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Conserved domains on  [gi|697090126|ref|XP_009657969|]
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Delta(12) fatty acid desaturase [Verticillium dahliae VdLs.17]

Protein Classification

fatty acid desaturase family protein( domain architecture ID 1056)

fatty acid desaturase (FADS) family protein similar to membrane FADSs, which are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains, and to beta-carotene ketolase/oxygenases (CrtW-like) and hydroxylases (CrtR-like)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Membrane-FADS-like super family cl00615
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 35-402 3.49e-118

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.


The actual alignment was detected with superfamily member PLN02505:

Pssm-ID: 445012  Cd Length: 381  Bit Score: 348.60  E-value: 3.49e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  35 IRNTIPAHCFEPSLWTSFYYVFRDLSMVTGLVWAALTFIPTIPnAYLRFAAWMVYGFVQGLVCTGVWILGHECGHGAFST 114
Cdd:PLN02505  36 IKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLP-GPLSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 115 HTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKDMAFVPATKapvSRLPSFLANLNlhelfedTPLAQLVPLIF 194
Cdd:PLN02505 115 YQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKK---SALPWYSKYLN-------NPPGRLLHIVV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 195 HQLFGWQAYLFFNVTaGKgskqsepsglgKYFR-VSHFEPTSAVFRSTEALYVAITDVGLALMFTALYYATQALDLSTVL 273
Cdd:PLN02505 185 QLTLGWPLYLAFNVS-GR-----------PYDRfACHFDPYSPIFNDRERLQIYISDAGILAVSFGLYRLAAAKGLAWVL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 274 FLYAVPYFWVHHWLVAITYLHHNHPDVPHFNEEGWTFVKGALATVDREFGFIgKHLFHGIIEKHVVHHLFPRIPFYKADE 353
Cdd:PLN02505 253 CVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGIL-NKVFHNITDTHVAHHLFSTMPHYHAME 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 697090126 354 ATEAMKPLLGDLYIRDDRSFLGQLWSVFGTLQYVENDPDIKGNMrWVKN 402
Cdd:PLN02505 332 ATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPDEGGKGVF-WYNN 379
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
 35-402 3.49e-118

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 348.60  E-value: 3.49e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  35 IRNTIPAHCFEPSLWTSFYYVFRDLSMVTGLVWAALTFIPTIPnAYLRFAAWMVYGFVQGLVCTGVWILGHECGHGAFST 114
Cdd:PLN02505  36 IKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLP-GPLSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 115 HTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKDMAFVPATKapvSRLPSFLANLNlhelfedTPLAQLVPLIF 194
Cdd:PLN02505 115 YQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKK---SALPWYSKYLN-------NPPGRLLHIVV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 195 HQLFGWQAYLFFNVTaGKgskqsepsglgKYFR-VSHFEPTSAVFRSTEALYVAITDVGLALMFTALYYATQALDLSTVL 273
Cdd:PLN02505 185 QLTLGWPLYLAFNVS-GR-----------PYDRfACHFDPYSPIFNDRERLQIYISDAGILAVSFGLYRLAAAKGLAWVL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 274 FLYAVPYFWVHHWLVAITYLHHNHPDVPHFNEEGWTFVKGALATVDREFGFIgKHLFHGIIEKHVVHHLFPRIPFYKADE 353
Cdd:PLN02505 253 CVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGIL-NKVFHNITDTHVAHHLFSTMPHYHAME 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 697090126 354 ATEAMKPLLGDLYIRDDRSFLGQLWSVFGTLQYVENDPDIKGNMrWVKN 402
Cdd:PLN02505 332 ATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPDEGGKGVF-WYNN 379
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 47-351 1.81e-67

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: 213.24  E-value: 1.81e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  47 SLWTSFYYVFRDLSMVTGLVWAAltfiptipNAYLRFAAWMVYGFVQGLVCTGVWILGHECGHGAFSTHTRLNDCVGWVL 126
Cdd:cd03507    2 SLFRSLSYLAPDILLLALLALAA--------SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 127 HSFLLVPYFSWKFSHHRHHRFTGHMNKDMAFVPATKAPVSRLPSFLanlnlhelfedtPLAQLVPLIFHQLFGWQAYLFF 206
Cdd:cd03507   74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRL------------PYRLYRNPFLMLSLGWPYYLLL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 207 NvtagkgskqsepsglgkyfrvshfeptsavfrstealyvaitdvglalmftalyyatqaldlstVLFLYAVPYFWVHHW 286
Cdd:cd03507  142 N----------------------------------------------------------------VLLYYLIPYLVVNAW 157

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697090126 287 LVAITYLHHNHPDVPHFNEEGWTFVKGALA-TVDREFGFIGKHLFHgIIEKHVVHHLFPRIPFYKA 351
Cdd:cd03507  158 LVLITYLQHTFPDIPWYRADEWNFAQAGLLgTVDRDYGGWLNWLTH-IIGTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
31-387 3.80e-27

