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Conserved domains on  [gi|2188159545|ref|WP_236849194|]
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acyl-CoA desaturase [Chania multitudinisentens]

Protein Classification

fatty acid desaturase family protein( domain architecture ID 11461513)

fatty acid desaturase family protein may remove two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; such as Mycobacterium tuberculosis NADPH-dependent stearoyl-CoA 9-desaturase

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
40-362 2.85e-46

Fatty acid desaturase [Lipid transport and metabolism];


:

Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 160.28  E-value: 2.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  40 RFADGGMFAKVLVLILLCAFCYYASlrqhnGWAYFGWYAGFIFSAMMLTVNVV-HDASHNAFFKRASLNHWLNFFVSMPL 118
Cdd:COG3239    27 GRRDWRYLLKLALTLALLAALWLLL-----SWSWLALLAALLLGLALAGLFSLgHDAGHGSLFRSRWLNDLLGRLLGLPL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 119 GLDADCWRVRHVIfHHAYNNIEGYDPDIEAngvlrqtPFQRRKAFMRVQQYYWPLVAALTFPYYIWLFDWLDRAGKTRIT 198
Cdd:COG3239   102 GTPYDAWRRSHNR-HHAYTNDPGKDPDIGY-------GVQAWRPLYLFQHLLRFFLLGLGGLYWLLALDFLPLRGRLELK 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 199 PKMRlqgaqGWGMFLLSKLAHFTLALVIPLWlmspvlgitTVLLVYLLSQMLSSLVFVMLIVGTHWAkarfyqaPAVQHG 278
Cdd:COG3239   174 ERRL-----EALLLLLFLAALLALLLALGWW---------AVLLFWLLPLLVAGLLLGLRFYLEHRG-------EDTGDG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 279 WYQHVFSTTFDWQTSPqWLGYWLGGANLHLTHHLFPHWSHRHYPALARIIADVAAQYGLDYQCLDLKTLLVLQQRFLAAM 358
Cdd:COG3239   233 EYRDQLLGSRNIRGGR-LLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRL 311


                  ....
gi 2188159545 359 GRKP 362
Cdd:COG3239   312 GLPA 315
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
40-362 2.85e-46

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 160.28  E-value: 2.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  40 RFADGGMFAKVLVLILLCAFCYYASlrqhnGWAYFGWYAGFIFSAMMLTVNVV-HDASHNAFFKRASLNHWLNFFVSMPL 118
Cdd:COG3239    27 GRRDWRYLLKLALTLALLAALWLLL-----SWSWLALLAALLLGLALAGLFSLgHDAGHGSLFRSRWLNDLLGRLLGLPL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 119 GLDADCWRVRHVIfHHAYNNIEGYDPDIEAngvlrqtPFQRRKAFMRVQQYYWPLVAALTFPYYIWLFDWLDRAGKTRIT 198
Cdd:COG3239   102 GTPYDAWRRSHNR-HHAYTNDPGKDPDIGY-------GVQAWRPLYLFQHLLRFFLLGLGGLYWLLALDFLPLRGRLELK 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 199 PKMRlqgaqGWGMFLLSKLAHFTLALVIPLWlmspvlgitTVLLVYLLSQMLSSLVFVMLIVGTHWAkarfyqaPAVQHG 278
Cdd:COG3239   174 ERRL-----EALLLLLFLAALLALLLALGWW---------AVLLFWLLPLLVAGLLLGLRFYLEHRG-------EDTGDG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 279 WYQHVFSTTFDWQTSPqWLGYWLGGANLHLTHHLFPHWSHRHYPALARIIADVAAQYGLDYQCLDLKTLLVLQQRFLAAM 358
Cdd:COG3239   233 EYRDQLLGSRNIRGGR-LLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRL 311


                  ....
gi 2188159545 359 GRKP 362
Cdd:COG3239   312 GLPA 315
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 84-337 1.49e-43

