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Conserved domains on  [gi|578830719|ref|XP_005257281|]
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fatty acid desaturase 6 isoform X1 [Homo sapiens]

Protein Classification

fatty acid desaturase( domain architecture ID 11996742)

fatty acid desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond, such as fatty acid desaturase 6 (FADS6)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DesA super family cl34570
Fatty acid desaturase [Lipid transport and metabolism];
31-363 7.73e-13

Fatty acid desaturase [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG3239:

Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 68.60  E-value: 7.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  31 MEPARSAHRGGEALLRELEVLVQDVVRTSSWWerhgvdcAILALSLFALPAGFLCLRWENALVFASGITILGVCHYTLTV 110
Cdd:COG3239    1 MTTATPLTPADEAELRALRARLRALLGRRDWR-------YLLKLALTLALLAALWLLLSWSWLALLAALLLGLALAGLFS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 111 KGsHLATHGALTESKRWSKiWLLFFVEVCTAFTAEHATHGHVKmHHAYTNVVGLGDSSTWRLPCLNR-------YVYMFL 183
Cdd:COG3239   74 LG-HDAGHGSLFRSRWLND-LLGRLLGLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGVQAWRPlylfqhlLRFFLL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 184 APFLLPIATPLVAVERLRKVELGTALRTLALISLGLYSHYWLLLnVSGFKNPSSALGCMFLTRSLLAHpylHVNIFQHIG 263
Cdd:COG3239  151 GLGGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLG---LRFYLEHRG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 264 LPMFSrdnkPRRIHMMsLGVLNLARLPVLDWAFGHsiISCHVEHHLFPRLSDNMCLKVKPVVSQFLREKQLPYNEDSYLA 343
Cdd:COG3239  227 EDTGD----GEYRDQL-LGSRNIRGGRLLRWLFGN--LNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLR 299

                        330       340
                 ....*....|....*....|
gi 578830719 344 RFQLFLRRYEEFMAFLDPQP 363
Cdd:COG3239  300 SYREVLRLLRRLGLPARPAP 319
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
31-363 7.73e-13

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 68.60  E-value: 7.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  31 MEPARSAHRGGEALLRELEVLVQDVVRTSSWWerhgvdcAILALSLFALPAGFLCLRWENALVFASGITILGVCHYTLTV 110
Cdd:COG3239    1 MTTATPLTPADEAELRALRARLRALLGRRDWR-------YLLKLALTLALLAALWLLLSWSWLALLAALLLGLALAGLFS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 111 KGsHLATHGALTESKRWSKiWLLFFVEVCTAFTAEHATHGHVKmHHAYTNVVGLGDSSTWRLPCLNR-------YVYMFL 183
Cdd:COG3239   74 LG-HDAGHGSLFRSRWLND-LLGRLLGLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGVQAWRPlylfqhlLRFFLL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 184 APFLLPIATPLVAVERLRKVELGTALRTLALISLGLYSHYWLLLnVSGFKNPSSALGCMFLTRSLLAHpylHVNIFQHIG 263
Cdd:COG3239  151 GLGGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLG---LRFYLEHRG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 264 LPMFSrdnkPRRIHMMsLGVLNLARLPVLDWAFGHsiISCHVEHHLFPRLSDNMCLKVKPVVSQFLREKQLPYNEDSYLA 343
Cdd:COG3239  227 EDTGD----GEYRDQL-LGSRNIRGGRLLRWLFGN--LNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLR 299

                        330       340
                 ....*....|....*....|
gi 578830719 344 RFQLFLRRYEEFMAFLDPQP 363
Cdd:COG3239  300 SYREVLRLLRRLGLPARPAP 319
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 100-338 2.58e-11

