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Conserved domains on  [gi|1481088731|gb|AYB30313|]
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acyl-CoA desaturase [Chryseolinea soli]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
5-366 2.49e-66

Fatty acid desaturase [Lipid transport and metabolism];


:

Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 212.67  E-value: 2.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731   5 NSIRFSSNRADFFSTLNRRVNDYFksnnisRYANAEMKVKTVFMYALYFVPYVLLLtgtvvNGWGMWGLAAIMGFGIAGI 84
Cdd:COG3239     3 TATPLTPADEAELRALRARLRALL------GRRDWRYLLKLALTLALLAALWLLLS-----WSWLALLAALLLGLALAGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  85 GlSVMHDANHGAYSNKGWVNNLMGYSLNV-IGAGAFNWKVQHNVlHHTYTNIHDVDEDIsprgilrMTPHSAYKAIHKFQ 163
Cdd:COG3239    72 F-SLGHDAGHGSLFRSRWLNDLLGRLLGLpLGTPYDAWRRSHNR-HHAYTNDPGKDPDI-------GYGVQAWRPLYLFQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 164 YLYAWFFYGLMTIVWVFHKDFARLTRyqkdgmvKKQKANVVAEWVILVATKTIYFVYILVIPmvvmditWWQWLIGFTTA 243
Cdd:COG3239   143 HLLRFFLLGLGGLYWLLALDFLPLRG-------RLELKERRLEALLLLLFLAALLALLLALG-------WWAVLLFWLLP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 244 HYIAGFILAVIFQPAHVIDGsefplpddegnMENSWAIHQLHTTTNFANkNRLLSWYVGGLNFQVEHHLFPNVCHVHYRH 323
Cdd:COG3239   209 LLVAGLLLGLRFYLEHRGED-----------TGDGEYRDQLLGSRNIRG-GRLLRWLFGNLNYHIEHHLFPSIPWYRLPE 276

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1481088731 324 ISKIVKATAEEFGLPYkAEPTFRGALLGHAKLLKDLGKRPVPA 366
Cdd:COG3239   277 AHRILKELCPEYGLPY-TEGSLLRSYREVLRLLRRLGLPARPA 318
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
5-366 2.49e-66

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 212.67  E-value: 2.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731   5 NSIRFSSNRADFFSTLNRRVNDYFksnnisRYANAEMKVKTVFMYALYFVPYVLLLtgtvvNGWGMWGLAAIMGFGIAGI 84
Cdd:COG3239     3 TATPLTPADEAELRALRARLRALL------GRRDWRYLLKLALTLALLAALWLLLS-----WSWLALLAALLLGLALAGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  85 GlSVMHDANHGAYSNKGWVNNLMGYSLNV-IGAGAFNWKVQHNVlHHTYTNIHDVDEDIsprgilrMTPHSAYKAIHKFQ 163
Cdd:COG3239    72 F-SLGHDAGHGSLFRSRWLNDLLGRLLGLpLGTPYDAWRRSHNR-HHAYTNDPGKDPDI-------GYGVQAWRPLYLFQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 164 YLYAWFFYGLMTIVWVFHKDFARLTRyqkdgmvKKQKANVVAEWVILVATKTIYFVYILVIPmvvmditWWQWLIGFTTA 243
Cdd:COG3239   143 HLLRFFLLGLGGLYWLLALDFLPLRG-------RLELKERRLEALLLLLFLAALLALLLALG-------WWAVLLFWLLP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 244 HYIAGFILAVIFQPAHVIDGsefplpddegnMENSWAIHQLHTTTNFANkNRLLSWYVGGLNFQVEHHLFPNVCHVHYRH 323
Cdd:COG3239   209 LLVAGLLLGLRFYLEHRGED-----------TGDGEYRDQLLGSRNIRG-GRLLRWLFGNLNYHIEHHLFPSIPWYRLPE 276

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1481088731 324 ISKIVKATAEEFGLPYkAEPTFRGALLGHAKLLKDLGKRPVPA 366
Cdd:COG3239   277 AHRILKELCPEYGLPY-TEGSLLRSYREVLRLLRRLGLPARPA 318
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 71-337 1.78e-51

