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Conserved domains on  [gi|17542730|ref|NP_502560|]
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Delta(12) fatty acid desaturase fat-2 [Caenorhabditis elegans]

Protein Classification

fatty acid desaturase( domain architecture ID 10131385)

fatty acid desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; similar to delta(12) fatty acid desaturase and related proteins

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 39-310 5.58e-74

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: 229.03  E-value: 5.58e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  39 KDPLTSISYLIKDYVLLAGLYFAVPYiehYLGWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPI 118
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAASL---LLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 119 LAPFWPWQKSHRQHHQYTSHVEKDKGHPWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLpdgshfwpwsrlfet 198
Cdd:cd03507  78 LVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLLLN--------------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 199 tedrvkcavsgvacaicayiafvlcdysvytFVKYYYIPLLFQGLILVIITYLQHQNEDIEVYEADEWGF-VRGQTQTID 277
Cdd:cd03507 143 -------------------------------VLLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADEWNFaQAGLLGTVD 191

                       250       260       270
                ....*....|....*....|....*....|...
gi 17542730 278 RHWGFGLDNIMHNItNGHVAHHfFFTKIPHYHL 310
Cdd:cd03507 192 RDYGGWLNWLTHII-GTHVAHH-LFPRIPHYNL 222
 
Name Accession Description Interval E-value
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 39-310 5.58e-74

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: 229.03  E-value: 5.58e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  39 KDPLTSISYLIKDYVLLAGLYFAVPYiehYLGWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPI 118
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAASL---LLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 119 LAPFWPWQKSHRQHHQYTSHVEKDKGHPWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLpdgshfwpwsrlfet 198
Cdd:cd03507  78 LVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLLLN--------------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 199 tedrvkcavsgvacaicayiafvlcdysvytFVKYYYIPLLFQGLILVIITYLQHQNEDIEVYEADEWGF-VRGQTQTID 277
Cdd:cd03507 143 -------------------------------VLLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADEWNFaQAGLLGTVD 191

                       250       260       270
                ....*....|....*....|....*....|...
gi 17542730 278 RHWGFGLDNIMHNItNGHVAHHfFFTKIPHYHL 310
Cdd:cd03507 192 RDYGGWLNWLTHII-GTHVAHH-LFPRIPHYNL 222
PLN02505 PLN02505
omega-6 fatty acid desaturase
 24-321 2.94e-63

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 206.84  E-value: 2.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730   24 SVAAVKAAIPEHCFVKDPLTSISYLIKDYVLLAGL-YFAVPYIEHYLGWIGLLGW--YWAM-GIVGSALFCVGHDCGHGS 99
Cdd:PLN02505  32 TLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLyYVATNYIPLLPGPLSYVAWplYWAAqGCVLTGVWVIAHECGHHA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  100 FSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKD--------KGHPWVTEEdYNNRTAIEKYFAVIPISGW 171
Cdd:PLN02505 112 FSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDevfvpkkkSALPWYSKY-LNNPPGRLLHIVVQLTLGW 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  172 lrwnPIY---TIVGLPD---GSHFWPWSRLFETTEdRVKCAVSGVACAICAYIAFVLcdYSVYTF---VKYYYIPLLFQG 242
Cdd:PLN02505 191 ----PLYlafNVSGRPYdrfACHFDPYSPIFNDRE-RLQIYISDAGILAVSFGLYRL--AAAKGLawvLCVYGVPLLIVN 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542730  243 LILVIITYLQHQNEDIEVYEADEWGFVRGQTQTIDRHWGFgLDNIMHNITNGHVAHHFFFTkIPHYHLLEATPAIKKAL 321
Cdd:PLN02505 264 AFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGI-LNKVFHNITDTHVAHHLFST-MPHYHAMEATKAIKPIL 340
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
12-322 4.33e-37

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 136.40  E-value: 4.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  12 KDLDTIKVPELPSVAAVKAAIPEHCFvKDPLTSISYLIKDYVLLAGLYFAVPYiehylGWIGLLGWyWAMGIVGSALFCV 91
Cdd:COG3239   2 TTATPLTPADEAELRALRARLRALLG-RRDWRYLLKLALTLALLAALWLLLSW-----SWLALLAA-LLLGLALAGLFSL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  92 GHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDkghpwvteEDYNNRtaIEKYFAVIPISGW 171
Cdd:COG3239  75 GHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKD--------PDIGYG--VQAWRPLYLFQHL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 172 LrWNPIYTIVGLPD--GSHFWPWSRLFETTEDRVKCAVSGVACAICAYIAFVLcdySVYTFVKYYYIPLLFQGLILVIIT 249
Cdd:COG3239 145 L-RFFLLGLGGLYWllALDFLPLRGRLELKERRLEALLLLLFLAALLALLLAL---GWWAVLLFWLLPLLVAGLLLGLRF 220

