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Conserved domains on  [gi|15227683|ref|NP_180559|]
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fatty acid desaturase 3 [Arabidopsis thaliana]

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 ...
 12-382 0e+00

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 PLN02498:

Pssm-ID: 445012 [Multi-domain]  Cd Length: 450  Bit Score: 639.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   12 NGDPGAGDRKKEERFDPSAQPPFKIGDIRAAIPKHCWVKSPLRSMSYVVRDIIAVAALAIAAVYVDSWFLWPLYWAAQGT 91
Cdd:PLN02498  80 EEGVNGVGEDEEGEFDPGAPPPFNLADIRAAIPKHCWVKNPWRSMSYVVRDVAVVFGLAAAAAYFNNWVVWPLYWFAQGT 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   92 LFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWVPLPERVYKKLPHSTRML 171
Cdd:PLN02498 160 MFWALFVLGHDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLSEKIYKSLDKVTRTL 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  172 RYTVPLPMLAYPLYLCYRSPGKEGSHFNPYSSLFAPSERKLIATSTTCWSIMFVSLIALSFVFGPLAVLKVYGVPYIIFV 251
Cdd:PLN02498 240 RFTLPFPMLAYPFYLWSRSPGKKGSHFHPDSDLFVPKERKDVITSTACWTAMAALLVCLSFVMGPIQMLKLYGIPYWIFV 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  252 MWLDAVTYLHHHGHDEKLPWYRGKEWSYLRGGLTTIDRDYGIFNNIHHDIGTHVIHHLFPQIPHYHLVDATKAAKHVLGR 331
Cdd:PLN02498 320 MWLDFVTYLHHHGHEDKLPWYRGKEWSYLRGGLTTLDRDYGWINNIHHDIGTHVIHHLFPQIPHYHLVEATEAAKPVLGK 399

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15227683  332 YYREPKTSGAIPIHLVESLVASIKKDHYVSDTGDIVFYETDPDLYVYASDK 382
Cdd:PLN02498 400 YYREPKKSGPLPFHLLGSLIRSMKQDHYVSDTGDVVYYQTDPQLSGSSKEE 450
 
Name Accession Description Interval E-value
PLN02498 PLN02498
omega-3 fatty acid desaturase
 12-382 0e+00

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 639.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   12 NGDPGAGDRKKEERFDPSAQPPFKIGDIRAAIPKHCWVKSPLRSMSYVVRDIIAVAALAIAAVYVDSWFLWPLYWAAQGT 91
Cdd:PLN02498  80 EEGVNGVGEDEEGEFDPGAPPPFNLADIRAAIPKHCWVKNPWRSMSYVVRDVAVVFGLAAAAAYFNNWVVWPLYWFAQGT 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   92 LFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWVPLPERVYKKLPHSTRML 171
Cdd:PLN02498 160 MFWALFVLGHDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLSEKIYKSLDKVTRTL 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  172 RYTVPLPMLAYPLYLCYRSPGKEGSHFNPYSSLFAPSERKLIATSTTCWSIMFVSLIALSFVFGPLAVLKVYGVPYIIFV 251
Cdd:PLN02498 240 RFTLPFPMLAYPFYLWSRSPGKKGSHFHPDSDLFVPKERKDVITSTACWTAMAALLVCLSFVMGPIQMLKLYGIPYWIFV 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  252 MWLDAVTYLHHHGHDEKLPWYRGKEWSYLRGGLTTIDRDYGIFNNIHHDIGTHVIHHLFPQIPHYHLVDATKAAKHVLGR 331
Cdd:PLN02498 320 MWLDFVTYLHHHGHEDKLPWYRGKEWSYLRGGLTTLDRDYGWINNIHHDIGTHVIHHLFPQIPHYHLVEATEAAKPVLGK 399

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15227683  332 YYREPKTSGAIPIHLVESLVASIKKDHYVSDTGDIVFYETDPDLYVYASDK 382
Cdd:PLN02498 400 YYREPKKSGPLPFHLLGSLIRSMKQDHYVSDTGDVVYYQTDPQLSGSSKEE 450
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 50-318 1.86e-76

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: 235.58  E-value: 1.86e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  50 KSPLRSMSYVVRDIIAVAALAIAAVYVDSWFLWPLYWAAQGTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVP 129
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSPLLVP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 130 YHGWRISHRTHHQNHGHVENDESWVPLPERVYKKLPHSTRMLRYTVPLPML--AYPLYLcyrspgkegsHFNpysslfap 207
Cdd:cd03507  81 YHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLslGWPYYL----------LLN-------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 208 serkliatsttcwsimfvslialsfvfgplaVLKVYGVPYIIFVMWLDAVTYLHHhgHDEKLPWYRGKEWSYLRGGL--T 285
Cdd:cd03507 143 -------------------------------VLLYYLIPYLVVNAWLVLITYLQH--TFPDIPWYRADEWNFAQAGLlgT 189

