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Conserved domains on  [gi|102230693|gb|ABF70324|]
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delta-12 desaturase, partial [Orychophragmus violaceus]

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 ...
 1-260 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 PLN02505:

Pssm-ID: 445012  Cd Length: 381  Bit Score: 512.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693   1 QVSPSSKKSETDALKRVPCETPPFTLGDLKKAIPPHCFKRSIPRSFSYLIWDIIIASCFYYVATNYFSLLPNPLSYLAWP 80
Cdd:PLN02505   8 SVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGPLSYVAWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  81 LYWVCQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKW 160
Cdd:PLN02505  88 LYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSALPW 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693 161 YGKYLNNPLGRTVMLTVQFTLGWPLYLAFNVSGKPYDGFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYRYAAAQG 240
Cdd:PLN02505 168 YSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGLYRLAAAKG 247

                        250       260
                 ....*....|....*....|
gi 102230693 241 IASMICIYGVPLLIVNGFLV 260
Cdd:PLN02505 248 LAWVLCVYGVPLLIVNAFLV 267
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
 1-260 0e+00

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 512.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693   1 QVSPSSKKSETDALKRVPCETPPFTLGDLKKAIPPHCFKRSIPRSFSYLIWDIIIASCFYYVATNYFSLLPNPLSYLAWP 80
Cdd:PLN02505   8 SVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGPLSYVAWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  81 LYWVCQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKW 160
Cdd:PLN02505  88 LYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSALPW 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693 161 YGKYLNNPLGRTVMLTVQFTLGWPLYLAFNVSGKPYDGFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYRYAAAQG 240
Cdd:PLN02505 168 YSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGLYRLAAAKG 247

                        250       260
                 ....*....|....*....|
gi 102230693 241 IASMICIYGVPLLIVNGFLV 260
Cdd:PLN02505 248 LAWVLCVYGVPLLIVNAFLV 267
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 40-214 3.15e-52

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: 169.33  E-value: 3.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  40 RSIPRSFSYLIWDIIIASCFYYVAtnyfsllPNPLSYLAWPLYWVCQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIF 119
Cdd:cd03507    1 RSLFRSLSYLAPDILLLALLALAA-------SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693 120 HSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGKYLNNPLGRTVMltVQFTLGWPLYLAFNVS---GKPY 196
Cdd:cd03507   74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPF--LMLSLGWPYYLLLNVLlyyLIPY 151

                        170       180
                 ....*....|....*....|....*..
gi 102230693 197 DGFAC---------HFHPNAPIYNDRE 214
Cdd:cd03507  152 LVVNAwlvlitylqHTFPDIPWYRADE 178
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
25-260 1.44e-19

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 85.94  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  25 TLGDLKKAIPPHCFKRSIpRSFSYLIWDIIIASCFYYVAtnyfsllpnPLSYLAWPLyWVCQGCVLTGVWVIAHECGHHA 104
Cdd:COG3239   14 ELRALRARLRALLGRRDW-RYLLKLALTLALLAALWLLL---------SWSWLALLA-ALLLGLALAGLFSLGHDAGHGS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693 105 FSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGkyLNNPLGRTVmltvqFTLGWP 184
Cdd:COG3239   83 LFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYL--FQHLLRFFL-----LGLGGL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 102230693 185 LYLafnvsgkpydgFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYryaAAQGIASMICIYGVPLLIVNGFLV 260
Cdd:COG3239  156 YWL-----------LALDFLPLRGRLELKERRLEALLLLLFLAALLALL---LALGWWAVLLFWLLPLLVAGLLLG 217
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 75-260 1.37e-11

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: 62.75  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693   75 SYLAWPLYWVCQGCVLTGVWVIAHECGHHAFSD----YQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVF 150
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  151 VPKKKSDIKWYGKYLNnplgrtvMLTVQFTLGWPLYLAFNVSGKPYDGFachfhpnAPIYNDRERLQIYISDAGILAVCY 230
Cdd:pfam00487  81 APLASRFRGLLRYLLR-------WLLGLLVLAWLLALVLPLWLRRLARR-------KRPIKSRRRRWRLIAWLLLLAAWL 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 102230693  231 GLYrYAAAQGIASMICIYGVPLLIVNGFLV 260
Cdd:pfam00487 147 GLW-LGFLGLGGLLLLLWLLPLLVFGFLLA 175
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
 1-260 0e+00

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 512.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693   1 QVSPSSKKSETDALKRVPCETPPFTLGDLKKAIPPHCFKRSIPRSFSYLIWDIIIASCFYYVATNYFSLLPNPLSYLAWP 80
Cdd:PLN02505   8 SVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGPLSYVAWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  81 LYWVCQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKW 160
Cdd:PLN02505  88 LYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSALPW 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693 161 YGKYLNNPLGRTVMLTVQFTLGWPLYLAFNVSGKPYDGFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYRYAAAQG 240
Cdd:PLN02505 168 YSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGLYRLAAAKG 247

                        250       260
                 ....*....|....*....|
gi 102230693 241 IASMICIYGVPLLIVNGFLV 260
Cdd:PLN02505 248 LAWVLCVYGVPLLIVNAFLV 267
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 40-214 3.15e-52

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: 169.33  E-value: 3.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  40 RSIPRSFSYLIWDIIIASCFYYVAtnyfsllPNPLSYLAWPLYWVCQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIF 119
Cdd:cd03507    1 RSLFRSLSYLAPDILLLALLALAA-------SLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693 120 HSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGKYLNNPLGRTVMltVQFTLGWPLYLAFNVS---GKPY 196
Cdd:cd03507   74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPF--LMLSLGWPYYLLLNVLlyyLIPY 151

