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Conserved domains on  [gi|33238186|gb|AAQ00253|]
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Fatty acid desaturase [Prochlorococcus marinus subsp. marinus str. CCMP1375]

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 ...
 24-329 3.38e-57

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: 185.89  E-value: 3.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  24 RAFWQVSTTIIPVALLWILIAWIDqssfKTPFRALGLIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNRITGFLLGTL 103
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAA----SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 104 NAIPQYPWSRDHAFHHRHNGNWEvyrGPVDVITLEDYQALSKINQF-LYSISRHWLMLFPGGFFYLVIKprltlinaiah 182
Cdd:cd03507  77 LLVPYHSWRISHNRHHAHTGNLE---GDEVWVPVTEEEYAELPKRLpYRLYRNPFLMLSLGWPYYLLLN----------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 183 fiwsilvelcnkllkrdfanlfsfstrfqanysgygnssgelidliannviviiswilmsrwlgaglFWSCYSIIMTASA 262
Cdd:cd03507 143 -------------------------------------------------------------------VLLYYLIPYLVVN 155

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33238186 263 AIFICIFFVQHNFEGSYANGSNEWSAILGAVDGSSNLDIPRLLNWFLADISFHSMHHLCDRIPNYNL 329
Cdd:cd03507 156 AWLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
 
Name Accession Description Interval E-value
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 24-329 3.38e-57

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: 185.89  E-value: 3.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  24 RAFWQVSTTIIPVALLWILIAWIDqssfKTPFRALGLIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNRITGFLLGTL 103
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAA----SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 104 NAIPQYPWSRDHAFHHRHNGNWEvyrGPVDVITLEDYQALSKINQF-LYSISRHWLMLFPGGFFYLVIKprltlinaiah 182
Cdd:cd03507  77 LLVPYHSWRISHNRHHAHTGNLE---GDEVWVPVTEEEYAELPKRLpYRLYRNPFLMLSLGWPYYLLLN----------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 183 fiwsilvelcnkllkrdfanlfsfstrfqanysgygnssgelidliannviviiswilmsrwlgaglFWSCYSIIMTASA 262
Cdd:cd03507 143 -------------------------------------------------------------------VLLYYLIPYLVVN 155

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33238186 263 AIFICIFFVQHNFEGSYANGSNEWSAILGAVDGSSNLDIPRLLNWFLADISFHSMHHLCDRIPNYNL 329
Cdd:cd03507 156 AWLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
14-340 3.89e-38

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 139.09  E-value: 3.89e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  14 ITPYLKRSNARAFWQVSTTIIPVALLWILIAWidqssfktpfrALGLIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLN 93
Cdd:COG3239  22 LRALLGRRDWRYLLKLALTLALLAALWLLLSW-----------SWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  94 RITGFLLGTLNAIPQYPWSRDHAFHHRHNGNWEvyRGPVDVITLEDYQALSKINQFLYsisrhWLMLFPGGFFYLVIKPR 173
Cdd:COG3239  91 DLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPG--KDPDIGYGVQAWRPLYLFQHLLR-----FFLLGLGGLYWLLALDF 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 174 LtlinaiahfiwsilvelcnkllkrdfanlfsfstrfqaNYSGYGNSSGELIDLIANNVIVIISWILMSrWLGAGLFWSC 253
Cdd:COG3239 164 L--------------------------------------PLRGRLELKERRLEALLLLLFLAALLALLL-ALGWWAVLLF 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 254 YSIIMTASAAIFICIFFVQHNFEGSYANgsnewsAILGAVDGSSNLDIPRLLNWFLADISFHSMHHLCDRIPNYNLRACH 333
Cdd:COG3239 205 WLLPLLVAGLLLGLRFYLEHRGEDTGDG------EYRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAH 278


                ....*..
gi 33238186 334 IRNKHLL 340
Cdd:COG3239 279 RILKELC 285
PLN02598 PLN02598
omega-6 fatty acid desaturase
 24-334 1.40e-09