                       250       260       270
                ....*....|....*....|....*....|...
gi 15227683 286 TIDRDYGIFNNIHHDIGTHVIHHLFPQIPHYHL 318
Cdd:cd03507 190 VDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
78-333 1.05e-43

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 154.12  E-value: 1.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  78 SWFLWPLyWAAQGTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDeswvplP 157
Cdd:COG3239  54 SWLALLA-ALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKD------P 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 158 ERVYKKLPHSTRMLRYTVPLPMLAYPLYLCYRSpgkeGSHFNPYSSLFAPSERKLiatSTTCWSIMFVSLIALSFVFGPL 237
Cdd:COG3239 127 DIGYGVQAWRPLYLFQHLLRFFLLGLGGLYWLL----ALDFLPLRGRLELKERRL---EALLLLLFLAALLALLLALGWW 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 238 AVLKVYGVPYIIFVMWLDAVTYLHHHGHDEKLPwyrgkewSYLRGGLTTIDRDYG-IFNNIHHDIGTHVIHHLFPQIPHY 316
Cdd:COG3239 200 AVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDG-------EYRDQLLGSRNIRGGrLLRWLFGNLNYHIEHHLFPSIPWY 272

                       250
                ....*....|....*..
gi 15227683 317 HLVDATKAAKHVLGRYY 333
Cdd:COG3239 273 RLPEAHRILKELCPEYG 289
DUF3474 pfam11960
Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. ...
 13-62 1.75e-25

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: 99.80  E-value: 1.75e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15227683    13 GDPGAGDRKKEERFDPSAQPPFKIGDIRAAIPKHCWVKSPLRSMSYVVRD 62
Cdd:pfam11960  69 TNGFNGVGEEEEEFDPGAPPPFKLADIRAAIPKHCWVKDPWRSMSYVVRD 118
 
Name Accession Description Interval E-value
PLN02498 PLN02498
omega-3 fatty acid desaturase
 12-382 0e+00

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 639.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   12 NGDPGAGDRKKEERFDPSAQPPFKIGDIRAAIPKHCWVKSPLRSMSYVVRDIIAVAALAIAAVYVDSWFLWPLYWAAQGT 91
Cdd:PLN02498  80 EEGVNGVGEDEEGEFDPGAPPPFNLADIRAAIPKHCWVKNPWRSMSYVVRDVAVVFGLAAAAAYFNNWVVWPLYWFAQGT 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   92 LFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWVPLPERVYKKLPHSTRML 171
Cdd:PLN02498 160 MFWALFVLGHDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLSEKIYKSLDKVTRTL 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  172 RYTVPLPMLAYPLYLCYRSPGKEGSHFNPYSSLFAPSERKLIATSTTCWSIMFVSLIALSFVFGPLAVLKVYGVPYIIFV 251
Cdd:PLN02498 240 RFTLPFPMLAYPFYLWSRSPGKKGSHFHPDSDLFVPKERKDVITSTACWTAMAALLVCLSFVMGPIQMLKLYGIPYWIFV 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  252 MWLDAVTYLHHHGHDEKLPWYRGKEWSYLRGGLTTIDRDYGIFNNIHHDIGTHVIHHLFPQIPHYHLVDATKAAKHVLGR 331
Cdd:PLN02498 320 MWLDFVTYLHHHGHEDKLPWYRGKEWSYLRGGLTTLDRDYGWINNIHHDIGTHVIHHLFPQIPHYHLVEATEAAKPVLGK 399

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15227683  332 YYREPKTSGAIPIHLVESLVASIKKDHYVSDTGDIVFYETDPDLYVYASDK 382
Cdd:PLN02498 400 YYREPKKSGPLPFHLLGSLIRSMKQDHYVSDTGDVVYYQTDPQLSGSSKEE 450
PLN02505 PLN02505
omega-6 fatty acid desaturase
 28-338 3.66e-94

