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Conserved domains on  [gi|15233152|ref|NP_191717|]
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Fatty acid/sphingolipid desaturase [Arabidopsis thaliana]

Protein Classification

fatty acid desaturase( domain architecture ID 10445761)

fatty acid desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond

EC:  1.14.19.-
Gene Ontology:  GO:0046872|GO:0016020|GO:0006633|GO:0016717
PubMed:  9767077

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 143-404 4.25e-59

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: 192.47  E-value: 4.25e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 143 IAAALLGLLWIQSAYIGHDSGHYVIMSNKSYNRFAQLLSGNCLtGISIAWWKWTHNAHHLACNSLDYDPDLQHIPVFAVS 222
Cdd:cd03506   2 LLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLL-GASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLARS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 223 TKFFssltsrfydrklTFDPVARFLVSYQHFTYYPVMCFgrinlfiqtFLLLFskrevpdralnFAGILVFWTWFpllvs 302
Cdd:cd03506  81 EPAF------------GKDQKKRFLHRYQHFYFFPLLAL---------LLLAF-----------LVVQLAGGLWL----- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 303 clpnwperfffvftsftvtalqHIQFTLNHFAADVYVGP-PTGSDWFEKQAAGTIDISCRSYMDWFFGGLQFQLEHHLFP 381
Cdd:cd03506 124 ----------------------AVVFQLNHFGMPVEDPPgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFP 181

                       250       260
                ....*....|....*....|...
gi 15233152 382 RLPRCHLRKVSPVVQELCKKHNL 404
Cdd:cd03506 182 TMPRHNYPKVAPLVRELCKKHGL 204
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 11-82 4.31e-25

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


:

Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 97.69  E-value: 4.31e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233152    11 TNEDLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGDTVILNLVGQDVTDAFIAF-HPGT-AWHHLDHLFTGYHI 82
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIgHSEDaAEKLLKKYRIGELA 74
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 143-404 4.25e-59

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: 192.47  E-value: 4.25e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 143 IAAALLGLLWIQSAYIGHDSGHYVIMSNKSYNRFAQLLSGNCLtGISIAWWKWTHNAHHLACNSLDYDPDLQHIPVFAVS 222
Cdd:cd03506   2 LLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLL-GASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLARS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 223 TKFFssltsrfydrklTFDPVARFLVSYQHFTYYPVMCFgrinlfiqtFLLLFskrevpdralnFAGILVFWTWFpllvs 302
Cdd:cd03506  81 EPAF------------GKDQKKRFLHRYQHFYFFPLLAL---------LLLAF-----------LVVQLAGGLWL----- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 303 clpnwperfffvftsftvtalqHIQFTLNHFAADVYVGP-PTGSDWFEKQAAGTIDISCRSYMDWFFGGLQFQLEHHLFP 381
Cdd:cd03506 124 ----------------------AVVFQLNHFGMPVEDPPgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFP 181

                       250       260
                ....*....|....*....|...
gi 15233152 382 RLPRCHLRKVSPVVQELCKKHNL 404
Cdd:cd03506 182 TMPRHNYPKVAPLVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 3-429 3.68e-58

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 199.53  E-value: 3.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152    3 EETEKKYITNEdLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGdTVILNLVGQDVTDAFIAFHPGTAWHHLDHLFTGYHI 82
Cdd:PLN03198 100 EKKSKSHLLSE-VAAHNKPNDCWIVIKNKVYDVSDFAAEHPGG-SVISTYFGRDGTDAFSSFHAASTWKILQDFYIGDVD 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   83 RDFQVSEVSRDYRRMAAEFRKLGLFENKGHVTLYTLAFVAAMFLGVLYGVLACTSVFAHQIAAALLGLLWIQSAYIGHDS 162
Cdd:PLN03198 178 NVEPTPELLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAASIAIICCSKSISAVLASACMMALCFQQCGWLSHDF 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  163 GHYVIMSNKSYNRFAQLLSGNCLTGISIAWWKWTHNAHHLACNSLD--YDP---DLQHIPVFAVSTKFFSSLTSRFYDRk 237
Cdd:PLN03198 258 LHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNECDqlYQPideDIDTLPLIAWSKDILATVENKTFLR- 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  238 ltfdpvarfLVSYQHFTYYPVMCFGRINLFIQTFLLLFSKREVP-DRALNFAGILVFWTWFpLLVSC--LPNWPERFFFV 314
Cdd:PLN03198 337 ---------ILQYQHLFFMALLFFARGSWLFWSWRYTSTAKLAPaDRLLEKGTILFHYFWF-IGTACylLPGWKPLVWMA 406