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: 170.52  E-value: 1.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  71 WGLAAIMGFGIAgIGLSVMHDANHGAYSNKGWVNNLMGYSL-NVIGAGAFNWKVQHNVlHHTYTNIHDVDEDISPRGILR 149
Cdd:cd03506     1 LLLAILLGLFWA-QGGFLAHDAGHGQVFKNRWLNKLLGLTVgNLLGASAGWWKNKHNV-HHAYTNILGHDPDIDTLPLLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 150 MTPH-----SAYKAIHKFQYLYAWFFYGLmtivwvfhkdfarltryqkdgmvkkqkanvvaewvilvatktiyfvyilvi 224
Cdd:cd03506    79 RSEPafgkdQKKRFLHRYQHFYFFPLLAL--------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 225 pmvvmditwwqWLIGFTTAHYIAGFILAVIFQPAHVIDGSEFPlpddEGNMENSWAIHQLHTTTNFaNKNRLLSWYVGGL 304
Cdd:cd03506   108 -----------LLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDP----PGESKNDWLERQVLTTRNI-TGSPFLDWLHGGL 171

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1481088731 305 NFQVEHHLFPNVCHVHYRHISKIVKATAEEFGL 337
Cdd:cd03506   172 NYQIEHHLFPTMPRHNYPKVAPLVRELCKKHGL 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 67-339 1.18e-22

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: 95.49  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  67 GWGMWGLAAIMGFGIAGIGLSVMHDANHGAYSNKG----WVNNLMGY-SLNVIGAGAFNWKVQHNVlHHTYTNIHDVDED 141
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRrlnrWLNDLLGRlAGLPLGISYSAWRIAHLV-HHRYTNGPDKDPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 142 IsprgilrmtpHSAYKAIHKFQYLYAWFFYGLMTIVWVF---HKDFARLTRYQKDGMVKKQKANVVAEWVILVATKTIYF 218
Cdd:pfam00487  80 T----------APLASRFRGLLRYLLRWLLGLLVLAWLLalvLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLW 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 219 VYILVIPMVVMDITWWQWLIGFTTAHYIAGFIlavifqpAHVIDgsefplpddegnmenSWAIHQLHTTTNFANKNRLLS 298
Cdd:pfam00487 150 LGFLGLGGLLLLLWLLPLLVFGFLLALIFNYL-------EHYGG---------------DWGERPVETTRSIRSPNWWLN 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1481088731 299 WYVGGLNFQVEHHLFPNVCHVHYRHISKIVKATAEEFGLPY 339
Cdd:pfam00487 208 LLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREALPEHGLPY 248
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 68-375 6.68e-15

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 75.88  E-value: 6.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  68 WGMWGLAAIMGFGIAGIGLsVMHDANHGAYSNKGWVNNLMGYSL--NVIGAGAFNWKVQHNvLHHTYTNIHD-----VDE 140
Cdd:PLN03198  234 SAVLASACMMALCFQQCGW-LSHDFLHNQVFETRWLNEVVGYLIgnAVLGFSTGWWKEKHN-LHHAAPNECDqlyqpIDE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 141 DIS-------PRGILRMTPHSAYKAIHKFQYLyawFFYGLMTIV---WVFHKdfarlTRYQKDGmvkkqkanVVAEWVIL 210
Cdd:PLN03198  312 DIDtlpliawSKDILATVENKTFLRILQYQHL---FFMALLFFArgsWLFWS-----WRYTSTA--------KLAPADRL 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 211 VATKTIYFVYILVIPMVVMDITWWQWLIGFTTAHYIAGFILAVIFQPAHviDGSEFPlpddegNMENSWAIHQLHTTTNF 290
Cdd:PLN03198  376 LEKGTILFHYFWFIGTACYLLPGWKPLVWMAVTELMCGMLLGFVFVLSH--NGMEVY------NKSKEFVNAQIVSTRDI 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 291 aNKNRLLSWYVGGLNFQVEHHLFPNVCHVHYRHISKIVKATAEEFGLPYKAEPTFRGAllghAKLLKDLgKRPVPAAEPA 370
Cdd:PLN03198  448 -KANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGT----CKVLKAL-KEVAEAAAEQ 521


