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Conserved domains on  [gi|636745380|gb|AIA21663|]
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oleate desaturase [Crambe glabrata]

Protein Classification

fatty acid desaturase( domain architecture ID 10791388)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
1-383 0e+00

omega-6 fatty acid desaturase


:

Pssm-ID: 178121  Cd Length: 381  Bit Score: 794.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380   1 MGAGGRMQVSPSPKKSETDTLKRVPCETPPFTVGELKKAIPPHCFKRSIPRSFSYLIWDIIIASCFYYVATNYFSLLPHP 80
Cdd:PLN02505   1 MGAGGRMSVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  81 LSYIAWPLYWACQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160
Cdd:PLN02505  81 LSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 161 KKSDIKWYGKYLNNPLGRTVMLTVQFTLGWPLYLAFNVSGRPYDGFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLY 240
Cdd:PLN02505 161 KKSALPWYSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGLY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 241 RYAAAQGVASMICLYGVPLLIVNGFLVLITYLQHTHPSLPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHL 320
Cdd:PLN02505 241 RLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636745380 321 FSTMPHYHAMEATKAIKPILGDYYQFDGTPVFKAMWREAKECIYVEPDrqGEKKGVFWYNNKL 383
Cdd:PLN02505 321 FSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPD--EGGKGVFWYNNKF 381
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
1-383 0e+00

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 794.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380   1 MGAGGRMQVSPSPKKSETDTLKRVPCETPPFTVGELKKAIPPHCFKRSIPRSFSYLIWDIIIASCFYYVATNYFSLLPHP 80
Cdd:PLN02505   1 MGAGGRMSVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  81 LSYIAWPLYWACQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160
Cdd:PLN02505  81 LSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 161 KKSDIKWYGKYLNNPLGRTVMLTVQFTLGWPLYLAFNVSGRPYDGFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLY 240
Cdd:PLN02505 161 KKSALPWYSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGLY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 241 RYAAAQGVASMICLYGVPLLIVNGFLVLITYLQHTHPSLPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHL 320
Cdd:PLN02505 241 RLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636745380 321 FSTMPHYHAMEATKAIKPILGDYYQFDGTPVFKAMWREAKECIYVEPDrqGEKKGVFWYNNKL 383
Cdd:PLN02505 321 FSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPD--EGGKGVFWYNNKF 381
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
47-329 6.40e-82

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: 249.45  E-value: 6.40e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  47 RSIPRSFSYLIWDIIIASCFYYVAtnyfsllPHPLSYIAWPLYWACQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIF 126
Cdd:cd03507    1 RSLFRSLSYLAPDILLLALLALAA-------SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 127 HSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGKYLNNPLGRTVMltVQFTLGWPLYLAFNVsgrpydgf 206
Cdd:cd03507   74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPF--LMLSLGWPYYLLLNV-------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 207 achfhpnapiyndrerlqiyisdagilavcyglyryaaaqgvasmICLYGVPLLIVNGFLVLITYLQHTHPSLPHYDSSE 286
Cdd:cd03507  144 ---------------------------------------------LLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADE 178
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 636745380 287 WDWL-RGALATVDRDYG-ILNKVFHNItDTHVAHHLFSTMPHYHA 329
Cdd:cd03507  179 WNFAqAGLLGTVDRDYGgWLNWLTHII-GTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
35-361 1.33e-33

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 127.15  E-value: 1.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  35 ELKKAIPPHCFKRSIpRSFSYLIWDIIIASCFYYVATNYFsllphplsyiAWPLYWACQGCVLTGVWVIAHECGHHAFSD 114
Cdd:COG3239   17 ALRARLRALLGRRDW-RYLLKLALTLALLAALWLLLSWSW----------LALLAALLLGLALAGLFSLGHDAGHGSLFR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 115 YQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGkyLNNPLGRTVmltvqFTLGWPLYL 194
Cdd:COG3239   86 SRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYL--FQHLLRFFL-----LGLGGLYWL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 195 afnvsgrpydgFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYryaAAQGVASMICLYGVPLLIVNGFLVLITYLQH 274
Cdd:COG3239  159 -----------LALDFLPLRGRLELKERRLEALLLLLFLAALLALL---LALGWWAVLLFWLLPLLVAGLLLGLRFYLEH 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 275 THPslphyDSSEWDWLRGALATVDRDYG-ILNKVFHNItDTHVAHHLFSTMPHYHAMEATKAIKPILGDYYQFDGTPVFK 353
Cdd:COG3239  225 RGE-----DTGDGEYRDQLLGSRNIRGGrLLRWLFGNL-NYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLL 298

