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Conserved domains on  [gi|1782765788|gb|QGU86500|]
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acyl-CoA desaturase [Erwinia sorbitola]

Protein Classification

acyl-CoA desaturase( domain architecture ID 10131368)

acyl-CoA desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; similar to Rebecca salina acyl-lipid 8-desaturase

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 87-323 9.61e-39

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: 137.00  E-value: 9.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  87 NVNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVhFHHVYANIEHYDLDTEENGFFRQTPF-----QRWRPWM 161
Cdd:cd03506    16 FLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHN-VHHAYTNILGHDPDIDTLPLLARSEPafgkdQKKRFLH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 162 RWQHLYWPLIAALSLPYLawvfdwadrcgktplaqrqvmpgvrgwllfclsktlhlllvlaiplwaaeqhgiaisvvlat 241
Cdd:cd03506    95 RYQHFYFFPLLALLLLAF-------------------------------------------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 242 wLGSQMAASLLVVFLLLGTHWAEAEFYQPGAEgelPHGWYRHNFATACDWQPSPaWLGYFTGGLNLHLTHHLFPGWHHRH 321
Cdd:cd03506   113 -LVVQLAGGLWLAVVFQLNHFGMPVEDPPGES---KNDWLERQVLTTRNITGSP-FLDWLHGGLNYQIEHHLFPTMPRHN 187


                  ..
gi 1782765788 322 YP 323
Cdd:cd03506   188 YP 189
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
6-363 2.91e-38

Fatty acid desaturase [Lipid transport and metabolism];


:

Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 139.09  E-value: 2.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788   6 PPLRYPADGEQAFHQALQRAAHHYLsgsrehRFAGGREWLKAGLLLVLCVTCYLLSLLqvsSGGFVICYLLFMLMAMLLN 85
Cdd:COG3239     2 TTATPLTPADEAELRALRARLRALL------GRRDWRYLLKLALTLALLAALWLLLSW---SWLALLAALLLGLALAGLF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  86 InVNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVhFHHVYANIEHYDLDteengffRQTPFQRWRPWMRWQH 165
Cdd:COG3239    73 S-LGHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHN-RHHAYTNDPGKDPD-------IGYGVQAWRPLYLFQH 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 166 LYWPLIAALSLPYLAWVFDWADRCGKtplaqRQVMPGVRGWLLFCLSKTLHLLLVLAIPLWAaeqhgiaisvVLATWLGS 245
Cdd:COG3239   144 LLRFFLLGLGGLYWLLALDFLPLRGR-----LELKERRLEALLLLLFLAALLALLLALGWWA----------VLLFWLLP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 246 QMAASLLVVFLLLGTHWAEaefyqpgaegELPHGWYRHNFATACDWQPSPaWLGYFTGGLNLHLTHHLFPGWHHRHYPAL 325
Cdd:COG3239   209 LLVAGLLLGLRFYLEHRGE----------DTGDGEYRDQLLGSRNIRGGR-LLRWLFGNLNYHIEHHLFPSIPWYRLPEA 277

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1782765788 326 AAILARLASEHGMNYRCISYRELLRRQQAFLRRMGQPQ 363
Cdd:COG3239   278 HRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPA 315
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 87-323 9.61e-39

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: 137.00  E-value: 9.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  87 NVNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVhFHHVYANIEHYDLDTEENGFFRQTPF-----QRWRPWM 161
Cdd:cd03506    16 FLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHN-VHHAYTNILGHDPDIDTLPLLARSEPafgkdQKKRFLH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 162 RWQHLYWPLIAALSLPYLawvfdwadrcgktplaqrqvmpgvrgwllfclsktlhlllvlaiplwaaeqhgiaisvvlat 241
Cdd:cd03506    95 RYQHFYFFPLLALLLLAF-------------------------------------------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 242 wLGSQMAASLLVVFLLLGTHWAEAEFYQPGAEgelPHGWYRHNFATACDWQPSPaWLGYFTGGLNLHLTHHLFPGWHHRH 321
Cdd:cd03506   113 -LVVQLAGGLWLAVVFQLNHFGMPVEDPPGES---KNDWLERQVLTTRNITGSP-FLDWLHGGLNYQIEHHLFPTMPRHN 187


                  ..
gi 1782765788 322 YP 323
Cdd:cd03506   188 YP 189
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
6-363 2.91e-38