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: 63.13  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  100 ILGVCHYTLTVKGSHLATHGALTESK---RWSKIWLLFFVEVCTAFTAEHATHGHVkMHHAYTNVVGlGDSSTWRLPCLN 176
Cdd:pfam00487  10 LLGLFLLGITGSLAHEASHGALFKKRrlnRWLNDLLGRLAGLPLGISYSAWRIAHL-VHHRYTNGPD-KDPDTAPLASRF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  177 RYVYMFLAPFLL--------------PIATPLVAVERLRKVELGTALRTLALISLGLYSHYWLLLNVSGFknpssALGCM 242
Cdd:pfam00487  88 RGLLRYLLRWLLgllvlawllalvlpLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGG-----LLLLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  243 FLTRSLLAHPYLHV--NIFQHIGLPMFSRDNKPRRIHMMSLGVLNlarlpvldWAFGHsiISCHVEHHLFPRLSDNMCLK 320
Cdd:pfam00487 163 WLLPLLVFGFLLALifNYLEHYGGDWGERPVETTRSIRSPNWWLN--------LLTGN--LNYHIEHHLFPGVPWYRLPK 232

                         250
                  ....*....|....*...
gi 578830719  321 VKPVVSQFLREKQLPYNE 338
Cdd:pfam00487 233 LHRRLREALPEHGLPYRS 250
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 113-331 3.01e-08

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: 53.41  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 113 SHLATHGALTESKRWSKiWLLFFVEVCTAFTAEHATHGHVKmHHAYTNVVGL-GDsstwrlpclnryvyMFLAPFLLPIA 191
Cdd:cd03506   18 AHDAGHGQVFKNRWLNK-LLGLTVGNLLGASAGWWKNKHNV-HHAYTNILGHdPD--------------IDTLPLLARSE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 192 TPLVAVERLRKvelgtalrtlalisLGLYSHYWLLLnvsgfknpssaLGCMFLTRSLLAH----PYLHVNIF-QHIGLPM 266
Cdd:cd03506   82 PAFGKDQKKRF--------------LHRYQHFYFFP-----------LLALLLLAFLVVQlaggLWLAVVFQlNHFGMPV 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830719 267 FSRDNKPRR---IHMMSLGVlNLARLPVLDWAFGHsiISCHVEHHLFPRLSDNMCLKVKPVVSQFLRE 331
Cdd:cd03506  137 EDPPGESKNdwlERQVLTTR-NITGSPFLDWLHGG--LNYQIEHHLFPTMPRHNYPKVAPLVRELCKK 201
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 214-338 5.01e-04

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 41.95  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 214 LISLGLYSHY-WLLLNVSGFKNPSSALGCMFLTRSLLAHPYLHVNIFQ--HIGLPMFSRDNKPRRIHMMSLGVLNLAR-- 288
Cdd:PLN03199 323 LEKAGILLHYaWMFTLSSGFGRFSFAYSAFYFFTATASCGFFLAIVFGlgHNGMATYDADARPDFWKLQVTTTRNIIGgh 402

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578830719 289 -LP--VLDWAFGHsiISCHVEHHLFPRLSDNMCLKVKPVVSQFLREKQLPYNE 338
Cdd:PLN03199 403 gFPqaFVDWFCGG--LQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHE 453
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
31-363 7.73e-13

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 68.60  E-value: 7.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  31 MEPARSAHRGGEALLRELEVLVQDVVRTSSWWerhgvdcAILALSLFALPAGFLCLRWENALVFASGITILGVCHYTLTV 110
Cdd:COG3239    1 MTTATPLTPADEAELRALRARLRALLGRRDWR-------YLLKLALTLALLAALWLLLSWSWLALLAALLLGLALAGLFS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 111 KGsHLATHGALTESKRWSKiWLLFFVEVCTAFTAEHATHGHVKmHHAYTNVVGLGDSSTWRLPCLNR-------YVYMFL 183
Cdd:COG3239   74 LG-HDAGHGSLFRSRWLND-LLGRLLGLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGVQAWRPlylfqhlLRFFLL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 184 APFLLPIATPLVAVERLRKVELGTALRTLALISLGLYSHYWLLLnVSGFKNPSSALGCMFLTRSLLAHpylHVNIFQHIG 263
Cdd:COG3239  151 GLGGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLG---LRFYLEHRG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 264 LPMFSrdnkPRRIHMMsLGVLNLARLPVLDWAFGHsiISCHVEHHLFPRLSDNMCLKVKPVVSQFLREKQLPYNEDSYLA 343
Cdd:COG3239  227 EDTGD----GEYRDQL-LGSRNIRGGRLLRWLFGN--LNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLR 299

