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Conserved domains on  [gi|66472330|ref|NP_001018541|]
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stearoyl-CoA desaturase b [Danio rerio]

Protein Classification

acyl-CoA desaturase (domain architecture ID 10131286)

acyl-CoA desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; similar to acyl-CoA delta(9) desaturase and acyl-CoA delta(11) desaturase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
54-294 1.02e-74

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: 227.05  E-value: 1.02e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330  54 SSLTLIWTGVCFMVSALGITAGAHRLWSHRSYRASLPLRIFLAVANSMAFQNDIYEWARDHRVHHKFSETDADPHNARRG 133
Cdd:cd03505   1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 134 FFFAHIGWLLvrkhpevidkgrkltfedlkadsvvmfqrrhyklsvvvmcfliptlvpwffweeslwtaylvpCLLRYAV 213
Cdd:cd03505  81 FWFSHVGWLG---------------------------------------------------------------GLLRIVL 97
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 214 VLNATWLVNSAAHMWGMRPYDHNINPRENKFVAFSAIGEGFHNYHHTFPHDYATSEFGSRLNVTKAFIDLMCFLGLANDC 293
Cdd:cd03505  98 VLHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDL 177

                .
gi 66472330 294 R 294
Cdd:cd03505 178 K 178
 
Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
54-294 1.02e-74

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: 227.05  E-value: 1.02e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330  54 SSLTLIWTGVCFMVSALGITAGAHRLWSHRSYRASLPLRIFLAVANSMAFQNDIYEWARDHRVHHKFSETDADPHNARRG 133
Cdd:cd03505   1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 134 FFFAHIGWLLvrkhpevidkgrkltfedlkadsvvmfqrrhyklsvvvmcfliptlvpwffweeslwtaylvpCLLRYAV 213
Cdd:cd03505  81 FWFSHVGWLG---------------------------------------------------------------GLLRIVL 97
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 214 VLNATWLVNSAAHMWGMRPYDHNINPRENKFVAFSAIGEGFHNYHHTFPHDYATSEFGSRLNVTKAFIDLMCFLGLANDC 293
Cdd:cd03505  98 VLHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDL 177

                .
gi 66472330 294 R 294
Cdd:cd03505 178 K 178
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
29-292 1.61e-57

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 224316  Cd Length: 289  Bit Score: 186.83  E-value: 1.61e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330  29 VWRNVILMTLLHLGALYGMTILPFVSSLTLIWTGVCFMVSALGITAGAHRLWSHRSYRASLPLRIFLAVANSMAFQNDIY 108
Cdd:COG1398  19 HWNNVLFFIGPLIVAYLAFYPDFFSWLAELIFTLAYYLIGGIGITLGLHRLWSHRAFKAHKWLEYVLAFWGALTTQGPAI 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 109 EWARDHRVHHKFSETDADPH-NARRGFFFAHIGWLLVRKhPEVIDkgrKLTFEDLKADSVVMFQRRHYKLSVVVMCFLIP 187
Cdd:COG1398  99 EWVGIHRKHHRKTDTDQDPHyDSFKGFWWSHIGWMLLYS-AEAKD---RETIQKLGKDIPLDWQHRNLYLIALLMQIVLP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 188 TLVPWFFWEeslWTAYLVPCLLRYAVVLNATWLVNSAAHMWGMRPYDHNINPRENKFVAFSAIGEGFHNYHHTFPHDYAT 267
Cdd:COG1398 175 LFIGYALGG---WLGLIWGGVQRLVLVQHATWCVNSLGHYIGYRPFDCRDTARNCWWVALVTFGEGWHNNHHAFPNSARN 251
                       250       260
                ....*....|....*....|....*
gi 66472330 268 SEFGSRLNVTKAFIDLMCFLGLAND 292
Cdd:COG1398 252 GLKWWEFDVTWWIIKLLSLLGLAKV 276
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
6-294 3.63e-27