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: 149.71  E-value: 1.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  84 AMMLTVNVVHDASHNAFFKRASLNHWLNFFVSMPLGLDADCWRVRHVIfHHAYNNIEGYDPDIEANGVLRQTPF-----Q 158
Cdd:cd03506    10 FWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNV-HHAYTNILGHDPDIDTLPLLARSEPafgkdQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 159 RRKAFMRVQQYYWPLVAALtfpyyiwlfdwldragktritpkmrlqgaqgwgmfllsklahftlalviplwlmspvlgit 238
Cdd:cd03506    89 KKRFLHRYQHFYFFPLLAL------------------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 239 tVLLVYLLSQMLSSLVFVMLIVGTHWAKARFYQAPAVQHGWYQHVFSTTFDWqTSPQWLGYWLGGANLHLTHHLFPHWSH 318
Cdd:cd03506   108 -LLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGESKNDWLERQVLTTRNI-TGSPFLDWLHGGLNYQIEHHLFPTMPR 185

                         250
                  ....*....|....*....
gi 2188159545 319 RHYPALARIIADVAAQYGL 337
Cdd:cd03506   186 HNYPKVAPLVRELCKKHGL 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 70-337 1.76e-18

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: 83.93  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  70 GWAYFGWYAGFIFSAMMLTVNVVHDASHNAFFKRASLNHWLN----FFVSMPLGLDADCWRVRHVIfHHAYNNIEGYDPD 145
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNdllgRLAGLPLGISYSAWRIAHLV-HHRYTNGPDKDPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 146 IeangvlrQTPFQRRKAFMRVQQYYWPLVAALTFPYYIWLFDWLDRAGKTRITPKMRLQGAQGWgmfllsklahftlalv 225
Cdd:pfam00487  80 T-------APLASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLI---------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 226 ipLWLMSPVLGITTVLLVYLLSQMLSSLVFVMLIVGTHWAKARFYQAPAVQHGWYQHVFSTTFDWQTSPQWLGYWLGGAN 305
Cdd:pfam00487 137 --AWLLLLAAWLGLWLGFLGLGGLLLLLWLLPLLVFGFLLALIFNYLEHYGGDWGERPVETTRSIRSPNWWLNLLTGNLN 214

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2188159545 306 LHLTHHLFPHWSHRHYPALARIIADVAAQYGL 337
Cdd:pfam00487 215 YHIEHHLFPGVPWYRLPKLHRRLREALPEHGL 246
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 93-346 2.17e-05

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 46.22  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  93 HDASHNAFFKRASLNHWLNFFV-SMPLGLDADCWRVRHVIFHHAYNNIEG-YDPDIEANGVLRQTPFQR-------RKAF 163
Cdd:PLN03198  255 HDFLHNQVFETRWLNEVVGYLIgNAVLGFSTGWWKEKHNLHHAAPNECDQlYQPIDEDIDTLPLIAWSKdilatveNKTF 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 164 MRVQQY-YWPLVAALTFPYYIWLFdWLDRAGKT-RITPKMRL--QGAQGWGMFLLSKLAHFTLALVIPLWLMSpvlgitt 239
Cdd:PLN03198  335 LRILQYqHLFFMALLFFARGSWLF-WSWRYTSTaKLAPADRLleKGTILFHYFWFIGTACYLLPGWKPLVWMA------- 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 240 vlLVYLLSQMLSSLVFVMLIVG--THWAKARFYQAPAVQhgwYQHVFSTTF-DWQTspqwlgywlGGANLHLTHHLFPHW 316
Cdd:PLN03198  407 --VTELMCGMLLGFVFVLSHNGmeVYNKSKEFVNAQIVS---TRDIKANIFnDWFT---------GGLNRQIEHHLFPTM 472

                         250       260       270
                  ....*....|....*....|....*....|
gi 2188159545 317 SHRHYPALARIIADVAAQYGLDYQCLDLKT 346
Cdd:PLN03198  473 PRHNLNKIAPQVEAFCIKHGLVYEDVSIAA 502
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
40-362 2.85e-46