                 ....*...
gi 636745380 354 AMWREAKE 361
Cdd:COG3239  299 RSYREVLR 306
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
82-344 5.10e-22

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: 93.95  E-value: 5.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380   82 SYIAWPLYWACQGCVLTGVWVIAHECGHHAFSD----YQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVF 157
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  158 VPKKKSDIKWYGKYLNnplgrtvMLTVQFTLGWPLYLAFNVSGRPYDGFachfhpnAPIYNDRERLQIYISDAGILAVCY 237
Cdd:pfam00487  81 APLASRFRGLLRYLLR-------WLLGLLVLAWLLALVLPLWLRRLARR-------KRPIKSRRRRWRLIAWLLLLAAWL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  238 GLYrYAAAQGVASMICLYGVPLLIVNGFLVLI-TYLQHTHPSLPHYDSSewdwlrgALATVDRDYGILNKVFHNItDTHV 316
Cdd:pfam00487 147 GLW-LGFLGLGGLLLLLWLLPLLVFGFLLALIfNYLEHYGGDWGERPVE-------TTRSIRSPNWWLNLLTGNL-NYHI 217
                         250       260
                  ....*....|....*....|....*...
gi 636745380  317 AHHLFSTMPHYHAMEATKAIKPILGDYY 344
Cdd:pfam00487 218 EHHLFPGVPWYRLPKLHRRLREALPEHG 245
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
1-383 0e+00

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 794.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380   1 MGAGGRMQVSPSPKKSETDTLKRVPCETPPFTVGELKKAIPPHCFKRSIPRSFSYLIWDIIIASCFYYVATNYFSLLPHP 80
Cdd:PLN02505   1 MGAGGRMSVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  81 LSYIAWPLYWACQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160
Cdd:PLN02505  81 LSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 161 KKSDIKWYGKYLNNPLGRTVMLTVQFTLGWPLYLAFNVSGRPYDGFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLY 240
Cdd:PLN02505 161 KKSALPWYSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGLY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 241 RYAAAQGVASMICLYGVPLLIVNGFLVLITYLQHTHPSLPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHL 320
Cdd:PLN02505 241 RLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636745380 321 FSTMPHYHAMEATKAIKPILGDYYQFDGTPVFKAMWREAKECIYVEPDrqGEKKGVFWYNNKL 383
Cdd:PLN02505 321 FSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPD--EGGKGVFWYNNKF 381
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
47-329 6.40e-82

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: 249.45  E-value: 6.40e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  47 RSIPRSFSYLIWDIIIASCFYYVAtnyfsllPHPLSYIAWPLYWACQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIF 126
Cdd:cd03507    1 RSLFRSLSYLAPDILLLALLALAA-------SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 127 HSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGKYLNNPLGRTVMltVQFTLGWPLYLAFNVsgrpydgf 206
Cdd:cd03507   74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPF--LMLSLGWPYYLLLNV-------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 207 achfhpnapiyndrerlqiyisdagilavcyglyryaaaqgvasmICLYGVPLLIVNGFLVLITYLQHTHPSLPHYDSSE 286
Cdd:cd03507  144 ---------------------------------------------LLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADE 178
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 636745380 287 WDWL-RGALATVDRDYG-ILNKVFHNItDTHVAHHLFSTMPHYHA 329
Cdd:cd03507  179 WNFAqAGLLGTVDRDYGgWLNWLTHII-GTHVAHHLFPRIPHYNL 222
PLN02498 PLN02498
omega-3 fatty acid desaturase
25-345 6.14e-72