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542730 250 YLQHQNEDieVYEADEWGFVRGqtqTIDRHWGFGLDNIMHNItNGHVAHHfFFTKIPHYHLLEATPAIKKALE 322
Cdd:COG3239 221 YLEHRGED--TGDGEYRDQLLG---SRNIRGGRLLRWLFGNL-NYHIEHH-LFPSIPWYRLPEAHRILKELCP 286
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 70-323 8.08e-15

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: 73.53  E-value: 8.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730    70 GWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSD----YEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDkgh 145
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKD--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730   146 PWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLPDGSHFWPWSRLFETTEDRVKCAVSGVACAICAYIAFVLcdY 225
Cdd:pfam00487  78 PDTAPLASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLG--L 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730   226 SVYTFVKYYYIPLLFQGLILVIITYLQHQnedievyeADEWGFVRGQTQTiDRHWGFGLDNIMHNITNGHVAHHfFFTKI 305
Cdd:pfam00487 156 GGLLLLLWLLPLLVFGFLLALIFNYLEHY--------GGDWGERPVETTR-SIRSPNWWLNLLTGNLNYHIEHH-LFPGV 225

                         250
                  ....*....|....*...
gi 17542730   306 PHYHLLEATPAIKKALEP 323
Cdd:pfam00487 226 PWYRLPKLHRRLREALPE 243
 
Name Accession Description Interval E-value
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 39-310 5.58e-74

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: 229.03  E-value: 5.58e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  39 KDPLTSISYLIKDYVLLAGLYFAVPYiehYLGWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPI 118
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAASL---LLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 119 LAPFWPWQKSHRQHHQYTSHVEKDKGHPWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLpdgshfwpwsrlfet 198
Cdd:cd03507  78 LVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLLLN--------------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 199 tedrvkcavsgvacaicayiafvlcdysvytFVKYYYIPLLFQGLILVIITYLQHQNEDIEVYEADEWGF-VRGQTQTID 277
Cdd:cd03507 143 -------------------------------VLLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADEWNFaQAGLLGTVD 191

                       250       260       270
                ....*....|....*....|....*....|...
gi 17542730 278 RHWGFGLDNIMHNItNGHVAHHfFFTKIPHYHL 310
Cdd:cd03507 192 RDYGGWLNWLTHII-GTHVAHH-LFPRIPHYNL 222
PLN02505 PLN02505
omega-6 fatty acid desaturase
 24-321 2.94e-63

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 206.84  E-value: 2.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730   24 SVAAVKAAIPEHCFVKDPLTSISYLIKDYVLLAGL-YFAVPYIEHYLGWIGLLGW--YWAM-GIVGSALFCVGHDCGHGS 99
Cdd:PLN02505  32 TLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLyYVATNYIPLLPGPLSYVAWplYWAAqGCVLTGVWVIAHECGHHA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  100 FSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKD--------KGHPWVTEEdYNNRTAIEKYFAVIPISGW 171
Cdd:PLN02505 112 FSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDevfvpkkkSALPWYSKY-LNNPPGRLLHIVVQLTLGW 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  172 lrwnPIY---TIVGLPD---GSHFWPWSRLFETTEdRVKCAVSGVACAICAYIAFVLcdYSVYTF---VKYYYIPLLFQG 242
Cdd:PLN02505 191 ----PLYlafNVSGRPYdrfACHFDPYSPIFNDRE-RLQIYISDAGILAVSFGLYRL--AAAKGLawvLCVYGVPLLIVN 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542730  243 LILVIITYLQHQNEDIEVYEADEWGFVRGQTQTIDRHWGFgLDNIMHNITNGHVAHHFFFTkIPHYHLLEATPAIKKAL 321
Cdd:PLN02505 264 AFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGI-LNKVFHNITDTHVAHHLFST-MPHYHAMEATKAIKPIL 340
PLN02498 PLN02498
omega-3 fatty acid desaturase
 25-321 5.99e-57