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  315 FTSFTVTALQHIQFTLNHFAADVYvgpPTGSDWFEKQAAGTIDISCRSYMDWFFGGLQFQLEHHLFPRLPRCHLRKVSPV 394
Cdd:PLN03198 407 VTELMCGMLLGFVFVLSHNGMEVY---NKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQ 483

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 15233152  395 VQELCKKHNLPYRSMSWFEANVLTINTLKTAAYQA 429
Cdd:PLN03198 484 VEAFCIKHGLVYEDVSIAAGTCKVLKALKEVAEAA 518
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
114-430 2.30e-33

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 127.92  E-value: 2.30e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 114 TLYTLAFVAAMFLGVLYGVLACTSVFAHQIAAALLGLLWIQSAYIGHDSGHYVIMSNKSYNRFAQLLSGNcLTGISIAWW 193
Cdd:COG3239  30 DWRYLLKLALTLALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRLLGL-PLGTPYDAW 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 194 KWTHNAHHLACNSLDYDPDLqhipVFAVSTKFFSSLTSRFYDRKLTFDPVARFLVSYQHFTYYPVMCFGRINLFIQTFLL 273
Cdd:COG3239 109 RRSHNRHHAYTNDPGKDPDI----GYGVQAWRPLYLFQHLLRFFLLGLGGLYWLLALDFLPLRGRLELKERRLEALLLLL 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 274 LFskrevpdrALNFAGILVFWTWFPLLVSCLPNWPerfffvftsftVTALQHIQFTLNHFAADvyvgppTGSDWFEKQAA 353
Cdd:COG3239 185 FL--------AALLALLLALGWWAVLLFWLLPLLV-----------AGLLLGLRFYLEHRGED------TGDGEYRDQLL 239

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233152 354 GTIDISCRSYMDWFFGGLQFQLEHHLFPRLPRCHLRKVSPVVQELCKKHNLPYRSMSWFEANVLTINTLKTAAYQAR 430
Cdd:COG3239 240 GSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPAR 316
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 11-82 4.31e-25

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 97.69  E-value: 4.31e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233152    11 TNEDLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGDTVILNLVGQDVTDAFIAF-HPGT-AWHHLDHLFTGYHI 82
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIgHSEDaAEKLLKKYRIGELA 74
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 6-82 2.85e-18

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 79.31  E-value: 2.85e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233152   6 EKKYITNEDLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGDTVILNLVGQDVTDAFIAFHPGTawHHLDHLFTGYHI 82
Cdd:COG5274  14 PEKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPHS--PKAERLLESYRI 88
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 138-408 3.01e-18

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: 83.93  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   138 VFAHQIAAALLGLLW-IQSAYIGHDSGHYVIMSNKSYNRFAQLLSGN---CLTGISIAWWKWTHNAHHLACNSLDYDPDL 213
Cdd:pfam00487   1 SWLALLLALLLGLFLlGITGSLAHEASHGALFKKRRLNRWLNDLLGRlagLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   214 QHipvfavstkFFSSLTSRFYDRKLTFDPVARFLVSYQHFTYYPVMCFGRINLFIQTFLLLFSKREVPDRALNFAGILVF 293
Cdd:pfam00487  81 AP---------LASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   294 WTWFPLLVSCLPNWPERFFFVFTSFTVTALQHiqftlnhfaadvyvgppTGSDWFEKQAAGTIDISCRS-YMDWFFGGLQ 372
Cdd:pfam00487 152 FLGLGGLLLLLWLLPLLVFGFLLALIFNYLEH-----------------YGGDWGERPVETTRSIRSPNwWLNLLTGNLN 214

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15233152   373 FQLEHHLFPRLPRCHLRKVSPVVQELCKKHNLPYRS 408
Cdd:pfam00487 215 YHIEHHLFPGVPWYRLPKLHRRLREALPEHGLPYRS 250
PLN02252 PLN02252
nitrate reductase [NADPH]
 1-91 2.45e-12

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 68.94  E-value: 2.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152    1 MAEETEKKYITNEDLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGDTVILNLVGQDVTDAFIAFHPGTAWHHLDhlftGY 80
Cdd:PLN02252 511 MNTNTGSKQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDKAKKMLE----DY 586