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 231.64  E-value: 6.14e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  25 PCETPPFTVGELKKAIPPHCFKRSIPRSFSYLIWDIIIAsCFYYVATNYFSllphplSYIAWPLYWACQGCVLTGVWVIA 104
Cdd:PLN02498  96 PGAPPPFNLADIRAAIPKHCWVKNPWRSMSYVVRDVAVV-FGLAAAAAYFN------NWVVWPLYWFAQGTMFWALFVLG 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 105 HECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKsdiKWYgKYLNNPLgRTVMLTV 184
Cdd:PLN02498 169 HDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLSE---KIY-KSLDKVT-RTLRFTL 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 185 QF-TLGWPLYLAFNVSGRPydgfACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYRYAAAQGVASMICLYGVPLLIVN 263
Cdd:PLN02498 244 PFpMLAYPFYLWSRSPGKK----GSHFHPDSDLFVPKERKDVITSTACWTAMAALLVCLSFVMGPIQMLKLYGIPYWIFV 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 264 GFLVLITYLQH--THPSLPHYDSSEWDWLRGALATVDRDYGILNKVFHNItDTHVAHHLFSTMPHYHAMEATKAIKPILG 341
Cdd:PLN02498 320 MWLDFVTYLHHhgHEDKLPWYRGKEWSYLRGGLTTLDRDYGWINNIHHDI-GTHVIHHLFPQIPHYHLVEATEAAKPVLG 398

                 ....
gi 636745380 342 DYYQ 345
Cdd:PLN02498 399 KYYR 402
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
35-361 1.33e-33

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 127.15  E-value: 1.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  35 ELKKAIPPHCFKRSIpRSFSYLIWDIIIASCFYYVATNYFsllphplsyiAWPLYWACQGCVLTGVWVIAHECGHHAFSD 114
Cdd:COG3239   17 ALRARLRALLGRRDW-RYLLKLALTLALLAALWLLLSWSW----------LALLAALLLGLALAGLFSLGHDAGHGSLFR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 115 YQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGkyLNNPLGRTVmltvqFTLGWPLYL 194
Cdd:COG3239   86 SRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYL--FQHLLRFFL-----LGLGGLYWL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 195 afnvsgrpydgFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYryaAAQGVASMICLYGVPLLIVNGFLVLITYLQH 274
Cdd:COG3239  159 -----------LALDFLPLRGRLELKERRLEALLLLLFLAALLALL---LALGWWAVLLFWLLPLLVAGLLLGLRFYLEH 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 275 THPslphyDSSEWDWLRGALATVDRDYG-ILNKVFHNItDTHVAHHLFSTMPHYHAMEATKAIKPILGDYYQFDGTPVFK 353
Cdd:COG3239  225 RGE-----DTGDGEYRDQLLGSRNIRGGrLLRWLFGNL-NYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLL 298

                 ....*...
gi 636745380 354 AMWREAKE 361
Cdd:COG3239  299 RSYREVLR 306
PLN02598 PLN02598
omega-6 fatty acid desaturase
69-343 1.94e-22

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 97.97  E-value: 1.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  69 VATNYFSLLPHPlsYIAWPLYWACQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNT 148
Cdd:PLN02598 110 YALGLAAIAVAP--WYLLPLAWAWLGTAITGFFVIGHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNTHHAHT 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 149 GSLERDEVFVPKKKSDI-KWygkylnNPLGRTVMltvQFTLGwPLYLAFNVsgrpydGFACHFHPNAPIYNDRERLQIYI 227
Cdd:PLN02598 188 NKLVMDTAWQPFRPHQFdNA------DPLRKAMM---RAGMG-PLWWWASI------GHWLFWHFDLNKFRPQEVPRVKI 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 228 SdagiLAVCYGLYRYAAA-----QGVASMICLYGVPLLIVNGFLVLITYLQHTHPSLPHYDSSEWDWLRGALA-TVDRDY 301
Cdd:PLN02598 252 S----LAAVFAFMALGLPpllytTGPVGFVKWWLMPWLGYHFWMSTFTMVHHTAPHIPFKQAREWNAAQAQLNgTVHCDY 327
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 636745380 302 -GILNKVFHNITdTHVAHHLFSTMPHYHAMEATKAIKPILGDY 343
Cdd:PLN02598 328 pAWIEFLCHDIS-VHIPHHISSKIPSYNLRKAHASLQENWGKH 369
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
82-344 5.10e-22