delta-9 acyl-lipid desaturase


Pssm-ID: 177866  Cd Length: 299  Bit Score: 107.58  E-value: 3.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330    6 TTTEDVFDDSYVEKPGPSPPVQIVWRNVILMTLLHLGALYGMTIL-PFVSSLTLIWTG-VCFMVSALGITAGAHRLWSHR 83
Cdd:PLN02220   4 TTKDDGSSQSKAVRKEKRAFFFRKWTRLDVVRASAVGTVHFLCLLaPFNYKWEALRFGlILYIVTGLSITFSYHRNLAHR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330   84 SYRASLPLRIFLAVANSMAFQNDIYEWARDHRVHHKFSETDADPHNARRGFFFAHIGWLLVRKHpeVIDK-GRKLTFEDL 162
Cdd:PLN02220  84 SFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQFTDSDRDPHSPIEGFWFSHVLWIFDTSY--IREKcGGRDNVMDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330  163 KADSVVMFQRRHYKLSVVVMCFLIPTL--VPWFFWEESLWTaylvpcllryAVVLNATWLVNSAAHMWGMRPYDHNINPR 240
Cdd:PLN02220 162 KQQWFYRFLRKTIGLHILMFWTLLYLWggLPYLTWGVGVGG----------AIGYHVTWLINSACHIWGSRTWKTKDTSR 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 66472330  241 ENKFVAFSAIGEGFHNYHHTFPHDYATSEFGSRLNVTKAFIDLMCFLGLANDCR 294
Cdd:PLN02220 232 NVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRFFEVLGLATDVK 285
FA_desaturase pfam00487
Fatty acid desaturase;
63-262 1.46e-08

Fatty acid desaturase;


Pssm-ID: 395391 [Multi-domain]  Cd Length: 253  Bit Score: 54.66  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330    63 VCFMVSALGITAGAHRLWSHRSYRASLPLR----IFLAVANSMAFQNDIYEWARDHRVHHKF-SETDADPHNA-----RR 132
Cdd:pfam00487  10 LLGLFLLLGITGVLAHEASHGALFKKRRLNrwlnDLLGRLAGLPLGISYSAWRIAHLVHHRYtNGPDEDPDTAplasrFR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330   133 GFFFAHIGWLLVRKHPEVIDKG----RKLTFEDLKADSVVMFQRRHYKLSVVVMCFLIPTLVPWFFWEESLWTAYLVPCL 208
Cdd:pfam00487  90 GLLRYLLRWLLGLLVLAWLLALvlglWARRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLLWLLPLL 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 66472330   209 LRYAVVlnaTWLVNSAAHMWGMRPYDHNINPRE----NKFVAFSAIGEGFHNYHHTFP 262
Cdd:pfam00487 170 VAGFLL---ALIFNYLEHYGGDWGERPVETTRSirspNWWLNLLTGNLNYHIEHHLFP 224
 
Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
54-294 1.02e-74

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: 227.05  E-value: 1.02e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330  54 SSLTLIWTGVCFMVSALGITAGAHRLWSHRSYRASLPLRIFLAVANSMAFQNDIYEWARDHRVHHKFSETDADPHNARRG 133
Cdd:cd03505   1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 134 FFFAHIGWLLvrkhpevidkgrkltfedlkadsvvmfqrrhyklsvvvmcfliptlvpwffweeslwtaylvpCLLRYAV 213
Cdd:cd03505  81 FWFSHVGWLG---------------------------------------------------------------GLLRIVL 97
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 214 VLNATWLVNSAAHMWGMRPYDHNINPRENKFVAFSAIGEGFHNYHHTFPHDYATSEFGSRLNVTKAFIDLMCFLGLANDC 293
Cdd:cd03505  98 VLHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDL 177

                .
gi 66472330 294 R 294
Cdd:cd03505 178 K 178
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
29-292 1.61e-57

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 224316  Cd Length: 289  Bit Score: 186.83  E-value: 1.61e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330  29 VWRNVILMTLLHLGALYGMTILPFVSSLTLIWTGVCFMVSALGITAGAHRLWSHRSYRASLPLRIFLAVANSMAFQNDIY 108
Cdd:COG1398  19 HWNNVLFFIGPLIVAYLAFYPDFFSWLAELIFTLAYYLIGGIGITLGLHRLWSHRAFKAHKWLEYVLAFWGALTTQGPAI 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 109 EWARDHRVHHKFSETDADPH-NARRGFFFAHIGWLLVRKhPEVIDkgrKLTFEDLKADSVVMFQRRHYKLSVVVMCFLIP 187
Cdd:COG1398  99 EWVGIHRKHHRKTDTDQDPHyDSFKGFWWSHIGWMLLYS-AEAKD---RETIQKLGKDIPLDWQHRNLYLIALLMQIVLP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330 188 TLVPWFFWEeslWTAYLVPCLLRYAVVLNATWLVNSAAHMWGMRPYDHNINPRENKFVAFSAIGEGFHNYHHTFPHDYAT 267
Cdd:COG1398 175 LFIGYALGG---WLGLIWGGVQRLVLVQHATWCVNSLGHYIGYRPFDCRDTARNCWWVALVTFGEGWHNNHHAFPNSARN 251
                       250       260
                ....*....|....*....|....*
gi 66472330 268 SEFGSRLNVTKAFIDLMCFLGLAND 292
Cdd:COG1398 252 GLKWWEFDVTWWIIKLLSLLGLAKV 276
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
6-294 3.63e-27

