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Conserved domains on  [gi|1162555301|ref|XP_020418766|]
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palmitoyl-monogalactosyldiacylglycerol delta-7 desaturase, chloroplastic [Prunus persica]

Protein Classification

fatty acid desaturase family protein( domain architecture ID 1056)

fatty acid desaturase (FADS) family protein similar to membrane FADSs, which are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains, and to beta-carotene ketolase/oxygenases (CrtW-like) and hydroxylases (CrtR-like)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Membrane-FADS-like super family cl00615
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 9-267 9.16e-125

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.


The actual alignment was detected with superfamily member PLN02220:

Pssm-ID: 445012 [Multi-domain]  Cd Length: 299  Bit Score: 357.19  E-value: 9.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301   9 LALHCLCIFAPFHFNWPAFWVAITLYVATGLGITLSYHRSLAHRSLRLPKWLEYFFAYCGVLSLQGSPIEWVSTHRYHHQ 88
Cdd:PLN02220   40 GTVHFLCLLAPFNYKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  89 FTDTKKDPHSPIQSLWFSHMGWMLDgrRRQLEKELGGLKNVEDLRKQPFYEFLLRTNLLHSIALGGVLYAVGGFPFLVWG 168
Cdd:PLN02220  120 FTDSDRDPHSPIEGFWFSHVLWIFD--TSYIREKCGGRDNVMDLKQQWFYRFLRKTIGLHILMFWTLLYLWGGLPYLTWG 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301 169 VGVRTTFLHHATFLVNSVGHMWGNKAWNTGDMSTNNWWLAIIVFGEGWHNNHHAFEYSARHGLKWWQIDFTWYTIRFLQA 248
Cdd:PLN02220  198 VGVGGAIGYHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRFFEV 277

                         250
                  ....*....|....*....
gi 1162555301 249 IGLATDVKVPTEIQKQRKA 267
Cdd:PLN02220  278 LGLATDVKLPTEAQKRKMA 296
 
Name Accession Description Interval E-value
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
 9-267 9.16e-125

delta-9 acyl-lipid desaturase


Pssm-ID: 177866 [Multi-domain]  Cd Length: 299  Bit Score: 357.19  E-value: 9.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301   9 LALHCLCIFAPFHFNWPAFWVAITLYVATGLGITLSYHRSLAHRSLRLPKWLEYFFAYCGVLSLQGSPIEWVSTHRYHHQ 88
Cdd:PLN02220   40 GTVHFLCLLAPFNYKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  89 FTDTKKDPHSPIQSLWFSHMGWMLDgrRRQLEKELGGLKNVEDLRKQPFYEFLLRTNLLHSIALGGVLYAVGGFPFLVWG 168
Cdd:PLN02220  120 FTDSDRDPHSPIEGFWFSHVLWIFD--TSYIREKCGGRDNVMDLKQQWFYRFLRKTIGLHILMFWTLLYLWGGLPYLTWG 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301 169 VGVRTTFLHHATFLVNSVGHMWGNKAWNTGDMSTNNWWLAIIVFGEGWHNNHHAFEYSARHGLKWWQIDFTWYTIRFLQA 248
Cdd:PLN02220  198 VGVGGAIGYHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRFFEV 277

                         250
                  ....*....|....*....
gi 1162555301 249 IGLATDVKVPTEIQKQRKA 267
Cdd:PLN02220  278 LGLATDVKLPTEAQKRKMA 296
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
3-260 3.10e-109

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 441008  Cd Length: 286  Bit Score: 317.54  E-value: 3.10e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301   3 FSVVVFLALHCLCIFAPF-----HFNWPAFWVAITLYVATGLGITLSYHRSLAHRSLRLPKWLEYFFAYCGVLSLQGSPI 77
Cdd:COG1398    17 VTVLFFVLLHLLALLAAVpyagvGFSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYLLAILGALALQGGPL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  78 EWVSTHRYHHQFTDTKKDPHSP-IQSLWFSHMGWMLDGRRRQLEKelgglKNVEDLRKQPFYEFLLRTNLLHSIALGGVL 156
Cdd:COG1398    97 WWVADHRRHHRHSDTEGDPHSPkLRGFWWSHMGWMLREDPTPNDY-----RYAPDLAKDPELRWLDRYYLLLQLALGLLL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301 157 YAVGGF------PFLVWGVGVRTTFLHHATFLVNSVGHMWGNKAWNTGDMSTNNWWLAIIVFGEGWHNNHHAFEYSARHG 230
Cdd:COG1398   172 PALLGGllgggwSGLLWGGFVRTVLLHHGTWFINSLAHVWGYRPFETRDTSRNNWWLALLTFGEGWHNNHHAFPTSARHG 251