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: 93.95  E-value: 5.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380   82 SYIAWPLYWACQGCVLTGVWVIAHECGHHAFSD----YQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVF 157
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  158 VPKKKSDIKWYGKYLNnplgrtvMLTVQFTLGWPLYLAFNVSGRPYDGFachfhpnAPIYNDRERLQIYISDAGILAVCY 237
Cdd:pfam00487  81 APLASRFRGLLRYLLR-------WLLGLLVLAWLLALVLPLWLRRLARR-------KRPIKSRRRRWRLIAWLLLLAAWL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  238 GLYrYAAAQGVASMICLYGVPLLIVNGFLVLI-TYLQHTHPSLPHYDSSewdwlrgALATVDRDYGILNKVFHNItDTHV 316
Cdd:pfam00487 147 GLW-LGFLGLGGLLLLLWLLPLLVFGFLLALIfNYLEHYGGDWGERPVE-------TTRSIRSPNWWLNLLTGNL-NYHI 217
                         250       260
                  ....*....|....*....|....*...
gi 636745380  317 AHHLFSTMPHYHAMEATKAIKPILGDYY 344
Cdd:pfam00487 218 EHHLFPGVPWYRLPKLHRRLREALPEHG 245
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
83-158 3.27e-16

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: 74.43  E-value: 3.27e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636745380  83 YIAWPLYWACQGcvlTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFV 158
Cdd:cd01060    1 LLLALLLGLLGG---LGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKDPDSA 73
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
81-344 2.87e-11

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: 62.27  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  81 LSYIAWPLYWACQGCvltgvwvIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEvfvpk 160
Cdd:cd03506    2 LLAILLGLFWAQGGF-------LAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHDP----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 161 kksDIKwygkylNNPLgrtvmltvqftlgwplyLAFNVSGRPYDGFACHFHPNAPIYndrerlqiyisdagilavCYGLY 240
Cdd:cd03506   70 ---DID------TLPL-----------------LARSEPAFGKDQKKRFLHRYQHFY------------------FFPLL 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 241 ryaaaqgvASMICLYGVPLLIVNGFLVLITYLQH-THPSLPHYDSSEWDWL-RGALATVDRDYGILNKVFH---NItdtH 315
Cdd:cd03506  106 --------ALLLLAFLVVQLAGGLWLAVVFQLNHfGMPVEDPPGESKNDWLeRQVLTTRNITGSPFLDWLHgglNY---Q 174
                        250       260
                 ....*....|....*....|....*....
gi 636745380 316 VAHHLFSTMPHYHAMEATKAIKPILGDYY 344
Cdd:cd03506  175 IEHHLFPTMPRHNYPKVAPLVRELCKKHG 203
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
82-330 5.36e-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: 62.77  E-value: 5.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380  82 SYIAWPLYWAcQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERD-EVFVPK 160
Cdd:cd03511   41 SWWALPAFLV-YGVLYAALFARWHECVHGTAFATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRYTQIPGRDpELAVPR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 161 KKSDIKWYGKYLNNPLGRTVMLTVQftlgwpLYLAFNVSGRPYDGFACHFHPnAPIYNDRERLQIYisdAGILAVCYGLy 240
Cdd:cd03511  120 PPTLREYLLALSGLPYWWGKLRTVF------RHAFGAVSEAEKPFIPAEERP-KVVREARAMLAVY---AGLIALSLYL- 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636745380 241 ryaaaqGVASMICLYGVPLLIVNGFLVLITYLQHTHpslphydssewdwlrgaLATVDRDY-----GILNKVFHNIT--- 312
Cdd:cd03511  189 ------GSPLLVLVWGLPLLLGQPILRLFLLAEHGG-----------------CPEDANDLrntrtTLTNPPLRFLYwnm 245
                        250
                 ....*....|....*...
gi 636745380 313 DTHVAHHLFSTMPhYHAM 330
Cdd:cd03511  246 PYHAEHHMYPSVP-FHAL 262
DUF3474 pfam11960
Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. ...
29-62 6.49e-04

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: 39.33  E-value: 6.49e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 636745380   29 PPFTVGELKKAIPPHCFKRSIPRSFSYLIWDIII 62
Cdd:pfam11960  88 PPFKLADIRAAIPKHCWVKDPWRSMSYVVRDVAV 121
 
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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