                  ....*
gi 1481088731 371 FAIAN 375
Cdd:PLN03198  522 HAAAS 526
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
5-366 2.49e-66

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 212.67  E-value: 2.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731   5 NSIRFSSNRADFFSTLNRRVNDYFksnnisRYANAEMKVKTVFMYALYFVPYVLLLtgtvvNGWGMWGLAAIMGFGIAGI 84
Cdd:COG3239     3 TATPLTPADEAELRALRARLRALL------GRRDWRYLLKLALTLALLAALWLLLS-----WSWLALLAALLLGLALAGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  85 GlSVMHDANHGAYSNKGWVNNLMGYSLNV-IGAGAFNWKVQHNVlHHTYTNIHDVDEDIsprgilrMTPHSAYKAIHKFQ 163
Cdd:COG3239    72 F-SLGHDAGHGSLFRSRWLNDLLGRLLGLpLGTPYDAWRRSHNR-HHAYTNDPGKDPDI-------GYGVQAWRPLYLFQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 164 YLYAWFFYGLMTIVWVFHKDFARLTRyqkdgmvKKQKANVVAEWVILVATKTIYFVYILVIPmvvmditWWQWLIGFTTA 243
Cdd:COG3239   143 HLLRFFLLGLGGLYWLLALDFLPLRG-------RLELKERRLEALLLLLFLAALLALLLALG-------WWAVLLFWLLP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 244 HYIAGFILAVIFQPAHVIDGsefplpddegnMENSWAIHQLHTTTNFANkNRLLSWYVGGLNFQVEHHLFPNVCHVHYRH 323
Cdd:COG3239   209 LLVAGLLLGLRFYLEHRGED-----------TGDGEYRDQLLGSRNIRG-GRLLRWLFGNLNYHIEHHLFPSIPWYRLPE 276

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1481088731 324 ISKIVKATAEEFGLPYkAEPTFRGALLGHAKLLKDLGKRPVPA 366
Cdd:COG3239   277 AHRILKELCPEYGLPY-TEGSLLRSYREVLRLLRRLGLPARPA 318
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 71-337 1.78e-51

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: 170.52  E-value: 1.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  71 WGLAAIMGFGIAgIGLSVMHDANHGAYSNKGWVNNLMGYSL-NVIGAGAFNWKVQHNVlHHTYTNIHDVDEDISPRGILR 149
Cdd:cd03506     1 LLLAILLGLFWA-QGGFLAHDAGHGQVFKNRWLNKLLGLTVgNLLGASAGWWKNKHNV-HHAYTNILGHDPDIDTLPLLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 150 MTPH-----SAYKAIHKFQYLYAWFFYGLmtivwvfhkdfarltryqkdgmvkkqkanvvaewvilvatktiyfvyilvi 224
Cdd:cd03506    79 RSEPafgkdQKKRFLHRYQHFYFFPLLAL--------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 225 pmvvmditwwqWLIGFTTAHYIAGFILAVIFQPAHVIDGSEFPlpddEGNMENSWAIHQLHTTTNFaNKNRLLSWYVGGL 304
Cdd:cd03506   108 -----------LLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDP----PGESKNDWLERQVLTTRNI-TGSPFLDWLHGGL 171

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1481088731 305 NFQVEHHLFPNVCHVHYRHISKIVKATAEEFGL 337
Cdd:cd03506   172 NYQIEHHLFPTMPRHNYPKVAPLVRELCKKHGL 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 67-339 1.18e-22

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: 95.49  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  67 GWGMWGLAAIMGFGIAGIGLSVMHDANHGAYSNKG----WVNNLMGY-SLNVIGAGAFNWKVQHNVlHHTYTNIHDVDED 141
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRrlnrWLNDLLGRlAGLPLGISYSAWRIAHLV-HHRYTNGPDKDPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 142 IsprgilrmtpHSAYKAIHKFQYLYAWFFYGLMTIVWVF---HKDFARLTRYQKDGMVKKQKANVVAEWVILVATKTIYF 218
Cdd:pfam00487  80 T----------APLASRFRGLLRYLLRWLLGLLVLAWLLalvLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLW 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 219 VYILVIPMVVMDITWWQWLIGFTTAHYIAGFIlavifqpAHVIDgsefplpddegnmenSWAIHQLHTTTNFANKNRLLS 298
Cdd:pfam00487 150 LGFLGLGGLLLLLWLLPLLVFGFLLALIFNYL-------EHYGG---------------DWGERPVETTRSIRSPNWWLN 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1481088731 299 WYVGGLNFQVEHHLFPNVCHVHYRHISKIVKATAEEFGLPY 339
Cdd:pfam00487 208 LLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREALPEHGLPY 248
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 68-375 6.68e-15