                        330       340
                 ....*....|....*....|
gi 578830719 344 RFQLFLRRYEEFMAFLDPQP 363
Cdd:COG3239  300 SYREVLRLLRRLGLPARPAP 319
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 100-338 2.58e-11

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: 63.13  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  100 ILGVCHYTLTVKGSHLATHGALTESK---RWSKIWLLFFVEVCTAFTAEHATHGHVkMHHAYTNVVGlGDSSTWRLPCLN 176
Cdd:pfam00487  10 LLGLFLLGITGSLAHEASHGALFKKRrlnRWLNDLLGRLAGLPLGISYSAWRIAHL-VHHRYTNGPD-KDPDTAPLASRF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  177 RYVYMFLAPFLL--------------PIATPLVAVERLRKVELGTALRTLALISLGLYSHYWLLLNVSGFknpssALGCM 242
Cdd:pfam00487  88 RGLLRYLLRWLLgllvlawllalvlpLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGG-----LLLLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719  243 FLTRSLLAHPYLHV--NIFQHIGLPMFSRDNKPRRIHMMSLGVLNlarlpvldWAFGHsiISCHVEHHLFPRLSDNMCLK 320
Cdd:pfam00487 163 WLLPLLVFGFLLALifNYLEHYGGDWGERPVETTRSIRSPNWWLN--------LLTGN--LNYHIEHHLFPGVPWYRLPK 232

                         250
                  ....*....|....*...
gi 578830719  321 VKPVVSQFLREKQLPYNE 338
Cdd:pfam00487 233 LHRRLREALPEHGLPYRS 250
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 113-331 3.01e-08

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: 53.41  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 113 SHLATHGALTESKRWSKiWLLFFVEVCTAFTAEHATHGHVKmHHAYTNVVGL-GDsstwrlpclnryvyMFLAPFLLPIA 191
Cdd:cd03506   18 AHDAGHGQVFKNRWLNK-LLGLTVGNLLGASAGWWKNKHNV-HHAYTNILGHdPD--------------IDTLPLLARSE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 192 TPLVAVERLRKvelgtalrtlalisLGLYSHYWLLLnvsgfknpssaLGCMFLTRSLLAH----PYLHVNIF-QHIGLPM 266
Cdd:cd03506   82 PAFGKDQKKRF--------------LHRYQHFYFFP-----------LLALLLLAFLVVQlaggLWLAVVFQlNHFGMPV 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830719 267 FSRDNKPRR---IHMMSLGVlNLARLPVLDWAFGHsiISCHVEHHLFPRLSDNMCLKVKPVVSQFLRE 331
Cdd:cd03506  137 EDPPGESKNdwlERQVLTTR-NITGSPFLDWLHGG--LNYQIEHHLFPTMPRHNYPKVAPLVRELCKK 201
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 214-338 5.01e-04

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 41.95  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 214 LISLGLYSHY-WLLLNVSGFKNPSSALGCMFLTRSLLAHPYLHVNIFQ--HIGLPMFSRDNKPRRIHMMSLGVLNLAR-- 288
Cdd:PLN03199 323 LEKAGILLHYaWMFTLSSGFGRFSFAYSAFYFFTATASCGFFLAIVFGlgHNGMATYDADARPDFWKLQVTTTRNIIGgh 402

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578830719 289 -LP--VLDWAFGHsiISCHVEHHLFPRLSDNMCLKVKPVVSQFLREKQLPYNE 338
Cdd:PLN03199 403 gFPqaFVDWFCGG--LQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHE 453
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 252-311 8.77e-04

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: 38.99  E-value: 8.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830719 252 PYLHVNIFQHIGLPMFSRDNKPRRIHmmslgVLNLARLPVLDWAFGHsiISCHVEHHLFP 311
Cdd:cd01060   70 PDSAVNYLEHYGGDRPFDTDGEWLRT-----TDNSRNGWLNLLLTGG--LGYHNEHHLFP 122
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 112-163 1.49e-03

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: 38.22  E-value: 1.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578830719 112 GSHLATHGALTESKRWSKIWLLFFvEVCTAFTAEHATHGHVKmHHAYTNVVG 163
Cdd:cd01060   18 LAHELGHRSFFRSRWLNRLLGALL-GLALGGSYGWWRRSHRR-HHRYTNTPG 67
 
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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