                        170       180
                 ....*....|....*....|....*..
gi 102230693 197 DGFAC---------HFHPNAPIYNDRE 214
Cdd:cd03507  152 LVVNAwlvlitylqHTFPDIPWYRADE 178
PLN02498 PLN02498
omega-3 fatty acid desaturase
 18-254 3.22e-39

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 141.50  E-value: 3.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  18 PCETPPFTLGDLKKAIPPHCFKRSIPRSFSYLIWDIIIAsCFYYVATNYFSllpnplSYLAWPLYWVCQGCVLTGVWVIA 97
Cdd:PLN02498  96 PGAPPPFNLADIRAAIPKHCWVKNPWRSMSYVVRDVAVV-FGLAAAAAYFN------NWVVWPLYWFAQGTMFWALFVLG 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  98 HECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKsdiKWYgKYLNNPLgRTVMLTV 177
Cdd:PLN02498 169 HDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLSE---KIY-KSLDKVT-RTLRFTL 243

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 102230693 178 QF-TLGWPLYLAFNVSGKPydgfACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYRYAAAQGIASMICIYGVPLLI 254
Cdd:PLN02498 244 PFpMLAYPFYLWSRSPGKK----GSHFHPDSDLFVPKERKDVITSTACWTAMAALLVCLSFVMGPIQMLKLYGIPYWI 317
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
25-260 1.44e-19

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 85.94  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  25 TLGDLKKAIPPHCFKRSIpRSFSYLIWDIIIASCFYYVAtnyfsllpnPLSYLAWPLyWVCQGCVLTGVWVIAHECGHHA 104
Cdd:COG3239   14 ELRALRARLRALLGRRDW-RYLLKLALTLALLAALWLLL---------SWSWLALLA-ALLLGLALAGLFSLGHDAGHGS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693 105 FSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGkyLNNPLGRTVmltvqFTLGWP 184
Cdd:COG3239   83 LFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYL--FQHLLRFFL-----LGLGGL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 102230693 185 LYLafnvsgkpydgFACHFHPNAPIYNDRERLQIYISDAGILAVCYGLYryaAAQGIASMICIYGVPLLIVNGFLV 260
Cdd:COG3239  156 YWL-----------LALDFLPLRGRLELKERRLEALLLLLFLAALLALL---LALGWWAVLLFWLLPLLVAGLLLG 217
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 76-151 3.26e-18

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: 77.90  E-value: 3.26e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 102230693  76 YLAWPLYWVCQGcvlTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFV 151
Cdd:cd01060    1 LLLALLLGLLGG---LGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKDPDSA 73
PLN02598 PLN02598
omega-6 fatty acid desaturase
 23-158 6.05e-14

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 70.62  E-value: 6.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  23 PFTLGDLKKAIPPHCFKRSIPRSFSYLIwdIIIASCfyyvATNYFSLLPNPLsYLaWPLYWVCQGCVLTGVWVIAHECGH 102
Cdd:PLN02598  77 NVTLKDVVKTLPKEVFEIDDFKAWKTVA--ITVTSY----ALGLAAIAVAPW-YL-LPLAWAWLGTAITGFFVIGHDCGH 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 102230693 103 HAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDI 158
Cdd:PLN02598 149 NSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNTHHAHTNKLVMDTAWQPFRPHQF 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 75-260 1.37e-11

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: 62.75  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693   75 SYLAWPLYWVCQGCVLTGVWVIAHECGHHAFSD----YQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVF 150
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  151 VPKKKSDIKWYGKYLNnplgrtvMLTVQFTLGWPLYLAFNVSGKPYDGFachfhpnAPIYNDRERLQIYISDAGILAVCY 230
Cdd:pfam00487  81 APLASRFRGLLRYLLR-------WLLGLLVLAWLLALVLPLWLRRLARR-------KRPIKSRRRRWRLIAWLLLLAAWL 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 102230693  231 GLYrYAAAQGIASMICIYGVPLLIVNGFLV 260
Cdd:pfam00487 147 GLW-LGFLGLGGLLLLLWLLPLLVFGFLLA 175
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 75-156 5.97e-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: 58.15  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 102230693  75 SYLAWPLYWVcQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERD-EVFVPK 153
Cdd:cd03511   41 SWWALPAFLV-YGVLYAALFARWHECVHGTAFATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRYTQIPGRDpELAVPR 119


                 ...
gi 102230693 154 KKS 156
Cdd:cd03511  120 PPT 122
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 96-147 5.92e-09

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: 54.57  E-value: 5.92e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 102230693  96 IAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERD 147
Cdd:cd03506   17 LAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHD 68
DUF3474 pfam11960
Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. ...
 22-55 2.68e-05

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: 42.80  E-value: 2.68e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 102230693   22 PPFTLGDLKKAIPPHCFKRSIPRSFSYLIWDIII 55
Cdd:pfam11960  88 PPFKLADIRAAIPKHCWVKDPWRSMSYVVRDVAV 121
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 69-142 2.92e-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: 37.65  E-value: 2.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 102230693  69 LLPNPLSYLAwPLYWVcqGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSF-LLVPYFSWKYSHRRHHSNTG 142
Cdd:cd03510   14 AWPNWLAYLL-AVLLI--GARQRALAILMHDAAHGLLFRNRRLNDFLGNWLAAVpIFQSLAAYRRSHLKHHRHLG 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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