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 192.35  E-value: 5.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730   25 VAAVKAAIPEHCFVKDPLTSISYLIKDYVLLAGLYFAVPYIEHYLGWigllGWYW-AMGIVGSALFCVGHDCGHGSFSDY 103
Cdd:PLN02498 104 LADIRAAIPKHCWVKNPWRSMSYVVRDVAVVFGLAAAAAYFNNWVVW----PLYWfAQGTMFWALFVLGHDCGHGSFSNN 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  104 EWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDKG-HPwVTEEDYNNRTAIEKYFAV---IPISGWlrwnPIYT 179
Cdd:PLN02498 180 PKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESwHP-LSEKIYKSLDKVTRTLRFtlpFPMLAY----PFYL 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  180 IVGLP--DGSHFWPWSRLFETTEDrvKCAVSGVAC-----AICAYIAFVLCDYSVytfVKYYYIPLLFQGLILVIITYLQ 252
Cdd:PLN02498 255 WSRSPgkKGSHFHPDSDLFVPKER--KDVITSTACwtamaALLVCLSFVMGPIQM---LKLYGIPYWIFVMWLDFVTYLH 329

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542730  253 HQNEDIEV--YEADEWGFVRGQTQTIDRHWGFgLDNIMHNITNgHVAHHfFFTKIPHYHLLEATPAIKKAL 321
Cdd:PLN02498 330 HHGHEDKLpwYRGKEWSYLRGGLTTLDRDYGW-INNIHHDIGT-HVIHH-LFPQIPHYHLVEATEAAKPVL 397
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
12-322 4.33e-37

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 136.40  E-value: 4.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  12 KDLDTIKVPELPSVAAVKAAIPEHCFvKDPLTSISYLIKDYVLLAGLYFAVPYiehylGWIGLLGWyWAMGIVGSALFCV 91
Cdd:COG3239   2 TTATPLTPADEAELRALRARLRALLG-RRDWRYLLKLALTLALLAALWLLLSW-----SWLALLAA-LLLGLALAGLFSL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  92 GHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDkghpwvteEDYNNRtaIEKYFAVIPISGW 171
Cdd:COG3239  75 GHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKD--------PDIGYG--VQAWRPLYLFQHL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 172 LrWNPIYTIVGLPD--GSHFWPWSRLFETTEDRVKCAVSGVACAICAYIAFVLcdySVYTFVKYYYIPLLFQGLILVIIT 249
Cdd:COG3239 145 L-RFFLLGLGGLYWllALDFLPLRGRLELKERRLEALLLLLFLAALLALLLAL---GWWAVLLFWLLPLLVAGLLLGLRF 220

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542730 250 YLQHQNEDieVYEADEWGFVRGqtqTIDRHWGFGLDNIMHNItNGHVAHHfFFTKIPHYHLLEATPAIKKALE 322
Cdd:COG3239 221 YLEHRGED--TGDGEYRDQLLG---SRNIRGGRLLRWLFGNL-NYHIEHH-LFPSIPWYRLPEAHRILKELCP 286
PLN02598 PLN02598
omega-6 fatty acid desaturase
 75-339 9.89e-23

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 98.74  E-value: 9.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730   75 LGWYWAmGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDKGHPWVTEEDYN 154
Cdd:PLN02598 127 LAWAWL-GTAITGFFVIGHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNTHHAHTNKLVMDTAWQPFRPHQFD 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  155 NRTAIEKyFAVIPISGWLRWnpiYTIVGlpdgsHFWPW----SRLFETTEDRVKCAVSGVAcaicAYIAFVLCDYSVYT- 229
Cdd:PLN02598 206 NADPLRK-AMMRAGMGPLWW---WASIG-----HWLFWhfdlNKFRPQEVPRVKISLAAVF----AFMALGLPPLLYTTg 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  230 ---FVKYYYIPLLFQGLILVIITYLQHQNEDIEVYEADEWGFVRGQTQ-TIDRHWGFGLDNIMHNItNGHVAHHfFFTKI 305
Cdd:PLN02598 273 pvgFVKWWLMPWLGYHFWMSTFTMVHHTAPHIPFKQAREWNAAQAQLNgTVHCDYPAWIEFLCHDI-SVHIPHH-ISSKI 350

                        250       260       270
                 ....*....|....*....|....*....|....
gi 17542730  306 PHYHLleatpaiKKALEPLKDTQYGYKREVNYNW 339
Cdd:PLN02598 351 PSYNL-------RKAHASLQENWGKHLNKATFNW 377
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 71-142 2.44e-15

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: 71.73  E-value: 2.44e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542730  71 WIGLLGWYWAMGIvgsALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKD 142
Cdd:cd01060   1 LLLALLLGLLGGL---GLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKD 69
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 70-323 8.08e-15

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: 73.53  E-value: 8.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730    70 GWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSD----YEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDkgh 145
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKD--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730   146 PWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLPDGSHFWPWSRLFETTEDRVKCAVSGVACAICAYIAFVLcdY 225
Cdd:pfam00487  78 PDTAPLASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLG--L 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730   226 SVYTFVKYYYIPLLFQGLILVIITYLQHQnedievyeADEWGFVRGQTQTiDRHWGFGLDNIMHNITNGHVAHHfFFTKI 305
Cdd:pfam00487 156 GGLLLLLWLLPLLVFGFLLALIFNYLEHY--------GGDWGERPVETTR-SIRSPNWWLNLLTGNLNYHIEHH-LFPGV 225