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 160.28  E-value: 2.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  40 RFADGGMFAKVLVLILLCAFCYYASlrqhnGWAYFGWYAGFIFSAMMLTVNVV-HDASHNAFFKRASLNHWLNFFVSMPL 118
Cdd:COG3239    27 GRRDWRYLLKLALTLALLAALWLLL-----SWSWLALLAALLLGLALAGLFSLgHDAGHGSLFRSRWLNDLLGRLLGLPL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 119 GLDADCWRVRHVIfHHAYNNIEGYDPDIEAngvlrqtPFQRRKAFMRVQQYYWPLVAALTFPYYIWLFDWLDRAGKTRIT 198
Cdd:COG3239   102 GTPYDAWRRSHNR-HHAYTNDPGKDPDIGY-------GVQAWRPLYLFQHLLRFFLLGLGGLYWLLALDFLPLRGRLELK 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 199 PKMRlqgaqGWGMFLLSKLAHFTLALVIPLWlmspvlgitTVLLVYLLSQMLSSLVFVMLIVGTHWAkarfyqaPAVQHG 278
Cdd:COG3239   174 ERRL-----EALLLLLFLAALLALLLALGWW---------AVLLFWLLPLLVAGLLLGLRFYLEHRG-------EDTGDG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 279 WYQHVFSTTFDWQTSPqWLGYWLGGANLHLTHHLFPHWSHRHYPALARIIADVAAQYGLDYQCLDLKTLLVLQQRFLAAM 358
Cdd:COG3239   233 EYRDQLLGSRNIRGGR-LLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRL 311


                  ....
gi 2188159545 359 GRKP 362
Cdd:COG3239   312 GLPA 315
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 84-337 1.49e-43

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: 149.71  E-value: 1.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  84 AMMLTVNVVHDASHNAFFKRASLNHWLNFFVSMPLGLDADCWRVRHVIfHHAYNNIEGYDPDIEANGVLRQTPF-----Q 158
Cdd:cd03506    10 FWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNV-HHAYTNILGHDPDIDTLPLLARSEPafgkdQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 159 RRKAFMRVQQYYWPLVAALtfpyyiwlfdwldragktritpkmrlqgaqgwgmfllsklahftlalviplwlmspvlgit 238
Cdd:cd03506    89 KKRFLHRYQHFYFFPLLAL------------------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 239 tVLLVYLLSQMLSSLVFVMLIVGTHWAKARFYQAPAVQHGWYQHVFSTTFDWqTSPQWLGYWLGGANLHLTHHLFPHWSH 318
Cdd:cd03506   108 -LLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGESKNDWLERQVLTTRNI-TGSPFLDWLHGGLNYQIEHHLFPTMPR 185

                         250
                  ....*....|....*....
gi 2188159545 319 RHYPALARIIADVAAQYGL 337
Cdd:cd03506   186 HNYPKVAPLVRELCKKHGL 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 70-337 1.76e-18

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: 83.93  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  70 GWAYFGWYAGFIFSAMMLTVNVVHDASHNAFFKRASLNHWLN----FFVSMPLGLDADCWRVRHVIfHHAYNNIEGYDPD 145
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNdllgRLAGLPLGISYSAWRIAHLV-HHRYTNGPDKDPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 146 IeangvlrQTPFQRRKAFMRVQQYYWPLVAALTFPYYIWLFDWLDRAGKTRITPKMRLQGAQGWgmfllsklahftlalv 225
Cdd:pfam00487  80 T-------APLASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLI---------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 226 ipLWLMSPVLGITTVLLVYLLSQMLSSLVFVMLIVGTHWAKARFYQAPAVQHGWYQHVFSTTFDWQTSPQWLGYWLGGAN 305
Cdd:pfam00487 137 --AWLLLLAAWLGLWLGFLGLGGLLLLLWLLPLLVFGFLLALIFNYLEHYGGDWGERPVETTRSIRSPNWWLNLLTGNLN 214

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2188159545 306 LHLTHHLFPHWSHRHYPALARIIADVAAQYGL 337
Cdd:pfam00487 215 YHIEHHLFPGVPWYRLPKLHRRLREALPEHGL 246
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 74-179 3.77e-12

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: 62.87  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  74 FGWYAGFIFSAMMLTVNVVHDASHNAFFKRASLNHWLNFFVSMPLGLDADCWRVRHVIfHHAYNNIEGYDPDIEAN---- 149
Cdd:cd01060     1 LLLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRR-HHRYTNTPGKDPDSAVNyleh 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2188159545 150 -GVLRQTPFQRRKAFMRVQQYYWPLVAALTF 179
Cdd:cd01060    80 yGGDRPFDTDGEWLRTTDNSRNGWLNLLLTG 110
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 46-163 2.78e-07