delta-9 acyl-lipid desaturase


Pssm-ID: 177866  Cd Length: 299  Bit Score: 107.58  E-value: 3.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330    6 TTTEDVFDDSYVEKPGPSPPVQIVWRNVILMTLLHLGALYGMTIL-PFVSSLTLIWTG-VCFMVSALGITAGAHRLWSHR 83
Cdd:PLN02220   4 TTKDDGSSQSKAVRKEKRAFFFRKWTRLDVVRASAVGTVHFLCLLaPFNYKWEALRFGlILYIVTGLSITFSYHRNLAHR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330   84 SYRASLPLRIFLAVANSMAFQNDIYEWARDHRVHHKFSETDADPHNARRGFFFAHIGWLLVRKHpeVIDK-GRKLTFEDL 162
Cdd:PLN02220  84 SFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQFTDSDRDPHSPIEGFWFSHVLWIFDTSY--IREKcGGRDNVMDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330  163 KADSVVMFQRRHYKLSVVVMCFLIPTL--VPWFFWEESLWTaylvpcllryAVVLNATWLVNSAAHMWGMRPYDHNINPR 240
Cdd:PLN02220 162 KQQWFYRFLRKTIGLHILMFWTLLYLWggLPYLTWGVGVGG----------AIGYHVTWLINSACHIWGSRTWKTKDTSR 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 66472330  241 ENKFVAFSAIGEGFHNYHHTFPHDYATSEFGSRLNVTKAFIDLMCFLGLANDCR 294
Cdd:PLN02220 232 NVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRFFEVLGLATDVK 285
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
58-140 1.18e-09

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: 55.17  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330  58 LIWTGVCFMVSALGITAGAHRLwSHRSY-RASLPLRIFLAVANsMAFQNDIYEWARDHRVHHKFSETD-ADPHNARrgFF 135
Cdd:cd01060   1 LLLALLLGLLGGLGLTVLAHEL-GHRSFfRSRWLNRLLGALLG-LALGGSYGWWRRSHRRHHRYTNTPgKDPDSAV--NY 76

                ....*
gi 66472330 136 FAHIG 140
Cdd:cd01060  77 LEHYG 81
FA_desaturase pfam00487
Fatty acid desaturase;
63-262 1.46e-08

Fatty acid desaturase;


Pssm-ID: 395391 [Multi-domain]  Cd Length: 253  Bit Score: 54.66  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330    63 VCFMVSALGITAGAHRLWSHRSYRASLPLR----IFLAVANSMAFQNDIYEWARDHRVHHKF-SETDADPHNA-----RR 132
Cdd:pfam00487  10 LLGLFLLLGITGVLAHEASHGALFKKRRLNrwlnDLLGRLAGLPLGISYSAWRIAHLVHHRYtNGPDEDPDTAplasrFR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472330   133 GFFFAHIGWLLVRKHPEVIDKG----RKLTFEDLKADSVVMFQRRHYKLSVVVMCFLIPTLVPWFFWEESLWTAYLVPCL 208
Cdd:pfam00487  90 GLLRYLLRWLLGLLVLAWLLALvlglWARRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLLWLLPLL 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 66472330   209 LRYAVVlnaTWLVNSAAHMWGMRPYDHNINPRE----NKFVAFSAIGEGFHNYHHTFP 262
Cdd:pfam00487 170 VAGFLL---ALIFNYLEHYGGDWGERPVETTRSirspNWWLNLLTGNLNYHIEHHLFP 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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