKWLIAGLSVVGLTKNLK 275
Cdd:PLN02220  257 RQGLEWWQIDITWYLIRFFEVLGLATDVK 285
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 41-263 1.38e-12

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: 66.99  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  41 AAWGSFVVLAvLCGLSITAGYHRLWAHRTY-EAHWVVRFVLMVFGT---MTVQNSILVWASGHRTHHRHVDDVDHDPYSA 116
Cdd:pfam00487   3 LALLLALLLG-LFLLGITGSLAHEASHGALfKKRRLNRWLNDLLGRlagLPLGISYSAWRIAHLVHHRYTNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 117 -----KRGFWFSHMGWMLRQYpSGRDDFSNAPDLLKDPMVMFQHKHYTALALGLNFTLPFILGYLLGDVWGVVLLGGLAR 191
Cdd:pfam00487  82 plasrFRGLLRYLLRWLLGLL-VLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 192 LVWC-------HQTTFFINSLAHI---WGRRPYTDENTARD-NDLLAVFTYGEGYHNYHHLFQydyrnGIKWYHIDPTKW 260
Cdd:pfam00487 161 LLWLlpllvfgFLLALIFNYLEHYggdWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFP-----GVPWYRLPKLHR 235


                  ...
gi 2787114989 261 LIA 263
Cdd:pfam00487 236 RLR 238
 
Name Accession Description Interval E-value
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
9-284 3.05e-124

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 441008  Cd Length: 286  Bit Score: 359.52  E-value: 3.05e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989   9 PVHWPAAITLYGTSLAALVLLPTYAWFNdFSAAAWGSFVVLAVLCGLSITAGYHRLWAHRTYEAHWVVRFVLMVFGTMTV 88
Cdd:COG1398    13 RINWVTVLFFVLLHLLALLAAVPYAGVG-FSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYLLAILGALAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  89 QNSILVWASGHRTHHRHVDDvDHDPYSAK-RGFWFSHMGWMLRQYPSgRDDFSNAPDLLKDPMVMFQHKHYTALALGLNF 167
Cdd:COG1398    92 QGGPLWWVADHRRHHRHSDT-EGDPHSPKlRGFWWSHMGWMLREDPT-PNDYRYAPDLAKDPELRWLDRYYLLLQLALGL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 168 TLPFILGYLLGDVWGVVLLGGLARLVWCHQTTFFINSLAHIWGRRPYTDENTARDNDLLAVFTYGEGYHNYHHLFQYDYR 247
Cdd:COG1398   170 LLPALLGGLLGGGWSGLLWGGFVRTVLLHHGTWFINSLAHVWGYRPFETRDTSRNNWWLALLTFGEGWHNNHHAFPTSAR 249

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2787114989 248 NGIKWYHIDPTKWLIAGLSVVGLTKNLKRCDKFAIEK 284
Cdd:COG1398   250 HGLRWWEIDPTWWLIRLLEKLGLAWDVRRPPAERIAA 286
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 39-275 3.10e-74

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: 228.21  E-value: 3.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  39 SAAAWGSFVVLAVLCGLSITAGYHRLWAHRTYEAHWVVRFVLMVFGTMTVQNSILVWASGHRTHHRHVDDvDHDPYSAKR 118
Cdd:cd03505     1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDT-DGDPHSPKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 119 GFWFSHMGWMlrqypsgrddfsnapdllkdpmvmfqhkhytalalglnftlpfilgyllgdvwgvvllGGLARLVWCHQT 198
Cdd:cd03505    80 GFWFSHVGWL----------------------------------------------------------GGLLRIVLVLHA 101