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 286.58  E-value: 3.66e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   28 PSAQPPFKIGDIRAAIPKHCWVKSPLRSMSYVVRD-------IIAVAALAIAAVYVDSWFLWPLYWAAQGTLFWAIFVLG 100
Cdd:PLN02505  25 PSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDlliaallYYVATNYIPLLPGPLSYVAWPLYWAAQGCVLTGVWVIA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  101 HDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWVPlpeRVYKKLPHST--------RMLR 172
Cdd:PLN02505 105 HECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVP---KKKSALPWYSkylnnppgRLLH 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  173 YTVPLpMLAYPLYLCYRSPGKE----GSHFNPYSSLFAPSERKLIATSTTcwSIMFVS--LIALSFVFGPLAVLKVYGVP 246
Cdd:PLN02505 182 IVVQL-TLGWPLYLAFNVSGRPydrfACHFDPYSPIFNDRERLQIYISDA--GILAVSfgLYRLAAAKGLAWVLCVYGVP 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  247 YIIFVMWLDAVTYLHHhgHDEKLPWYRGKEWSYLRGGLTTIDRDYGIFNNIHHDIG-THVIHHLFPQIPHYHLVDATKAA 325
Cdd:PLN02505 259 LLIVNAFLVLITYLQH--THPALPHYDSSEWDWLRGALATVDRDYGILNKVFHNITdTHVAHHLFSTMPHYHAMEATKAI 336

                        330
                 ....*....|...
gi 15227683  326 KHVLGRYYREPKT 338
Cdd:PLN02505 337 KPILGEYYQFDGT 349
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 50-318 1.86e-76

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: 235.58  E-value: 1.86e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  50 KSPLRSMSYVVRDIIAVAALAIAAVYVDSWFLWPLYWAAQGTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVP 129
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSPLLVP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 130 YHGWRISHRTHHQNHGHVENDESWVPLPERVYKKLPHSTRMLRYTVPLPML--AYPLYLcyrspgkegsHFNpysslfap 207
Cdd:cd03507  81 YHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLslGWPYYL----------LLN-------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 208 serkliatsttcwsimfvslialsfvfgplaVLKVYGVPYIIFVMWLDAVTYLHHhgHDEKLPWYRGKEWSYLRGGL--T 285
Cdd:cd03507 143 -------------------------------VLLYYLIPYLVVNAWLVLITYLQH--TFPDIPWYRADEWNFAQAGLlgT 189

                       250       260       270
                ....*....|....*....|....*....|...
gi 15227683 286 TIDRDYGIFNNIHHDIGTHVIHHLFPQIPHYHL 318
Cdd:cd03507 190 VDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
78-333 1.05e-43

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 154.12  E-value: 1.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  78 SWFLWPLyWAAQGTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDeswvplP 157
Cdd:COG3239  54 SWLALLA-ALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKD------P 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 158 ERVYKKLPHSTRMLRYTVPLPMLAYPLYLCYRSpgkeGSHFNPYSSLFAPSERKLiatSTTCWSIMFVSLIALSFVFGPL 237
Cdd:COG3239 127 DIGYGVQAWRPLYLFQHLLRFFLLGLGGLYWLL----ALDFLPLRGRLELKERRL---EALLLLLFLAALLALLLALGWW 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 238 AVLKVYGVPYIIFVMWLDAVTYLHHHGHDEKLPwyrgkewSYLRGGLTTIDRDYG-IFNNIHHDIGTHVIHHLFPQIPHY 316
Cdd:COG3239 200 AVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDG-------EYRDQLLGSRNIRGGrLLRWLFGNLNYHIEHHLFPSIPWY 272

                       250
                ....*....|....*..
gi 15227683 317 HLVDATKAAKHVLGRYY 333
Cdd:COG3239 273 RLPEAHRILKELCPEYG 289
PLN02598 PLN02598
omega-6 fatty acid desaturase
 79-335 3.92e-34

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 130.71  E-value: 3.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   79 WFLWPLYWAAQGTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWVPLPE 158
Cdd:PLN02598 122 WYLLPLAWAWLGTAITGFFVIGHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNTHHAHTNKLVMDTAWQPFRP 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  159 RVYKKLPHSTRML-RYTV-PL-PMLAYPLYLCYrspgkegsHFNpySSLFAPSERKLIATSTTC-WSIMFVSLIALSFVF 234
Cdd:PLN02598 202 HQFDNADPLRKAMmRAGMgPLwWWASIGHWLFW--------HFD--LNKFRPQEVPRVKISLAAvFAFMALGLPPLLYTT 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  235 GPLAVLKVYGVPYIIFVMWLDAVTYLHHHGhdEKLPWYRGKEWSYLRGGLT-TIDRDYGIFNNI-HHDIGTHVIHHLFPQ 312
Cdd:PLN02598 272 GPVGFVKWWLMPWLGYHFWMSTFTMVHHTA--PHIPFKQAREWNAAQAQLNgTVHCDYPAWIEFlCHDISVHIPHHISSK 349