                         250
                  ....*....|....*...
gi 17542730   306 PHYHLLEATPAIKKALEP 323
Cdd:pfam00487 226 PWYRLPKLHRRLREALPE 243
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 75-319 2.27e-12

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: 65.36  E-value: 2.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  75 LGWYWAMGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDkghpwvteEDyn 154
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHD--------PD-- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 155 nrtaiekyfavIPISGWLRWNPIYtivglPDGSHFWPWSRLFETTedrvkcavsgvacaicaYIAFVLCdysvyTFVKYY 234
Cdd:cd03506  71 -----------IDTLPLLARSEPA-----FGKDQKKRFLHRYQHF-----------------YFFPLLA-----LLLLAF 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 235 YIPLLFQGLILVIITYLQHQNEDIEVYEADEWG-FVRGQTQ-TIDRHWGFGLDNIMHNItNGHVAHHFFFTkIPHYHLLE 312
Cdd:cd03506 113 LVVQLAGGLWLAVVFQLNHFGMPVEDPPGESKNdWLERQVLtTRNITGSPFLDWLHGGL-NYQIEHHLFPT-MPRHNYPK 190


                ....*..
gi 17542730 313 ATPAIKK 319
Cdd:cd03506 191 VAPLVRE 197
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 70-309 3.70e-10

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: 60.08  E-value: 3.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  70 GWIGLLGWYWAM------GIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDk 143
Cdd:cd03511  34 LIAWTWGSWWALpaflvyGVLYAALFARWHECVHGTAFATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRYTQIPGRD- 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 144 ghPWVTEEDYNNRTAIEKYFAVIPisGWLR-----WNPIYTIVGLpDGSHFWP---WSRLFEttEDRVKCAVSGVACAIC 215
Cdd:cd03511 113 --PELAVPRPPTLREYLLALSGLP--YWWGklrtvFRHAFGAVSE-AEKPFIPaeeRPKVVR--EARAMLAVYAGLIALS 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730 216 AYIAFVLcdysvytFVKYYYIPLLFQGLILVIITYLQHQNEDievyeADEWGFVRgqTQTIDRHWGFGLdnIMHNItNGH 295
Cdd:cd03511 186 LYLGSPL-------LVLVWGLPLLLGQPILRLFLLAEHGGCP-----EDANDLRN--TRTTLTNPPLRF--LYWNM-PYH 248

                       250
                ....*....|....*...
gi 17542730 296 VAHHFF----FTKIPHYH 309
Cdd:cd03511 249 AEHHMYpsvpFHALPKLH 266
DUF3474 pfam11960
Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. ...
 26-58 9.46e-08

Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 126 to 140 amino acids in length. This domain is found associated with pfam00487.


Pssm-ID: 403244  Cd Length: 127  Bit Score: 50.50  E-value: 9.46e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 17542730    26 AAVKAAIPEHCFVKDPLTSISYLIKDYVLLAGL 58
Cdd:pfam11960  93 ADIRAAIPKHCWVKDPWRSMSYVVRDVAVVFGL 125
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 72-136 8.54e-07

This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in Bradyrhizobium japonicum USDA110, and other related proteins. Dihydrorhizobitoxine desaturase is reported to be involved in the final step of rhizobitoxine biosynthesis. 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, 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 homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239587 [Multi-domain]  Cd Length: 175  Bit Score: 48.82  E-value: 8.54e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542730  72 IGLLGWYW-----AMGIVGS---ALFCVGHDCGHGSFSDYEWLNDLCGH-LAHAPILAPFWPWQKSHRQHHQYT 136
Cdd:cd03510  11 LALAWPNWlayllAVLLIGArqrALAILMHDAAHGLLFRNRRLNDFLGNwLAAVPIFQSLAAYRRSHLKHHRHL 84
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
 58-145 1.06e-06

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: 48.90  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542730  58 LYFAVPYIEHYLGWIGLLGWYWAM-------GIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHR 130
Cdd:cd03514   1 LLFLISMALVWLSTWGYVISYLPLwvcfilnTLSLHLAGTVIHDASHKAASRNRWINELIGHVSAFFLGFPFPVFRRVHM 80

                        90
                ....*....|....*
gi 17542730 131 QHHQYTSHVEKDKGH 145
Cdd:cd03514  81 QHHAHTNDPEKDPDH 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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