                         250       260       270
                  ....*....|....*....|....*....|
gi 1162555301 231 LKWWQIDFTWYTIRFLQAIGLATDVKVPTE 260
Cdd:COG1398   252 LRWWEIDPTWWLIRLLEKLGLAWDVRRPPA 281
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 23-256 5.05e-77

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: 231.68  E-value: 5.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  23 NWPAFWVAITLYVATGLGITLSYHRSLAHRSLRLPKWLEYFFAYCGVLSLQGSPIEWVSTHRYHHQFTDTKKDPHSPIQS 102
Cdd:cd03505     1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301 103 LWFSHMGWMldgrrrqlekelgglknvedlrkqpfyefllrtnllhsialggvlyavggfpflvwGVGVRTTFLHHATFL 182
Cdd:cd03505    81 FWFSHVGWL--------------------------------------------------------GGLLRIVLVLHATWL 104

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162555301 183 VNSVGHMWGNKAWNTGDMSTNNWWLAIIVFGEGWHNNHHAFEYSARHGLKWWQIDFTWYTIRFLQAIGLATDVK 256
Cdd:cd03505   105 VNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDLK 178
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 23-223 7.63e-10

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: 58.13  E-value: 7.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  23 NWPAFWVAITLYVATGlGITLSYHRSLAHRSL----RLPKWLEYFFAYCGVLSLQGSPIEWVSTHRYHHQFT-DTKKDPH 97
Cdd:pfam00487   1 SWLALLLALLLGLFLL-GITGSLAHEASHGALfkkrRLNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTnGPDKDPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  98 -----SPIQSLWFSHMGWMLDGRRRQLEKELGGLKNVEDLRKQPFYEFLLRTN---------LLHSIALGGVLYAVGGFP 163
Cdd:pfam00487  80 taplaSRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRwrliawlllLAAWLGLWLGFLGLGGLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162555301 164 FLVWGVGVRTTFLHHATFLvNSVGHMWGNKAW----NTGDMSTNNWWLAIIVFGEGWHNNHHAF 223
Cdd:pfam00487 160 LLLWLLPLLVFGFLLALIF-NYLEHYGGDWGErpveTTRSIRSPNWWLNLLTGNLNYHIEHHLF 222
 
Name Accession Description Interval E-value
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
 9-267 9.16e-125

delta-9 acyl-lipid desaturase


Pssm-ID: 177866 [Multi-domain]  Cd Length: 299  Bit Score: 357.19  E-value: 9.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301   9 LALHCLCIFAPFHFNWPAFWVAITLYVATGLGITLSYHRSLAHRSLRLPKWLEYFFAYCGVLSLQGSPIEWVSTHRYHHQ 88
Cdd:PLN02220   40 GTVHFLCLLAPFNYKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  89 FTDTKKDPHSPIQSLWFSHMGWMLDgrRRQLEKELGGLKNVEDLRKQPFYEFLLRTNLLHSIALGGVLYAVGGFPFLVWG 168
Cdd:PLN02220  120 FTDSDRDPHSPIEGFWFSHVLWIFD--TSYIREKCGGRDNVMDLKQQWFYRFLRKTIGLHILMFWTLLYLWGGLPYLTWG 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301 169 VGVRTTFLHHATFLVNSVGHMWGNKAWNTGDMSTNNWWLAIIVFGEGWHNNHHAFEYSARHGLKWWQIDFTWYTIRFLQA 248
Cdd:PLN02220  198 VGVGGAIGYHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRFFEV 277

                         250
                  ....*....|....*....
gi 1162555301 249 IGLATDVKVPTEIQKQRKA 267
Cdd:PLN02220  278 LGLATDVKLPTEAQKRKMA 296
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
3-260 3.10e-109

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 441008  Cd Length: 286  Bit Score: 317.54  E-value: 3.10e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301   3 FSVVVFLALHCLCIFAPF-----HFNWPAFWVAITLYVATGLGITLSYHRSLAHRSLRLPKWLEYFFAYCGVLSLQGSPI 77
Cdd:COG1398    17 VTVLFFVLLHLLALLAAVpyagvGFSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYLLAILGALALQGGPL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  78 EWVSTHRYHHQFTDTKKDPHSP-IQSLWFSHMGWMLDGRRRQLEKelgglKNVEDLRKQPFYEFLLRTNLLHSIALGGVL 156
Cdd:COG1398    97 WWVADHRRHHRHSDTEGDPHSPkLRGFWWSHMGWMLREDPTPNDY-----RYAPDLAKDPELRWLDRYYLLLQLALGLLL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301 157 YAVGGF------PFLVWGVGVRTTFLHHATFLVNSVGHMWGNKAWNTGDMSTNNWWLAIIVFGEGWHNNHHAFEYSARHG 230
Cdd:COG1398   172 PALLGGllgggwSGLLWGGFVRTVLLHHGTWFINSLAHVWGYRPFETRDTSRNNWWLALLTFGEGWHNNHHAFPTSARHG 251