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2787114989 199 TFFINSLAHIWGRRPYTDENTARDNDLLAVFTYGEGYHNYHHLFQYDYRNGIKWYHIDPTKWLIAGLSVVGLTKNLK 275
Cdd:cd03505   102 TWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDLK 178
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
 12-275 1.62e-35

delta-9 acyl-lipid desaturase


Pssm-ID: 177866 [Multi-domain]  Cd Length: 299  Bit Score: 131.85  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  12 WPAAITLYGTSLAALVLLPTYAWFNdFSAAAWGSFVVLAVLCGLSITAGYHRLWAHRTYEAHWVVRFVLMVFGTMTVQNS 91
Cdd:PLN02220   28 WTRLDVVRASAVGTVHFLCLLAPFN-YKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  92 ILVWASGHRTHHRHVDDvDHDPYSAKRGFWFSHMGWM-----LRQYPSGRDdfsNAPDLLKDPMVMFQHKHYTALALGLn 166
Cdd:PLN02220  107 PIDWVSTHRFHHQFTDS-DRDPHSPIEGFWFSHVLWIfdtsyIREKCGGRD---NVMDLKQQWFYRFLRKTIGLHILMF- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 167 FTLPFILGYLLGDVWGVVLLGGLArlvwcHQTTFFINSLAHIWGRRPYTDENTARDNDLLAVFTYGEGYHNYHHLFQYDY 246
Cdd:PLN02220  182 WTLLYLWGGLPYLTWGVGVGGAIG-----YHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSA 256

                         250       260
                  ....*....|....*....|....*....
gi 2787114989 247 RNGIKWYHIDPTKWLIAGLSVVGLTKNLK 275
Cdd:PLN02220  257 RQGLEWWQIDITWYLIRFFEVLGLATDVK 285
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 43-126 6.74e-13

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: 64.80  E-value: 6.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  43 WGSFVVLAVLCGLSITAGYHRLwAHRTY-EAHWVVRFVLMVFGTMTvQNSILVWASGHRTHHRHVDDVDHDPYSAkrGFW 121
Cdd:cd01060     1 LLLALLLGLLGGLGLTVLAHEL-GHRSFfRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDSA--VNY 76


                  ....*
gi 2787114989 122 FSHMG 126
Cdd:cd01060    77 LEHYG 81
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 41-263 1.38e-12

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: 66.99  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  41 AAWGSFVVLAvLCGLSITAGYHRLWAHRTY-EAHWVVRFVLMVFGT---MTVQNSILVWASGHRTHHRHVDDVDHDPYSA 116
Cdd:pfam00487   3 LALLLALLLG-LFLLGITGSLAHEASHGALfKKRRLNRWLNDLLGRlagLPLGISYSAWRIAHLVHHRYTNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 117 -----KRGFWFSHMGWMLRQYpSGRDDFSNAPDLLKDPMVMFQHKHYTALALGLNFTLPFILGYLLGDVWGVVLLGGLAR 191
Cdd:pfam00487  82 plasrFRGLLRYLLRWLLGLL-VLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989 192 LVWC-------HQTTFFINSLAHI---WGRRPYTDENTARD-NDLLAVFTYGEGYHNYHHLFQydyrnGIKWYHIDPTKW 260
Cdd:pfam00487 161 LLWLlpllvfgFLLALIFNYLEHYggdWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFP-----GVPWYRLPKLHR 235


                  ...
gi 2787114989 261 LIA 263
Cdd:pfam00487 236 RLR 238
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
24-242 3.88e-05

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 45.11  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  24 AALVLLPTYAWFndFSAAAWGSFVVLAVLCGLSITAGYHRLW------AHRTYEAH-WVVRFVLMVFGTMTVQNSiLVWA 96
Cdd:COG3239    33 YLLKLALTLALL--AALWLLLSWSWLALLAALLLGLALAGLFslghdaGHGSLFRSrWLNDLLGRLLGLPLGTPY-DAWR 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114989  97 SGHRTHHRHVDDVDHDP---YSAKRGFWFSHMGWMLRQYPSGRDDFS---NAPDLLKDPMVMFQHKHYTALALGLNFTLP 170
Cdd:COG3239   110 RSHNRHHAYTNDPGKDPdigYGVQAWRPLYLFQHLLRFFLLGLGGLYwllALDFLPLRGRLELKERRLEALLLLLFLAAL 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114989 171 FILGYLLGdvWGVVLLGGLARLVWCHQTTFFINSLAHIW-------GRRPYTDENTARDNDLLAVFTYGEGYHNYHHLF 242
Cdd:COG3239   190 LALLLALG--WWAVLLFWLLPLLVAGLLLGLRFYLEHRGedtgdgeYRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLF 266
 
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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