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 59.07  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186   24 RAFWQVSTTIIPVALLWILIAwidqssfKTPFRALGLipVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNRITGFLLGTL 103
Cdd:PLN02598  98 KAWKTVAITVTSYALGLAAIA-------VAPWYLLPL--AWAWLGTAITGFFVIGHDCGHNSFSKNQLVEDIVGTIAFTP 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  104 NAIPQYPWSRDHAFHHRHNgNWEVYRGPVDVITLEDYQALSKINQFLYSisrhwlmlfpggFFYLVIKPRLTLIN-AIAH 182
Cdd:PLN02598 169 LIYPFEPWRIKHNTHHAHT-NKLVMDTAWQPFRPHQFDNADPLRKAMMR------------AGMGPLWWWASIGHwLFWH 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  183 FIWSILVELCNKLLKRDFANLFSFStrfqanysgygnSSGELIDLIANNVIVIISWILMSrWLGAGLFWSCYSIimtasa 262
Cdd:PLN02598 236 FDLNKFRPQEVPRVKISLAAVFAFM------------ALGLPPLLYTTGPVGFVKWWLMP-WLGYHFWMSTFTM------ 296

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33238186  263 aificiffVQHNFEGSYANGSNEWSAILGAVDGSSNLDIPRLLNWFLADISFHSMHHLCDRIPNYNLRACHI 334
Cdd:PLN02598 297 --------VHHTAPHIPFKQAREWNAAQAQLNGTVHCDYPAWIEFLCHDISVHIPHHISSKIPSYNLRKAHA 360
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 58-340 4.29e-08

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: 53.50  E-value: 4.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186    58 LGLIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNR----ITGFLLGTLNAIPQYPWSRDHAFHHRHNGNwevyrGPVD 133
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRwlndLLGRLAGLPLGISYSAWRIAHLVHHRYTNG-----PDKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186   134 VITLEDYQALSKINQFLYsisRHWLMLFPGGFFYLVIKPrltlinaiahfiwsilvelcnkLLKRDFANLFSFSTRFQAN 213
Cdd:pfam00487  78 PDTAPLASRFRGLLRYLL---RWLLGLLVLAWLLALVLP----------------------LWLRRLARRKRPIKSRRRR 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186   214 YsgygnssgelidLIANNVIVIISWILMSrWLGAGLFWSCYSIIMTASAAIFICIFFVQHNFEGSYANGSNEWSAILGAV 293
Cdd:pfam00487 133 W------------RLIAWLLLLAAWLGLW-LGFLGLGGLLLLLWLLPLLVFGFLLALIFNYLEHYGGDWGERPVETTRSI 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 33238186   294 DgssnlDIPRLLNWFLADISFHSMHHLCDRIPNYNLRACHIRNKHLL 340
Cdd:pfam00487 200 R-----SPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREAL 241
 
Name Accession Description Interval E-value
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 24-329 3.38e-57

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: 185.89  E-value: 3.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  24 RAFWQVSTTIIPVALLWILIAWIDqssfKTPFRALGLIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNRITGFLLGTL 103
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAA----SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 104 NAIPQYPWSRDHAFHHRHNGNWEvyrGPVDVITLEDYQALSKINQF-LYSISRHWLMLFPGGFFYLVIKprltlinaiah 182
Cdd:cd03507  77 LLVPYHSWRISHNRHHAHTGNLE---GDEVWVPVTEEEYAELPKRLpYRLYRNPFLMLSLGWPYYLLLN----------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 183 fiwsilvelcnkllkrdfanlfsfstrfqanysgygnssgelidliannviviiswilmsrwlgaglFWSCYSIIMTASA 262
Cdd:cd03507 143 -------------------------------------------------------------------VLLYYLIPYLVVN 155

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33238186 263 AIFICIFFVQHNFEGSYANGSNEWSAILGAVDGSSNLDIPRLLNWFLADISFHSMHHLCDRIPNYNL 329
Cdd:cd03507 156 AWLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
14-340 3.89e-38