                         250       260       270
                  ....*....|....*....|....*....|
gi 1162555301 231 LKWWQIDFTWYTIRFLQAIGLATDVKVPTE 260
Cdd:COG1398   252 LRWWEIDPTWWLIRLLEKLGLAWDVRRPPA 281
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 23-256 5.05e-77

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: 231.68  E-value: 5.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  23 NWPAFWVAITLYVATGLGITLSYHRSLAHRSLRLPKWLEYFFAYCGVLSLQGSPIEWVSTHRYHHQFTDTKKDPHSPIQS 102
Cdd:cd03505     1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301 103 LWFSHMGWMldgrrrqlekelgglknvedlrkqpfyefllrtnllhsialggvlyavggfpflvwGVGVRTTFLHHATFL 182
Cdd:cd03505    81 FWFSHVGWL--------------------------------------------------------GGLLRIVLVLHATWL 104

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162555301 183 VNSVGHMWGNKAWNTGDMSTNNWWLAIIVFGEGWHNNHHAFEYSARHGLKWWQIDFTWYTIRFLQAIGLATDVK 256
Cdd:cd03505   105 VNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDLK 178
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 23-223 7.63e-10

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: 58.13  E-value: 7.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  23 NWPAFWVAITLYVATGlGITLSYHRSLAHRSL----RLPKWLEYFFAYCGVLSLQGSPIEWVSTHRYHHQFT-DTKKDPH 97
Cdd:pfam00487   1 SWLALLLALLLGLFLL-GITGSLAHEASHGALfkkrRLNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTnGPDKDPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  98 -----SPIQSLWFSHMGWMLDGRRRQLEKELGGLKNVEDLRKQPFYEFLLRTN---------LLHSIALGGVLYAVGGFP 163
Cdd:pfam00487  80 taplaSRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRwrliawlllLAAWLGLWLGFLGLGGLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162555301 164 FLVWGVGVRTTFLHHATFLvNSVGHMWGNKAW----NTGDMSTNNWWLAIIVFGEGWHNNHHAF 223
Cdd:pfam00487 160 LLLWLLPLLVFGFLLALIF-NYLEHYGGDWGErpveTTRSIRSPNWWLNLLTGNLNYHIEHHLF 222
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 27-109 8.31e-10

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: 55.55  E-value: 8.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  27 FWVAITLYVATGLGITLSYHRsLAHRSLRLPKWLEYFFAYCGVLSLQGSPIEWVSTHRYHHQFTDT-KKDPHSPIqsLWF 105
Cdd:cd01060     1 LLLALLLGLLGGLGLTVLAHE-LGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTpGKDPDSAV--NYL 77


                  ....
gi 1162555301 106 SHMG 109
Cdd:cd01060    78 EHYG 81
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
7-223 2.66e-03

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 38.56  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301   7 VFLALHCLCIFAPFHFNWPAFWVAITLYVATGLGITLSY-------HRSLaHRSLRLPKWLEYFFAycgvLSLQGSPIEW 79
Cdd:COG3239    34 LLKLALTLALLAALWLLLSWSWLALLAALLLGLALAGLFslghdagHGSL-FRSRWLNDLLGRLLG----LPLGTPYDAW 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301  80 VSTHRYHHQFT-DTKKDP--------HSPIQSL--WFSHMGWMLDGRRRQLEKELGGLKNVEDLRKQPFYefLLRTNLLH 148
Cdd:COG3239   109 RRSHNRHHAYTnDPGKDPdigygvqaWRPLYLFqhLLRFFLLGLGGLYWLLALDFLPLRGRLELKERRLE--ALLLLLFL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162555301 149 SIALGGVLYAVGGFPFLVWGVGVRTTFLHhaTFLVNSVGHMW----GNKAWNTGDMSTN---NWWLAIIVFGEGWHNNHH 221
Cdd:COG3239   187 AALLALLLALGWWAVLLFWLLPLLVAGLL--LGLRFYLEHRGedtgDGEYRDQLLGSRNirgGRLLRWLFGNLNYHIEHH 264


                  ..
gi 1162555301 222 AF 223
Cdd:COG3239   265 LF 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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