                        250       260
                 ....*....|....*....|...
gi 15227683  313 IPHYHLVDATKAAKHVLGRYYRE 335
Cdd:PLN02598 350 IPSYNLRKAHASLQENWGKHLNK 372
DUF3474 pfam11960
Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. ...
 13-62 1.75e-25

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: 99.80  E-value: 1.75e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15227683    13 GDPGAGDRKKEERFDPSAQPPFKIGDIRAAIPKHCWVKSPLRSMSYVVRD 62
Cdd:pfam11960  69 TNGFNGVGEEEEEFDPGAPPPFKLADIRAAIPKHCWVKDPWRSMSYVVRD 118
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 78-333 1.28e-21

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: 92.79  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683    78 SWFLWPLYWAAQGTLFWAIFVLGHDCGHGSFSDIPL----LNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESW 153
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRlnrwLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   154 VPLPervykkLPHSTRMLRYTVPLPMLAYPLYLCYRSPGKEGSHFNPYSSLFAPSERKLIATSttcWSIMFVSLIALSFV 233
Cdd:pfam00487  81 APLA------SRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIA---WLLLLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683   234 FGPLAVL--KVYGVPYIIFVMWLDAV-TYLHHHGHDEKLPWYRGkewsylrggLTTIDRDYGIFNNIHHDIGTHVIHHLF 310
Cdd:pfam00487 152 FLGLGGLllLLWLLPLLVFGFLLALIfNYLEHYGGDWGERPVET---------TRSIRSPNWWLNLLTGNLNYHIEHHLF 222

                         250       260
                  ....*....|....*....|...
gi 15227683   311 PQIPHYHLVDATKAAKHVLGRYY 333
Cdd:pfam00487 223 PGVPWYRLPKLHRRLREALPEHG 245
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 79-154 1.16e-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: 69.81  E-value: 1.16e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227683  79 WFLWPLYWAAQGtlfWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWV 154
Cdd:cd01060   1 LLLALLLGLLGG---LGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKDPDSA 73
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 78-334 3.76e-11

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: 63.16  E-value: 3.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  78 SWFLWPLYWAaQGTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDeswvplP 157
Cdd:cd03511  41 SWWALPAFLV-YGVLYAALFARWHECVHGTAFATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRYTQIPGRD------P 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 158 ERVYKKLPHSTRMLRYTVPLPMLAYPLYLCYRSP----GKEGSHFNPysslfaPSERKLIATSTTCWSIMFVSLIALSFV 233
Cdd:cd03511 114 ELAVPRPPTLREYLLALSGLPYWWGKLRTVFRHAfgavSEAEKPFIP------AEERPKVVREARAMLAVYAGLIALSLY 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 234 FGPLAVLKVYGVPYIIFVMWLDAVTYLHHHGHDEKLPWYRGKewsylRGGLTTidrdyGIFNNIHHDIGTHVIHHLFPQI 313
Cdd:cd03511 188 LGSPLLVLVWGLPLLLGQPILRLFLLAEHGGCPEDANDLRNT-----RTTLTN-----PPLRFLYWNMPYHAEHHMYPSV 257

                       250       260
                ....*....|....*....|.
gi 15227683 314 PHYHLVDATKAAKHVLGRYYR 334
Cdd:cd03511 258 PFHALPKLHELIKDDLPVPYP 278
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 92-318 1.86e-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: 54.18  E-value: 1.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683  92 LFWAIFV-LGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWVPLPERVYKKLPHSTRM 170
Cdd:cd03506   9 LFWAQGGfLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLARSEPAFGKDQ 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 171 LRYtvplPMLAYPLYLCYrspgkegshfnpysslfapserkliatsttcwsimfvslialsFVFGPLAVlkVYGVPYIIF 250
Cdd:cd03506  89 KKR----FLHRYQHFYFF-------------------------------------------PLLALLLL--AFLVVQLAG 119

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227683 251 VMWLDAVTYLHHHGHD-EKLPWYRGKEWsYLRGGLTTIDRDYGIFNNIHH-DIGTHVIHHLFPQIPHYHL 318
Cdd:cd03506 120 GLWLAVVFQLNHFGMPvEDPPGESKNDW-LERQVLTTRNITGSPFLDWLHgGLNYQIEHHLFPTMPRHNY 188
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 79-145 7.61e-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: 36.88  E-value: 7.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227683  79 WFLWPLYWAAQ---GTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSF-ILVPYHGWRISHRTHHQNHG 145
Cdd:cd03510  15 WPNWLAYLLAVlliGARQRALAILMHDAAHGLLFRNRRLNDFLGNWLAAVpIFQSLAAYRRSHLKHHRHLG 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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