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 139.09  E-value: 3.89e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  14 ITPYLKRSNARAFWQVSTTIIPVALLWILIAWidqssfktpfrALGLIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLN 93
Cdd:COG3239  22 LRALLGRRDWRYLLKLALTLALLAALWLLLSW-----------SWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  94 RITGFLLGTLNAIPQYPWSRDHAFHHRHNGNWEvyRGPVDVITLEDYQALSKINQFLYsisrhWLMLFPGGFFYLVIKPR 173
Cdd:COG3239  91 DLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPG--KDPDIGYGVQAWRPLYLFQHLLR-----FFLLGLGGLYWLLALDF 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 174 LtlinaiahfiwsilvelcnkllkrdfanlfsfstrfqaNYSGYGNSSGELIDLIANNVIVIISWILMSrWLGAGLFWSC 253
Cdd:COG3239 164 L--------------------------------------PLRGRLELKERRLEALLLLLFLAALLALLL-ALGWWAVLLF 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 254 YSIIMTASAAIFICIFFVQHNFEGSYANgsnewsAILGAVDGSSNLDIPRLLNWFLADISFHSMHHLCDRIPNYNLRACH 333
Cdd:COG3239 205 WLLPLLVAGLLLGLRFYLEHRGEDTGDG------EYRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAH 278


                ....*..
gi 33238186 334 IRNKHLL 340
Cdd:COG3239 279 RILKELC 285
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 60-126 1.54e-12

The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane hydroxylases, beta carotene ketolases (CrtW-like), hydroxylases (CrtR-like), and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial, integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs, and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin, respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H, HXX(X)HH, and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition, the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase.


Pssm-ID: 238511 [Multi-domain]  Cd Length: 122  Bit Score: 63.64  E-value: 1.54e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33238186  60 LIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNRITGFLLGTLNAIPQYPWSRDHAFHHRHNGNWE 126
Cdd:cd01060   1 LLLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPG 67
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 19-121 7.27e-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: 59.31  E-value: 7.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  19 KRSNARAFWQVSTTIIPVALLWILIAWIDQSSFktpfrALGLIPVLAILTLLSsraFSLMHDCGHGSLFRSRRLNRITGF 98
Cdd:cd03511  11 QRSDAPGLLDTALWLGALAVSGILIAWTWGSWW-----ALPAFLVYGVLYAAL---FARWHECVHGTAFATRWLNDAVGQ 82

                        90       100
                ....*....|....*....|...
gi 33238186  99 LLGTLNAIPQYPWSRDHAFHHRH 121
Cdd:cd03511  83 IAGLMILLPPDFFRWSHARHHRY 105
PLN02598 PLN02598
omega-6 fatty acid desaturase
 24-334 1.40e-09

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 59.07  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186   24 RAFWQVSTTIIPVALLWILIAwidqssfKTPFRALGLipVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNRITGFLLGTL 103
Cdd:PLN02598  98 KAWKTVAITVTSYALGLAAIA-------VAPWYLLPL--AWAWLGTAITGFFVIGHDCGHNSFSKNQLVEDIVGTIAFTP 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  104 NAIPQYPWSRDHAFHHRHNgNWEVYRGPVDVITLEDYQALSKINQFLYSisrhwlmlfpggFFYLVIKPRLTLIN-AIAH 182
Cdd:PLN02598 169 LIYPFEPWRIKHNTHHAHT-NKLVMDTAWQPFRPHQFDNADPLRKAMMR------------AGMGPLWWWASIGHwLFWH 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  183 FIWSILVELCNKLLKRDFANLFSFStrfqanysgygnSSGELIDLIANNVIVIISWILMSrWLGAGLFWSCYSIimtasa 262
Cdd:PLN02598 236 FDLNKFRPQEVPRVKISLAAVFAFM------------ALGLPPLLYTTGPVGFVKWWLMP-WLGYHFWMSTFTM------ 296

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33238186  263 aificiffVQHNFEGSYANGSNEWSAILGAVDGSSNLDIPRLLNWFLADISFHSMHHLCDRIPNYNLRACHI 334
Cdd:PLN02598 297 --------VHHTAPHIPFKQAREWNAAQAQLNGTVHCDYPAWIEFLCHDISVHIPHHISSKIPSYNLRKAHA 360
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 58-340 4.29e-08

