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Conserved domains on  [gi|118781711|ref|XP_311819|]
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AGAP003051-PA [Anopheles gambiae str. PEST]

Protein Classification

acyl-CoA desaturase( domain architecture ID 10787615)

acyl-CoA desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; similar to acyl-CoA delta(9) desaturase

EC:  1.14.19.-
Gene Ontology:  GO:0046872|GO:0016020|GO:0006633|GO:0016717|GO:0016717|GO:0006636
PubMed:  9767077|15189125

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
49-338 5.84e-70

Fatty-acid desaturase [Lipid transport and metabolism];


:

Pssm-ID: 441008  Cd Length: 286  Bit Score: 221.24  E-value: 5.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  49 ASVPPTPFRARIRWPDLFAQLFVHGGFLIGLYYLVTFQAKFYTYLWTLGLVWATGIGITAGAHRLWSHKSYKARWPLRLL 128
Cdd:COG1398    3 TATPAPPEKGRINWVTVLFFVLLHLLALLAAVPYAGVGFSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 129 LMFLFTICGQRDAYTWAHDHRVHHKYSETDADPHNAK-RGFFFAHVGWvFLTPHPEVVAKRKAidmSDLEADPIVMLQRR 207
Cdd:COG1398   83 LAILGALALQGGPLWWVADHRRHHRHSDTEGDPHSPKlRGFWWSHMGW-MLREDPTPNDYRYA---PDLAKDPELRWLDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 208 YYLPLFALLVIGLPVLVPWyWWGEQLAVAFWVCFtFRFTTTLNIAFFVNSVAHMFGNKPYDRSISPVENLAVAIAAMGEG 287
Cdd:COG1398  159 YYLLLQLALGLLLPALLGG-LLGGGWSGLLWGGF-VRTVLLHHGTWFINSLAHVWGYRPFETRDTSRNNWWLALLTFGEG 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 118781711 288 WHNYHHVFPWDYKTSeLGSYLFNVTTGFIDCFARLGWAYDRKSVPPEVVAR 338
Cdd:COG1398  237 WHNNHHAFPTSARHG-LRWWEIDPTWWLIRLLEKLGLAWDVRRPPAERIAA 286
 
Name Accession Description Interval E-value
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
49-338 5.84e-70

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 441008  Cd Length: 286  Bit Score: 221.24  E-value: 5.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  49 ASVPPTPFRARIRWPDLFAQLFVHGGFLIGLYYLVTFQAKFYTYLWTLGLVWATGIGITAGAHRLWSHKSYKARWPLRLL 128
Cdd:COG1398    3 TATPAPPEKGRINWVTVLFFVLLHLLALLAAVPYAGVGFSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 129 LMFLFTICGQRDAYTWAHDHRVHHKYSETDADPHNAK-RGFFFAHVGWvFLTPHPEVVAKRKAidmSDLEADPIVMLQRR 207
Cdd:COG1398   83 LAILGALALQGGPLWWVADHRRHHRHSDTEGDPHSPKlRGFWWSHMGW-MLREDPTPNDYRYA---PDLAKDPELRWLDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 208 YYLPLFALLVIGLPVLVPWyWWGEQLAVAFWVCFtFRFTTTLNIAFFVNSVAHMFGNKPYDRSISPVENLAVAIAAMGEG 287
Cdd:COG1398  159 YYLLLQLALGLLLPALLGG-LLGGGWSGLLWGGF-VRTVLLHHGTWFINSLAHVWGYRPFETRDTSRNNWWLALLTFGEG 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 118781711 288 WHNYHHVFPWDYKTSeLGSYLFNVTTGFIDCFARLGWAYDRKSVPPEVVAR 338
Cdd:COG1398  237 WHNNHHAFPTSARHG-LRWWEIDPTWWLIRLLEKLGLAWDVRRPPAERIAA 286
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 91-329 4.50e-67

The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXXH, HXXHH, and H/QXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.