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 75.88  E-value: 6.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  68 WGMWGLAAIMGFGIAGIGLsVMHDANHGAYSNKGWVNNLMGYSL--NVIGAGAFNWKVQHNvLHHTYTNIHD-----VDE 140
Cdd:PLN03198  234 SAVLASACMMALCFQQCGW-LSHDFLHNQVFETRWLNEVVGYLIgnAVLGFSTGWWKEKHN-LHHAAPNECDqlyqpIDE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 141 DIS-------PRGILRMTPHSAYKAIHKFQYLyawFFYGLMTIV---WVFHKdfarlTRYQKDGmvkkqkanVVAEWVIL 210
Cdd:PLN03198  312 DIDtlpliawSKDILATVENKTFLRILQYQHL---FFMALLFFArgsWLFWS-----WRYTSTA--------KLAPADRL 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 211 VATKTIYFVYILVIPMVVMDITWWQWLIGFTTAHYIAGFILAVIFQPAHviDGSEFPlpddegNMENSWAIHQLHTTTNF 290
Cdd:PLN03198  376 LEKGTILFHYFWFIGTACYLLPGWKPLVWMAVTELMCGMLLGFVFVLSH--NGMEVY------NKSKEFVNAQIVSTRDI 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 291 aNKNRLLSWYVGGLNFQVEHHLFPNVCHVHYRHISKIVKATAEEFGLPYKAEPTFRGAllghAKLLKDLgKRPVPAAEPA 370
Cdd:PLN03198  448 -KANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGT----CKVLKAL-KEVAEAAAEQ 521


                  ....*
gi 1481088731 371 FAIAN 375
Cdd:PLN03198  522 HAAAS 526
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 71-142 1.56e-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: 58.25  E-value: 1.56e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1481088731  71 WGLAAIMGFGIAGIGLSVMHDANHGAYSNKGWVNNLMGYSLN-VIGAGAFNWKVQHNVlHHTYTNIHDVDEDI 142
Cdd:cd01060     1 LLLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGlALGGSYGWWRRSHRR-HHRYTNTPGKDPDS 72
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 88-361 3.62e-07

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 51.96  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  88 VMHDANHGAYSNKGWVNNLMGYSLNVigagafnWKVQHNVlHHTYTNIH-------DVDEDISPRGILRMTPHSA--YKA 158
Cdd:PLN03199  187 VFKKRKHGDLGGIFWGDLMQGFSMQW-------WKNKHNG-HHAVPNLHcssadaqDGDPDIDTMPLLAWSLKQAqsFRE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 159 IH---------KFQYLYAWFFYG----LMTIVWV---FHKDFARLTRYQKDGMVKKQKAnvvAEWVIL-VATKTIYFVYI 221
Cdd:PLN03199  259 INadgkdsgfvKFAIKFQAFFYFpillLARISWLnesFKCAFGLGAASENAALELEAKG---LQYPLLeKAGILLHYAWM 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 222 LVIPMVVMDITWWQWLIGFTTAHYIAGFILAVIFQPAH----VIDGSEFPlpddegnmeNSWAIhQLHTTTNFANKNRL- 296
Cdd:PLN03199  336 FTLSSGFGRFSFAYSAFYFFTATASCGFFLAIVFGLGHngmaTYDADARP---------DFWKL-QVTTTRNIIGGHGFp 405

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1481088731 297 ---LSWYVGGLNFQVEHHLFPNVCHVHYRHISKIVKATAEEFGLPYKAEPTFRGALlghaKLLKDLGK 361
Cdd:PLN03199  406 qafVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTM----EVLHHLGK 469
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 50-180 7.18e-07