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 139.09  E-value: 2.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788   6 PPLRYPADGEQAFHQALQRAAHHYLsgsrehRFAGGREWLKAGLLLVLCVTCYLLSLLqvsSGGFVICYLLFMLMAMLLN 85
Cdd:COG3239     2 TTATPLTPADEAELRALRARLRALL------GRRDWRYLLKLALTLALLAALWLLLSW---SWLALLAALLLGLALAGLF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  86 InVNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVhFHHVYANIEHYDLDteengffRQTPFQRWRPWMRWQH 165
Cdd:COG3239    73 S-LGHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHN-RHHAYTNDPGKDPD-------IGYGVQAWRPLYLFQH 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 166 LYWPLIAALSLPYLAWVFDWADRCGKtplaqRQVMPGVRGWLLFCLSKTLHLLLVLAIPLWAaeqhgiaisvVLATWLGS 245
Cdd:COG3239   144 LLRFFLLGLGGLYWLLALDFLPLRGR-----LELKERRLEALLLLLFLAALLALLLALGWWA----------VLLFWLLP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 246 QMAASLLVVFLLLGTHWAEaefyqpgaegELPHGWYRHNFATACDWQPSPaWLGYFTGGLNLHLTHHLFPGWHHRHYPAL 325
Cdd:COG3239   209 LLVAGLLLGLRFYLEHRGE----------DTGDGEYRDQLLGSRNIRGGR-LLRWLFGNLNYHIEHHLFPSIPWYRLPEA 277

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1782765788 326 AAILARLASEHGMNYRCISYRELLRRQQAFLRRMGQPQ 363
Cdd:COG3239   278 HRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPA 315
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 85-344 3.52e-16

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: 77.39  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  85 NINVNHDASHGVFSRSPR----INRIISRVVTLPLGLDPDYWRVRHVHfHHVYANIEHYDLDTeengffrQTPFQRWRPW 160
Cdd:pfam00487  19 TGSLAHEASHGALFKKRRlnrwLNDLLGRLAGLPLGISYSAWRIAHLV-HHRYTNGPDKDPDT-------APLASRFRGL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 161 MRWQHLYWPLIAALSLPYLAWVFDWADRCG--KTPLAQRQVMPGVRGWLLFCLSKTLHLLLVLAIPLWAAeqhgiaisvv 238
Cdd:pfam00487  91 LRYLLRWLLGLLVLAWLLALVLPLWLRRLArrKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLL---------- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 239 lATWLGSQMAASLLVVFLLlgtHWAEaefyqpgaegELPHGWYRHNFATACDWQPSPAWLGYFTGGLNLHLTHHLFPGWH 318
Cdd:pfam00487 161 -LLWLLPLLVFGFLLALIF---NYLE----------HYGGDWGERPVETTRSIRSPNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 1782765788 319 HRHYPALAAILARLASEHGMNYRCIS 344
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
PLN02598 PLN02598
omega-6 fatty acid desaturase
 88-184 5.49e-03

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 38.65  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  88 VNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVHfHHVYANIEHYDLDTEEngfFRQTPFQRWRPWMR--WQH 165
Cdd:PLN02598  142 IGHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNT-HHAHTNKLVMDTAWQP---FRPHQFDNADPLRKamMRA 217

                          90       100
                  ....*....|....*....|
gi 1782765788 166 LYWPLIAALSLP-YLAWVFD 184
Cdd:PLN02598  218 GMGPLWWWASIGhWLFWHFD 237
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 87-323 9.61e-39

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: 137.00  E-value: 9.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  87 NVNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVhFHHVYANIEHYDLDTEENGFFRQTPF-----QRWRPWM 161
Cdd:cd03506    16 FLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHN-VHHAYTNILGHDPDIDTLPLLARSEPafgkdQKKRFLH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 162 RWQHLYWPLIAALSLPYLawvfdwadrcgktplaqrqvmpgvrgwllfclsktlhlllvlaiplwaaeqhgiaisvvlat 241
Cdd:cd03506    95 RYQHFYFFPLLALLLLAF-------------------------------------------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 242 wLGSQMAASLLVVFLLLGTHWAEAEFYQPGAEgelPHGWYRHNFATACDWQPSPaWLGYFTGGLNLHLTHHLFPGWHHRH 321
Cdd:cd03506   113 -LVVQLAGGLWLAVVFQLNHFGMPVEDPPGES---KNDWLERQVLTTRNITGSP-FLDWLHGGLNYQIEHHLFPTMPRHN 187


                  ..
gi 1782765788 322 YP 323
Cdd:cd03506   188 YP 189
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
6-363 2.91e-38