Pssm-ID: 239582  Cd Length: 178  Bit Score: 210.10  E-value: 4.50e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  91 TYLWTLGLVWATGIGITAGAHRLWSHKSYKARWPLRLLLMFLFTICGQRDAYTWAHDHRVHHKYSETDADPHNAKRGFFF 170
Cdd:cd03505    4 TLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRGFWF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 171 AHVGwvfltphpevvakrkaidmsdleadpivmlqrryylplfallviglpvlvpwywwgeqlavafWVCFTFRFTTTLN 250
Cdd:cd03505   84 SHVG---------------------------------------------------------------WLGGLLRIVLVLH 100

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118781711 251 IAFFVNSVAHMFGNKPYDRSISPVENLAVAIAAMGEGWHNYHHVFPWDYKTSeLGSYLFNVTTGFIDCFARLGWAYDRK 329
Cdd:cd03505  101 ATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNG-LKWYQIDPTKWVIRLLEKLGLAWDLK 178
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
 61-341 2.19e-18

delta-9 acyl-lipid desaturase


Pssm-ID: 177866 [Multi-domain]  Cd Length: 299  Bit Score: 84.47  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  61 RWPDLFAQLFVHGGFLIGLYYLVTFQAKFYTYLWTLGLVWATGIGITAGAHRLWSHKSYK-ARWplrllLMFLFTICG-- 137
Cdd:PLN02220  27 KWTRLDVVRASAVGTVHFLCLLAPFNYKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKlPKW-----LEYPFAYSAlf 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 138 --QRDAYTWAHDHRVHHKYSETDADPHNAKRGFFFAHVGWVFLTPHPEVVAKRKAidmsdleadpIVMLQRRYYLPLFAL 215
Cdd:PLN02220 102 alQGDPIDWVSTHRFHHQFTDSDRDPHSPIEGFWFSHVLWIFDTSYIREKCGGRD----------NVMDLKQQWFYRFLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 216 LVIGLPVLVPW---YWWGeqlAVAFWVC-FTFRFTTTLNIAFFVNSVAHMFGNKPYDRSISPVENLAVAIAAMGEGWHNY 291
Cdd:PLN02220 172 KTIGLHILMFWtllYLWG---GLPYLTWgVGVGGAIGYHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNN 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 118781711 292 HHVFPWDYKTSeLGSYLFNVTTGFIDCFARLGWAYDRKsVPPEVVARRAA 341
Cdd:PLN02220 249 HHAFESSARQG-LEWWQIDITWYLIRFFEVLGLATDVK-LPTEAQKRKMA 296
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 89-296 2.76e-13

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: 68.91  E-value: 2.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711   89 FYTYLWTLGLVWATGIGITA--GAHRLWSHKSYKARWPLRLLLMFLFTICGQrDAYTWAHDHRVHHKY-SETDADPHNA- 164
Cdd:pfam00487   4 ALLLALLLGLFLLGITGSLAheASHGALFKKRRLNRWLNDLLGRLAGLPLGI-SYSAWRIAHLVHHRYtNGPDKDPDTAp 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  165 ----KRGFFFAHVGWVFLTPHPEVVAKRKAI----DMSDLEADPIVMLQRRYYLPLFALLVIGLPVLVPWYWWGEQLAVA 236
Cdd:pfam00487  83 lasrFRGLLRYLLRWLLGLLVLAWLLALVLPlwlrRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118781711  237 FWVCFtfrFTTTLNIAFFVNSVAHMFGNKPYD--------RSISPVENLAVaiaaMGEGWHNYHHVFP 296
Cdd:pfam00487 163 WLLPL---LVFGFLLALIFNYLEHYGGDWGERpvettrsiRSPNWWLNLLT----GNLNYHIEHHLFP 223
 
Name Accession Description Interval E-value
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
49-338 5.84e-70

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 441008  Cd Length: 286  Bit Score: 221.24  E-value: 5.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  49 ASVPPTPFRARIRWPDLFAQLFVHGGFLIGLYYLVTFQAKFYTYLWTLGLVWATGIGITAGAHRLWSHKSYKARWPLRLL 128
Cdd:COG1398    3 TATPAPPEKGRINWVTVLFFVLLHLLALLAAVPYAGVGFSWSAVALALVLYVLTGLGITVGYHRLFSHRSFKTPRWLEYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 129 LMFLFTICGQRDAYTWAHDHRVHHKYSETDADPHNAK-RGFFFAHVGWvFLTPHPEVVAKRKAidmSDLEADPIVMLQRR 207
Cdd:COG1398   83 LAILGALALQGGPLWWVADHRRHHRHSDTEGDPHSPKlRGFWWSHMGW-MLREDPTPNDYRYA---PDLAKDPELRWLDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 208 YYLPLFALLVIGLPVLVPWyWWGEQLAVAFWVCFtFRFTTTLNIAFFVNSVAHMFGNKPYDRSISPVENLAVAIAAMGEG 287
Cdd:COG1398  159 YYLLLQLALGLLLPALLGG-LLGGGWSGLLWGGF-VRTVLLHHGTWFINSLAHVWGYRPFETRDTSRNNWWLALLTFGEG 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 118781711 288 WHNYHHVFPWDYKTSeLGSYLFNVTTGFIDCFARLGWAYDRKSVPPEVVAR 338
Cdd:COG1398  237 WHNNHHAFPTSARHG-LRWWEIDPTWWLIRLLEKLGLAWDVRRPPAERIAA 286
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
 91-329 4.50e-67

The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXXH, HXXHH, and H/QXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.