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: 49.53  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  50 ALYFVPYVLLLTGT--VVNGWGMWGLAAIMGF--GIAGIGL-SVMHDANHGAYSNKGWVNNLMGYSLNVIGAGAFN-WKV 123
Cdd:cd03507     7 LSYLAPDILLLALLalAASLLLSWWLWPLYWIvqGLFLTGLfVLGHDCGHGSFSDNRRLNDIVGHILHSPLLVPYHsWRI 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1481088731 124 QHNVlHHTYTNIHDVDED---ISPRGILRMTPHSAYKAI--HKFQYLYAWFFYGLMTIVWVF 180
Cdd:cd03507    87 SHNR-HHAHTGNLEGDEVwvpVTEEEYAELPKRLPYRLYrnPFLMLSLGWPYYLLLNVLLYY 147
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 57-316 9.64e-04

This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine (3-O-methyl-scyllo-inosamine, 3-O-MSI) oxygenase, and other related proteins. It has been proposed that MocD, MocE (Rieske-like ferredoxin), and MocF (ferredoxin reductase) under the regulation of MocR, act in concert to form a ferredoxin oxygenase system that demethylates 3-O-MSI to form scyllo-inosamine. 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, HXXHH, 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: 239588 [Multi-domain]  Cd Length: 285  Bit Score: 40.43  E-value: 9.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  57 VLLLTGTVVNGWGMWglAAIMGFGIAGIGLSVM----HDANHGAYSNKGWVNNLMGYSLNVIGAGAFNWKVQHNVLHHTY 132
Cdd:cd03511    28 LAVSGILIAWTWGSW--WALPAFLVYGVLYAALfarwHECVHGTAFATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRY 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 133 TNIHDVD-EDISPRgilrmTPHSAYKAIHKFQYLYAWffyGLMTIVWVFHkdFARLTRYQKDGMVKKQKANVVAEWVILV 211
Cdd:cd03511   106 TQIPGRDpELAVPR-----PPTLREYLLALSGLPYWW---GKLRTVFRHA--FGAVSEAEKPFIPAEERPKVVREARAML 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731 212 AtktiyfVYILVIPMVVMDITWWQWLIGFTTAHYiAGFILAVIFQPAHVidgsefplpddeGNMENSWAIHQLHTTTNfa 291
Cdd:cd03511   176 A------VYAGLIALSLYLGSPLLVLVWGLPLLL-GQPILRLFLLAEHG------------GCPEDANDLRNTRTTLT-- 234

                         250       260
                  ....*....|....*....|....*
gi 1481088731 292 nkNRLLSWYVGGLNFQVEHHLFPNV 316
Cdd:cd03511   235 --NPPLRFLYWNMPYHAEHHMYPSV 257
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
 51-142 2.43e-03

Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the addition of hydroxyl groups to the beta-ionone rings of beta-carotene to form zeaxanthin and is found in bacteria and red algae. Carotenoids are important natural pigments; zeaxanthin and lutein are the only dietary carotenoids that accumulate in the macular region of the retina and lens. It is proposed that these carotenoids protect ocular tissues against photooxidative damage. CrtR does not show overall amino acid sequence similarity to the beta-carotene hydroxylases similar to CrtZ, an astaxanthin biosynthetic beta-carotene hydroxylase. However, CrtR does show sequence similarity to the green alga, Haematococcus pluvialis, beta-carotene ketolase (CrtW), which converts beta-carotene to canthaxanthin. Sequences of the CrtR_beta-carotene-hydroxylase domain family, as well as, the CrtW_beta-carotene-ketolase domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common 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: 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 homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239591 [Multi-domain]  Cd Length: 207  Bit Score: 38.89  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481088731  51 LYFVPYVLLLTGTVvnGWGMWGLAAIMGFGIAGIGL----SVMHDANHGAYSNKGWVNNLMGYSLNVIGAGAFNWKVQHN 126
Cdd:cd03514     2 LFLISMALVWLSTW--GYVISYLPLWVCFILNTLSLhlagTVIHDASHKAASRNRWINELIGHVSAFFLGFPFPVFRRVH 79

                          90
                  ....*....|....*.
gi 1481088731 127 VLHHTYTNIHDVDEDI 142
Cdd:cd03514    80 MQHHAHTNDPEKDPDH 95
 
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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