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 109.82  E-value: 3.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  31 DIQTIRNTIPAHcFEPSLWTSFYYVFRDLSMVtGLVWAALTFiptipnAYLRFAAWMVYGFVQglvcTGVWILGHECGHG 110
Cdd:COG3239   14 ELRALRARLRAL-LGRRDWRYLLKLALTLALL-AALWLLLSW------SWLALLAALLLGLAL----AGLFSLGHDAGHG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 111 AFSTHTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKD--MAFVPATKAPVSRLPSFLANlnlhelfedtplaq 188
Cdd:COG3239   82 SLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDpdIGYGVQAWRPLYLFQHLLRF-------------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 189 lvPLIFHQLFGWQAYLFFNVTAGKGSKQSEPSGLgkyfrvshfeptsavfrstealyvaitdVGLALMFTALYYATQALD 268
Cdd:COG3239  148 --FLLGLGGLYWLLALDFLPLRGRLELKERRLEA----------------------------LLLLLFLAALLALLLALG 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 269 LSTVLFLYAVPYFWVHHWLVAITYLHHNHPDVPHFNeegwtFVKGALATVDREFGFIGKHLFHGiIEKHVVHHLFPRIPF 348
Cdd:COG3239  198 WWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGE-----YRDQLLGSRNIRGGRLLRWLFGN-LNYHIEHHLFPSIPW 271

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 697090126 349 YKADEATEAMKPLLGDLYIRDDR-SFLGQLWSVFGTLQYV 387
Cdd:COG3239  272 YRLPEAHRILKELCPEYGLPYTEgSLLRSYREVLRLLRRL 311
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 79-368 2.24e-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: 69.68  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126   79 AYLRFAAWMVYGFVQGLVCtgvWILGHECGHGAFSTHTR----LNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKD 154
Cdd:pfam00487   1 SWLALLLALLLGLFLLGIT---GSLAHEASHGALFKKRRlnrwLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  155 mafvPATKAPVSRLPSFLANLnlhelfedtplaqLVPLIFHQLFGWQAYLFFNVTAgkgskqsepsglgkyFRVSHFEPT 234
Cdd:pfam00487  78 ----PDTAPLASRFRGLLRYL-------------LRWLLGLLVLAWLLALVLPLWL---------------RRLARRKRP 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  235 SAVFRSTEALYVAITDVGLALMFTALYYATQALDLSTVLFLYAVPYFWVHHWLvaiTYLHHNHPDVPHFNEEgwtfvkgA 314
Cdd:pfam00487 126 IKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLLWLLPLLVFGFLLALIF---NYLEHYGGDWGERPVE-------T 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 697090126  315 LATVDREFGFIGkhLFHGIIEKHVVHHLFPRIPFYKADEATEAMKPLLGDLYIR 368
Cdd:pfam00487 196 TRSIRSPNWWLN--LLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREALPEHGLP 247
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
 35-402 3.49e-118

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 348.60  E-value: 3.49e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  35 IRNTIPAHCFEPSLWTSFYYVFRDLSMVTGLVWAALTFIPTIPnAYLRFAAWMVYGFVQGLVCTGVWILGHECGHGAFST 114
Cdd:PLN02505  36 IKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLP-GPLSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 115 HTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKDMAFVPATKapvSRLPSFLANLNlhelfedTPLAQLVPLIF 194
Cdd:PLN02505 115 YQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKK---SALPWYSKYLN-------NPPGRLLHIVV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 195 HQLFGWQAYLFFNVTaGKgskqsepsglgKYFR-VSHFEPTSAVFRSTEALYVAITDVGLALMFTALYYATQALDLSTVL 273
Cdd:PLN02505 185 QLTLGWPLYLAFNVS-GR-----------PYDRfACHFDPYSPIFNDRERLQIYISDAGILAVSFGLYRLAAAKGLAWVL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 274 FLYAVPYFWVHHWLVAITYLHHNHPDVPHFNEEGWTFVKGALATVDREFGFIgKHLFHGIIEKHVVHHLFPRIPFYKADE 353
Cdd:PLN02505 253 CVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGIL-NKVFHNITDTHVAHHLFSTMPHYHAME 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 697090126 354 ATEAMKPLLGDLYIRDDRSFLGQLWSVFGTLQYVENDPDIKGNMrWVKN 402
Cdd:PLN02505 332 ATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPDEGGKGVF-WYNN 379
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 47-351 1.81e-67