Pssm-ID: 239582  Cd Length: 178  Bit Score: 210.10  E-value: 4.50e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  91 TYLWTLGLVWATGIGITAGAHRLWSHKSYKARWPLRLLLMFLFTICGQRDAYTWAHDHRVHHKYSETDADPHNAKRGFFF 170
Cdd:cd03505    4 TLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRGFWF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 171 AHVGwvfltphpevvakrkaidmsdleadpivmlqrryylplfallviglpvlvpwywwgeqlavafWVCFTFRFTTTLN 250
Cdd:cd03505   84 SHVG---------------------------------------------------------------WLGGLLRIVLVLH 100

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118781711 251 IAFFVNSVAHMFGNKPYDRSISPVENLAVAIAAMGEGWHNYHHVFPWDYKTSeLGSYLFNVTTGFIDCFARLGWAYDRK 329
Cdd:cd03505  101 ATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNG-LKWYQIDPTKWVIRLLEKLGLAWDLK 178
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
 61-341 2.19e-18

delta-9 acyl-lipid desaturase


Pssm-ID: 177866 [Multi-domain]  Cd Length: 299  Bit Score: 84.47  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  61 RWPDLFAQLFVHGGFLIGLYYLVTFQAKFYTYLWTLGLVWATGIGITAGAHRLWSHKSYK-ARWplrllLMFLFTICG-- 137
Cdd:PLN02220  27 KWTRLDVVRASAVGTVHFLCLLAPFNYKWEALRFGLILYIVTGLSITFSYHRNLAHRSFKlPKW-----LEYPFAYSAlf 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 138 --QRDAYTWAHDHRVHHKYSETDADPHNAKRGFFFAHVGWVFLTPHPEVVAKRKAidmsdleadpIVMLQRRYYLPLFAL 215
Cdd:PLN02220 102 alQGDPIDWVSTHRFHHQFTDSDRDPHSPIEGFWFSHVLWIFDTSYIREKCGGRD----------NVMDLKQQWFYRFLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 216 LVIGLPVLVPW---YWWGeqlAVAFWVC-FTFRFTTTLNIAFFVNSVAHMFGNKPYDRSISPVENLAVAIAAMGEGWHNY 291
Cdd:PLN02220 172 KTIGLHILMFWtllYLWG---GLPYLTWgVGVGGAIGYHVTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNN 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 118781711 292 HHVFPWDYKTSeLGSYLFNVTTGFIDCFARLGWAYDRKsVPPEVVARRAA 341
Cdd:PLN02220 249 HHAFESSARQG-LEWWQIDITWYLIRFFEVLGLATDVK-LPTEAQKRKMA 296
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 89-296 2.76e-13

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: 68.91  E-value: 2.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711   89 FYTYLWTLGLVWATGIGITA--GAHRLWSHKSYKARWPLRLLLMFLFTICGQrDAYTWAHDHRVHHKY-SETDADPHNA- 164
Cdd:pfam00487   4 ALLLALLLGLFLLGITGSLAheASHGALFKKRRLNRWLNDLLGRLAGLPLGI-SYSAWRIAHLVHHRYtNGPDKDPDTAp 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  165 ----KRGFFFAHVGWVFLTPHPEVVAKRKAI----DMSDLEADPIVMLQRRYYLPLFALLVIGLPVLVPWYWWGEQLAVA 236
Cdd:pfam00487  83 lasrFRGLLRYLLRWLLGLLVLAWLLALVLPlwlrRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118781711  237 FWVCFtfrFTTTLNIAFFVNSVAHMFGNKPYD--------RSISPVENLAVaiaaMGEGWHNYHHVFP 296
Cdd:pfam00487 163 WLLPL---LVFGFLLALIFNYLEHYGGDWGERpvettrsiRSPNWWLNLLT----GNLNYHIEHHLFP 223
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 92-174 6.94e-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: 62.10  E-value: 6.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  92 YLWTLGLVWATGIGITAGAHRLwSHKSY-KARWPLRLLLMFLFTiCGQRDAYTWAHDHRVHHKYSETD-ADPHNAkrGFF 169
Cdd:cd01060    1 LLLALLLGLLGGLGLTVLAHEL-GHRSFfRSRWLNRLLGALLGL-ALGGSYGWWRRSHRRHHRYTNTPgKDPDSA--VNY 76