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: 53.50  E-value: 4.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186    58 LGLIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNR----ITGFLLGTLNAIPQYPWSRDHAFHHRHNGNwevyrGPVD 133
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRwlndLLGRLAGLPLGISYSAWRIAHLVHHRYTNG-----PDKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186   134 VITLEDYQALSKINQFLYsisRHWLMLFPGGFFYLVIKPrltlinaiahfiwsilvelcnkLLKRDFANLFSFSTRFQAN 213
Cdd:pfam00487  78 PDTAPLASRFRGLLRYLL---RWLLGLLVLAWLLALVLP----------------------LWLRRLARRKRPIKSRRRR 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186   214 YsgygnssgelidLIANNVIVIISWILMSrWLGAGLFWSCYSIIMTASAAIFICIFFVQHNFEGSYANGSNEWSAILGAV 293
Cdd:pfam00487 133 W------------RLIAWLLLLAAWLGLW-LGFLGLGGLLLLLWLLPLLVFGFLLALIFNYLEHYGGDWGERPVETTRSI 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 33238186   294 DgssnlDIPRLLNWFLADISFHSMHHLCDRIPNYNLRACHIRNKHLL 340
Cdd:pfam00487 200 R-----SPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREAL 241
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 61-332 8.42e-07

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: 49.18  E-value: 8.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186  61 IPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNRITGFLLGTLNAIPQYPWSRDHAFHHrhngnwevyrgpvdvitledy 140
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHH--------------------- 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 141 qalSKINqflysISRHWLMLFPGGFFYlvikprltlinaiahfiwsilveLCNKLLKRDFANLFSFstRFQANYSgygns 220
Cdd:cd03506  60 ---AYTN-----ILGHDPDIDTLPLLA-----------------------RSEPAFGKDQKKRFLH--RYQHFYF----- 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186 221 sgelidliannviviiswilmsrWLGAGLFWSCYSIIMTASAAIFICIFFVQHNFEGSYANGS---NEWSAilGAVDGSS 297
Cdd:cd03506 102 -----------------------FPLLALLLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGeskNDWLE--RQVLTTR 156

                       250       260       270
                ....*....|....*....|....*....|....*
gi 33238186 298 NLDIPRLLNWFLADISFHSMHHLCDRIPNYNLRAC 332
Cdd:cd03506 157 NITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPKV 191
PLN02498 PLN02498
omega-3 fatty acid desaturase
 75-126 1.10e-05

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 47.13  E-value: 1.10e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 33238186   75 FSLMHDCGHGSLFRSRRLNRITGFLLGTLNAIPQYPWSRDHAFHHRHNGNWE 126
Cdd:PLN02498 165 FVLGHDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVE 216
DesA_FADS-like cd03509
Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, ...
 56-120 5.82e-04

Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, DesA-like, yet uncharacterized subgroup of membrane fatty acid desaturase proteins found in alpha-, beta-, and gamma-proteobacteria. Sequences of this 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: 239586 [Multi-domain]  Cd Length: 288  Bit Score: 41.19  E-value: 5.82e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33238186  56 RALGLIPVLAILTLLSSRAFSLMHDCGHGSLFRSRRLNRITGFLlgTLNAIPQYPWSRD-HAFHHR 120
Cdd:cd03509  23 ARLPLPLATLLLIPLAALHSSLQHELLHGHPTRSRWVNEALGYP--PLALWYPYTRYRDtHLAHHR 86
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 75-123 2.55e-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: 38.42  E-value: 2.55e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 33238186  75 FSLMHDCGHGSLFRSRRLNRITGFLLG---TLNAIPQYpwSRDHAFHHRHNG 123
Cdd:cd03510  36 AILMHDAAHGLLFRNRRLNDFLGNWLAavpIFQSLAAY--RRSHLKHHRHLG 85
PLN02505 PLN02505
omega-6 fatty acid desaturase
 21-126 2.61e-03

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 39.67  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33238186   21 SNARAFWQVSTTIIPV---ALLWIL--IAWIDQSSFKTPfralglIPVLAiltllssrafslmHDCGHGSLFRSRRLNRI 95
Cdd:PLN02505  61 LIAALLYYVATNYIPLlpgPLSYVAwpLYWAAQGCVLTG------VWVIA-------------HECGHHAFSDYQWLDDT 121

                         90       100       110
                 ....*....|....*....|....*....|.
gi 33238186   96 TGFLLGTLNAIPQYPWSRDHAFHHRHNGNWE 126
Cdd:PLN02505 122 VGLVLHSALLVPYFSWKYSHRRHHSNTGSLE 152
 
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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