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: 213.24  E-value: 1.81e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  47 SLWTSFYYVFRDLSMVTGLVWAAltfiptipNAYLRFAAWMVYGFVQGLVCTGVWILGHECGHGAFSTHTRLNDCVGWVL 126
Cdd:cd03507    2 SLFRSLSYLAPDILLLALLALAA--------SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 127 HSFLLVPYFSWKFSHHRHHRFTGHMNKDMAFVPATKAPVSRLPSFLanlnlhelfedtPLAQLVPLIFHQLFGWQAYLFF 206
Cdd:cd03507   74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRL------------PYRLYRNPFLMLSLGWPYYLLL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 207 NvtagkgskqsepsglgkyfrvshfeptsavfrstealyvaitdvglalmftalyyatqaldlstVLFLYAVPYFWVHHW 286
Cdd:cd03507  142 N----------------------------------------------------------------VLLYYLIPYLVVNAW 157

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697090126 287 LVAITYLHHNHPDVPHFNEEGWTFVKGALA-TVDREFGFIGKHLFHgIIEKHVVHHLFPRIPFYKA 351
Cdd:cd03507  158 LVLITYLQHTFPDIPWYRADEWNFAQAGLLgTVDRDYGGWLNWLTH-IIGTHVAHHLFPRIPHYNL 222
PLN02498 PLN02498
omega-3 fatty acid desaturase
 35-372 6.42e-54

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 185.03  E-value: 6.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  35 IRNTIPAHCFEPSLWTSFYYVFRDLSMVTGLVWAAltfiptipnAYL-RFAAWMVYGFVQGLVCTGVWILGHECGHGAFS 113
Cdd:PLN02498 107 IRAAIPKHCWVKNPWRSMSYVVRDVAVVFGLAAAA---------AYFnNWVVWPLYWFAQGTMFWALFVLGHDCGHGSFS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 114 THTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKDMAFVPATKAPVSRLPSFLANLNLHELFedtplaqlvPLI 193
Cdd:PLN02498 178 NNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLSEKIYKSLDKVTRTLRFTLPF---------PML 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 194 FHQLFGWqaylffNVTAGKGSkqsepsglgkyfrvSHFEPTSAVFRSTEALYVAITDVGLALMFTALYYATQALDLSTVL 273
Cdd:PLN02498 249 AYPFYLW------SRSPGKKG--------------SHFHPDSDLFVPKERKDVITSTACWTAMAALLVCLSFVMGPIQML 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 274 FLYAVPYFWVHHWLVAITYLHHN-HPD-VPHFNEEGWTFVKGALATVDREFGFIGKhlFHGIIEKHVVHHLFPRIPFYKA 351
Cdd:PLN02498 309 KLYGIPYWIFVMWLDFVTYLHHHgHEDkLPWYRGKEWSYLRGGLTTLDRDYGWINN--IHHDIGTHVIHHLFPQIPHYHL 386

                        330       340
                 ....*....|....*....|.
gi 697090126 352 DEATEAMKPLLGDLYIRDDRS 372
Cdd:PLN02498 387 VEATEAAKPVLGKYYREPKKS 407
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
31-387 3.80e-27

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 109.82  E-value: 3.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  31 DIQTIRNTIPAHcFEPSLWTSFYYVFRDLSMVtGLVWAALTFiptipnAYLRFAAWMVYGFVQglvcTGVWILGHECGHG 110
Cdd:COG3239   14 ELRALRARLRAL-LGRRDWRYLLKLALTLALL-AALWLLLSW------SWLALLAALLLGLAL----AGLFSLGHDAGHG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 111 AFSTHTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKD--MAFVPATKAPVSRLPSFLANlnlhelfedtplaq 188
Cdd:COG3239   82 SLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDpdIGYGVQAWRPLYLFQHLLRF-------------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 189 lvPLIFHQLFGWQAYLFFNVTAGKGSKQSEPSGLgkyfrvshfeptsavfrstealyvaitdVGLALMFTALYYATQALD 268
Cdd:COG3239  148 --FLLGLGGLYWLLALDFLPLRGRLELKERRLEA----------------------------LLLLLFLAALLALLLALG 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 269 LSTVLFLYAVPYFWVHHWLVAITYLHHNHPDVPHFNeegwtFVKGALATVDREFGFIGKHLFHGiIEKHVVHHLFPRIPF 348
Cdd:COG3239  198 WWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGE-----YRDQLLGSRNIRGGRLLRWLFGN-LNYHIEHHLFPSIPW 271

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 697090126 349 YKADEATEAMKPLLGDLYIRDDR-SFLGQLWSVFGTLQYV 387
Cdd:COG3239  272 YRLPEAHRILKELCPEYGLPYTEgSLLRSYREVLRLLRRL 311
PLN02598 PLN02598
omega-6 fatty acid desaturase
 79-359 2.14e-16