                 ....*
gi 118781711 170 FAHVG 174
Cdd:cd01060   77 LEHYG 81
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
55-296 7.10e-05

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 44.33  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  55 PFRARIRWPdLFAQLFVHGGFLIGLYYLVTFQakfytyLWTLGLVWATGIGITA-------GAHRLWSHKsykaRWPLRL 127
Cdd:COG3239   24 ALLGRRDWR-YLLKLALTLALLAALWLLLSWS------WLALLAALLLGLALAGlfslghdAGHGSLFRS----RWLNDL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 128 LLMFLFTICGQrDAYTWAHDHRVHHKYS-ETDADP------HNAKRGFFFAHVGWVFLTPhPEVVAKRKAIDMSDLEADP 200
Cdd:COG3239   93 LGRLLGLPLGT-PYDAWRRSHNRHHAYTnDPGKDPdigygvQAWRPLYLFQHLLRFFLLG-LGGLYWLLALDFLPLRGRL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 201 IVMLQRRYYLPLFALLVIGLPVLVpwyWWGEQLAVAFWVCFTFRFTTTLNIAFFVNsvaHMFGNKPYDRSISPVEN---- 276
Cdd:COG3239  171 ELKERRLEALLLLLFLAALLALLL---ALGWWAVLLFWLLPLLVAGLLLGLRFYLE---HRGEDTGDGEYRDQLLGsrni 244

                        250       260
                 ....*....|....*....|...
gi 118781711 277 ---LAVAIAAMGEGWHNYHHVFP 296
Cdd:COG3239  245 rggRLLRWLFGNLNYHIEHHLFP 267
Alkane-hydroxylase cd03512
Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement ...
 52-237 3.56e-04

Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement for iron and oxygen for activity similar to that of the non-heme integral-membrane acyl coenzyme A (CoA) desaturases and acyl lipid desaturases. The alk genes in Pseudomonas oleovorans encode conversion of alkanes to acyl CoA. The alkane omega-hydroxylase (AlkB) system is responsible for the initial oxidation of inactivated alkanes. It is a three-component system comprising a soluble NADH-rubredoxin reductase (AlkT), a soluble rubredoxin (AlkG), and the integral membrane oxygenase (AlkB). AlkB utilizes the oxygen rebound mechanism to hydroxylate alkanes. This mechanism involves homolytic cleavage of the C-H bond by an electrophilic metal-oxo intermediate to generate a substrate-based radical. 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. The active site structure of AlkB is not known, however, spectroscopic and genetic evidence points 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. Like all other members of this superfamily, there are eight conserved histidines seen in the histidine cluster motifs: HXXXH, HXXXHH, 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. Also included in this CD are terminal alkane hydroxylases (AlkM), xylene monooxygenase hydroxylases (XylM), p-cymene monooxygenase hydroxylases (CymAa), and other related proteins.


Pssm-ID: 239589  Cd Length: 314  Bit Score: 42.26  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711  52 PPTPFRARIRWPD--LFAQLFVHGGFLI-GLYYLVTFQAKFYTYL-WTLGLVWATG-IGITAgAHRLwSHKSYK-ARWPL 125
Cdd:cd03512   29 PEEPPLEKDRYYRwlLYLLLPLQFALLFlGVWAVSTGDLSALEKVgLILSLGLLSGvIGINT-AHEL-IHRRSRlERWLG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118781711 126 RLLLMFL----FTIcgqrdaytwAHDhRVHHKYSETDADPHNAKRG---FFFAHVGWVFltphpevvAKRKAIdmsDLEA 198
Cdd:cd03512  107 KLLLASLlyghFAI---------EHV-RGHHRYVATPEDPATARRGesfYRFLPRALVG--------SFRSAW---KLEK 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 118781711 199 DpivMLQRRYYLP-------LFALLVIGLPVLVPWYWWGEQLAVAF 237
Cdd:cd03512  166 K---RLRRKGRSPwsprnevLRYLALAVALLALAAALGGLAGLLFL 208
 
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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