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 139.09  E-value: 2.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788   6 PPLRYPADGEQAFHQALQRAAHHYLsgsrehRFAGGREWLKAGLLLVLCVTCYLLSLLqvsSGGFVICYLLFMLMAMLLN 85
Cdd:COG3239     2 TTATPLTPADEAELRALRARLRALL------GRRDWRYLLKLALTLALLAALWLLLSW---SWLALLAALLLGLALAGLF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  86 InVNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVhFHHVYANIEHYDLDteengffRQTPFQRWRPWMRWQH 165
Cdd:COG3239    73 S-LGHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHN-RHHAYTNDPGKDPD-------IGYGVQAWRPLYLFQH 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 166 LYWPLIAALSLPYLAWVFDWADRCGKtplaqRQVMPGVRGWLLFCLSKTLHLLLVLAIPLWAaeqhgiaisvVLATWLGS 245
Cdd:COG3239   144 LLRFFLLGLGGLYWLLALDFLPLRGR-----LELKERRLEALLLLLFLAALLALLLALGWWA----------VLLFWLLP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 246 QMAASLLVVFLLLGTHWAEaefyqpgaegELPHGWYRHNFATACDWQPSPaWLGYFTGGLNLHLTHHLFPGWHHRHYPAL 325
Cdd:COG3239   209 LLVAGLLLGLRFYLEHRGE----------DTGDGEYRDQLLGSRNIRGGR-LLRWLFGNLNYHIEHHLFPSIPWYRLPEA 277

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1782765788 326 AAILARLASEHGMNYRCISYRELLRRQQAFLRRMGQPQ 363
Cdd:COG3239   278 HRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPA 315
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 85-344 3.52e-16

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: 77.39  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  85 NINVNHDASHGVFSRSPR----INRIISRVVTLPLGLDPDYWRVRHVHfHHVYANIEHYDLDTeengffrQTPFQRWRPW 160
Cdd:pfam00487  19 TGSLAHEASHGALFKKRRlnrwLNDLLGRLAGLPLGISYSAWRIAHLV-HHRYTNGPDKDPDT-------APLASRFRGL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 161 MRWQHLYWPLIAALSLPYLAWVFDWADRCG--KTPLAQRQVMPGVRGWLLFCLSKTLHLLLVLAIPLWAAeqhgiaisvv 238
Cdd:pfam00487  91 LRYLLRWLLGLLVLAWLLALVLPLWLRRLArrKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLL---------- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 239 lATWLGSQMAASLLVVFLLlgtHWAEaefyqpgaegELPHGWYRHNFATACDWQPSPAWLGYFTGGLNLHLTHHLFPGWH 318
Cdd:pfam00487 161 -LLWLLPLLVFGFLLALIF---NYLE----------HYGGDWGERPVETTRSIRSPNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 1782765788 319 HRHYPALAAILARLASEHGMNYRCIS 344
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 86-143 6.40e-07

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: 47.85  E-value: 6.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1782765788  86 INVNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVHfHHVYANIEHYDLDT 143
Cdd:cd01060    16 TVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRR-HHRYTNTPGKDPDS 72
PLN02598 PLN02598
omega-6 fatty acid desaturase
 88-184 5.49e-03

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 38.65  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  88 VNHDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVHfHHVYANIEHYDLDTEEngfFRQTPFQRWRPWMR--WQH 165
Cdd:PLN02598  142 IGHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNT-HHAHTNKLVMDTAWQP---FRPHQFDNADPLRKamMRA 217

                          90       100
                  ....*....|....*....|
gi 1782765788 166 LYWPLIAALSLP-YLAWVFD 184
Cdd:PLN02598  218 GMGPLWWWASIGhWLFWHFD 237
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 90-315 5.95e-03

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: 37.59  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788  90 HDASHGVFSRSPRINRIISRVVTLPLGLDPDYWRVRHVHfHHVYANieHYDLDTeengffrqtpfqRWRPWMRWQHLYWP 169
Cdd:cd03507    52 HDCGHGSFSDNRRLNDIVGHILHSPLLVPYHSWRISHNR-HHAHTG--NLEGDE------------VWVPVTEEEYAELP 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782765788 170 LIaalsLPYLAwvfdwadrcgktpLAQRQVMPGVRGWLLFclskTLHLLLVLAIPLWAaeqhgIAISVVLATWLGSQMAa 249
Cdd:cd03507   117 KR----LPYRL-------------YRNPFLMLSLGWPYYL----LLNVLLYYLIPYLV-----VNAWLVLITYLQHTFP- 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782765788 250 sllvvflllGTHWAEAE---FYQPGAEGelphgwyrhnfATACDWqpsPAWLGYFTGGLNLHLTHHLFP 315
Cdd:cd03507   170 ---------DIPWYRADewnFAQAGLLG-----------TVDRDY---GGWLNWLTHIIGTHVAHHLFP 215
 
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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