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 80.25  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  79 AYLRFAAWMVYGFV---QGLVCTGVWILGHECGHGAFSTHTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKDM 155
Cdd:PLN02598 115 AAIAVAPWYLLPLAwawLGTAITGFFVIGHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNTHHAHTNKLVMDT 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 156 AFVPATKAPVSRLPSFLANLNLHELFEDTPLAQlvplIFHQLFgWqaylffnvtagkgskqsepsglgkYFRVSHFEP-- 233
Cdd:PLN02598 195 AWQPFRPHQFDNADPLRKAMMRAGMGPLWWWAS----IGHWLF-W------------------------HFDLNKFRPqe 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 234 TSAVFRSTEALYVAitdvgLALMFTALYYATQALDLstvLFLYAVPYFWVHHWLVAITYLHHNHPDVPHFNEEGWTFVKG 313
Cdd:PLN02598 246 VPRVKISLAAVFAF-----MALGLPPLLYTTGPVGF---VKWWLMPWLGYHFWMSTFTMVHHTAPHIPFKQAREWNAAQA 317

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 697090126 314 ALA-TVDREFGFIGKHLFHGiIEKHVVHHLFPRIPFYKADEATEAMK 359
Cdd:PLN02598 318 QLNgTVHCDYPAWIEFLCHD-ISVHIPHHISSKIPSYNLRKAHASLQ 363
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 83-154 2.38e-14

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: 69.04  E-value: 2.38e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697090126  83 FAAWMVYGFVQGLvctGVWILGHECGHGAFSTHTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKD 154
Cdd:cd01060    1 LLLALLLGLLGGL---GLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKD 69
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 79-368 2.24e-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: 69.68  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126   79 AYLRFAAWMVYGFVQGLVCtgvWILGHECGHGAFSTHTR----LNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKD 154
Cdd:pfam00487   1 SWLALLLALLLGLFLLGIT---GSLAHEASHGALFKKRRlnrwLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  155 mafvPATKAPVSRLPSFLANLnlhelfedtplaqLVPLIFHQLFGWQAYLFFNVTAgkgskqsepsglgkyFRVSHFEPT 234
Cdd:pfam00487  78 ----PDTAPLASRFRGLLRYL-------------LRWLLGLLVLAWLLALVLPLWL---------------RRLARRKRP 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  235 SAVFRSTEALYVAITDVGLALMFTALYYATQALDLSTVLFLYAVPYFWVHHWLvaiTYLHHNHPDVPHFNEEgwtfvkgA 314
Cdd:pfam00487 126 IKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLLWLLPLLVFGFLLALIF---NYLEHYGGDWGERPVE-------T 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 697090126  315 LATVDREFGFIGkhLFHGIIEKHVVHHLFPRIPFYKADEATEAMKPLLGDLYIR 368
Cdd:pfam00487 196 TRSIRSPNWWLN--LLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREALPEHGLP 247
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 87-347 5.24e-08

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: 52.64  E-value: 5.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126  87 MVYGFVQGLVCTGVWILGHECGHGAFSTHTRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFTGHMNKDMafvpatkapvs 166
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHDP----------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 167 rlpsflaNLNLHELFEDTPLAQLVPLIFHQLFGWQAYLFFNVTAGkgskqsepsglgkyfrvshfeptsavfrstealyv 246
Cdd:cd03506   70 -------DIDTLPLLARSEPAFGKDQKKRFLHRYQHFYFFPLLAL----------------------------------- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697090126 247 aitdvglalmftalyyatqaldlstVLFLYAVPYFWVHHWLVAITYLHHN---HPDVPHFNEEGWtFVKGALATVDREFG 323
Cdd:cd03506  108 -------------------------LLLAFLVVQLAGGLWLAVVFQLNHFgmpVEDPPGESKNDW-LERQVLTTRNITGS 161

                        250       260
                 ....*....|....*....|....
gi 697090126 324 FIGkHLFHGIIEKHVVHHLFPRIP 347
Cdd:cd03506  162 PFL-DWLHGGLNYQIEHHLFPTMP 184
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 84-148 3.60e-06

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: 48.14  E-value: 3.60e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697090126  84 AAWMVYGFVQGLVCTGVWILGHECGHG-AFSTHtRLNDCVGWVLHSFLLVPYFSWKFSHHRHHRFT 148
Cdd:cd03511   42 WWALPAFLVYGVLYAALFARWHECVHGtAFATR-WLNDAVGQIAGLMILLPPDFFRWSHARHHRYT 106
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 81-149 4.06e-03

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: 38.03  E-value: 4.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697090126  81 LRFAAWMVYGFVQGLVCT---GVWILGHECGHGAFSTHTRLNDCVGWVLHSF-LLVPYFSWKFSHHRHHRFTG 149
Cdd:cd03510   13 LAWPNWLAYLLAVLLIGArqrALAILMHDAAHGLLFRNRRLNDFLGNWLAAVpIFQSLAAYRRSHLKHHRHLG 85
 
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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