The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the integral-membrane enzymes, dihydroceramide Delta-4 desaturase, involved in the synthesis of sphingosine; and the human membrane fatty acid (lipid) desaturase (MLD), reported to modulate biosynthesis of the epidermal growth factor receptor; and other related proteins. These proteins are found in various eukaryotes including vertebrates, higher plants, and fungi. Studies show that MLD is localized to the endoplasmic reticulum. 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, HXXHH, and 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: 239585 [Multi-domain]  Cd Length: 289  Bit Score: 51.49  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  46 MFAKVLVLILLCAFCYYASLRQHNGWAYFgwYAGFIFSAMMLtvnVVHDASHNAFFKRASLNHWLNFFVSMPLGLDADCW 125
Cdd:cd03508    22 VLGVVLLQIITAYLLRDSSWWKILLVAYF--FGGTINHSLFL---AIHEISHNLAFGKPLWNRLFGIFANLPIGVPYSIS 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2188159545 126 RVRHVIFHHAYNNIEGYDPDI--EANGVLRQTPFqrRKAF 163
Cdd:cd03508    97 FKKYHLEHHRYLGEDGLDTDIptEFEGKLFSTVL--GKAI 134
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 93-346 2.17e-05

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 46.22  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  93 HDASHNAFFKRASLNHWLNFFV-SMPLGLDADCWRVRHVIFHHAYNNIEG-YDPDIEANGVLRQTPFQR-------RKAF 163
Cdd:PLN03198  255 HDFLHNQVFETRWLNEVVGYLIgNAVLGFSTGWWKEKHNLHHAAPNECDQlYQPIDEDIDTLPLIAWSKdilatveNKTF 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 164 MRVQQY-YWPLVAALTFPYYIWLFdWLDRAGKT-RITPKMRL--QGAQGWGMFLLSKLAHFTLALVIPLWLMSpvlgitt 239
Cdd:PLN03198  335 LRILQYqHLFFMALLFFARGSWLF-WSWRYTSTaKLAPADRLleKGTILFHYFWFIGTACYLLPGWKPLVWMA------- 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545 240 vlLVYLLSQMLSSLVFVMLIVG--THWAKARFYQAPAVQhgwYQHVFSTTF-DWQTspqwlgywlGGANLHLTHHLFPHW 316
Cdd:PLN03198  407 --VTELMCGMLLGFVFVLSHNGmeVYNKSKEFVNAQIVS---TRDIKANIFnDWFT---------GGLNRQIEHHLFPTM 472

                         250       260       270
                  ....*....|....*....|....*....|
gi 2188159545 317 SHRHYPALARIIADVAAQYGLDYQCLDLKT 346
Cdd:PLN03198  473 PRHNLNKIAPQVEAFCIKHGLVYEDVSIAA 502
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 50-138 4.99e-05

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: 44.14  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  50 VLVLILLCAFCYYA--SLRQHNGWAYFGWYAGFIFSAMMLtvnVVHDASHNAFFKRASLNHWLNFFVSMPLGLDADCWRV 127
Cdd:cd03507    10 LAPDILLLALLALAasLLLSWWLWPLYWIVQGLFLTGLFV---LGHDCGHGSFSDNRRLNDIVGHILHSPLLVPYHSWRI 86

                          90
                  ....*....|.
gi 2188159545 128 RHViFHHAYNN 138
Cdd:cd03507    87 SHN-RHHAHTG 96
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 50-146 7.69e-05

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 43.96  E-value: 7.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188159545  50 VLVLILLCAfcyyASLRQHNGW------AYFgwYAGFIFSAMMLTVnvvHDASHNAFFKRASLNHWLNFFVSMPLGLDAD 123
Cdd:PLN02579   53 AVVLLQLCT----ATLLHDAGWpkillvAYF--FGGFLNHNLFLAI---HELSHNLAFKTPVYNRWLGIFANLPIGIPMS 123

                          90       100
                  ....*....|....*....|...
gi 2188159545 124 CWRVRHVIFHHAYNNIEGYDPDI 146
Cdd:PLN02579  124 VTFQKYHLEHHRFQGVDGIDMDI 146
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 90-146 8.94e-04

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: 8.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2188159545  90 NVVHDASHNAFFKRASLNHWL-NFFVSMPLGLDADCWRVRHVIfHHAYNNIEGyDPDI 146
Cdd:cd03510    37 ILMHDAAHGLLFRNRRLNDFLgNWLAAVPIFQSLAAYRRSHLK-HHRHLGTED-DPDL 92
 
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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