                         90
                 ....*....|.
gi 15233152   81 HIRDFQVSEVS 91
Cdd:PLN02252 587 RIGELVTTGAA 597
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 143-404 4.25e-59

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: 192.47  E-value: 4.25e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 143 IAAALLGLLWIQSAYIGHDSGHYVIMSNKSYNRFAQLLSGNCLtGISIAWWKWTHNAHHLACNSLDYDPDLQHIPVFAVS 222
Cdd:cd03506   2 LLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLL-GASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLARS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 223 TKFFssltsrfydrklTFDPVARFLVSYQHFTYYPVMCFgrinlfiqtFLLLFskrevpdralnFAGILVFWTWFpllvs 302
Cdd:cd03506  81 EPAF------------GKDQKKRFLHRYQHFYFFPLLAL---------LLLAF-----------LVVQLAGGLWL----- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 303 clpnwperfffvftsftvtalqHIQFTLNHFAADVYVGP-PTGSDWFEKQAAGTIDISCRSYMDWFFGGLQFQLEHHLFP 381
Cdd:cd03506 124 ----------------------AVVFQLNHFGMPVEDPPgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFP 181

                       250       260
                ....*....|....*....|...
gi 15233152 382 RLPRCHLRKVSPVVQELCKKHNL 404
Cdd:cd03506 182 TMPRHNYPKVAPLVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 3-429 3.68e-58

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 199.53  E-value: 3.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152    3 EETEKKYITNEdLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGdTVILNLVGQDVTDAFIAFHPGTAWHHLDHLFTGYHI 82
Cdd:PLN03198 100 EKKSKSHLLSE-VAAHNKPNDCWIVIKNKVYDVSDFAAEHPGG-SVISTYFGRDGTDAFSSFHAASTWKILQDFYIGDVD 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   83 RDFQVSEVSRDYRRMAAEFRKLGLFENKGHVTLYTLAFVAAMFLGVLYGVLACTSVFAHQIAAALLGLLWIQSAYIGHDS 162
Cdd:PLN03198 178 NVEPTPELLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAASIAIICCSKSISAVLASACMMALCFQQCGWLSHDF 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  163 GHYVIMSNKSYNRFAQLLSGNCLTGISIAWWKWTHNAHHLACNSLD--YDP---DLQHIPVFAVSTKFFSSLTSRFYDRk 237
Cdd:PLN03198 258 LHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNECDqlYQPideDIDTLPLIAWSKDILATVENKTFLR- 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  238 ltfdpvarfLVSYQHFTYYPVMCFGRINLFIQTFLLLFSKREVP-DRALNFAGILVFWTWFpLLVSC--LPNWPERFFFV 314
Cdd:PLN03198 337 ---------ILQYQHLFFMALLFFARGSWLFWSWRYTSTAKLAPaDRLLEKGTILFHYFWF-IGTACylLPGWKPLVWMA 406

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  315 FTSFTVTALQHIQFTLNHFAADVYvgpPTGSDWFEKQAAGTIDISCRSYMDWFFGGLQFQLEHHLFPRLPRCHLRKVSPV 394
Cdd:PLN03198 407 VTELMCGMLLGFVFVLSHNGMEVY---NKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQ 483

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 15233152  395 VQELCKKHNLPYRSMSWFEANVLTINTLKTAAYQA 429
Cdd:PLN03198 484 VEAFCIKHGLVYEDVSIAAGTCKVLKALKEVAEAA 518
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 1-426 1.50e-57

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 197.18  E-value: 1.50e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152    1 MAEETEKkyITNEDLKKHNKSGDLWIAIQGKVYNVSDWIKtHPGGdTVILNLVGQDVTDAFIAFHPGTAWHHLDHLFTGY 80
Cdd:PLN03199  19 LAEKPQK--ISWQEVKKHASPDDAWIIHQNKVYDVSNWHD-HPGG-AVIFTHAGDDMTDIFAAFHAPGSQALMKKFYIGD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   81 HI------RDFQVSEVSRDYRRMAAEFRKLGLFENKGHVTLYTLAFVAAMFLGVLYGVLACTSVFAHQIAAALLGLLWIQ 154
Cdd:PLN03199  95 LIpestehKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLFNMAIWAAACALVFYSDRFAMHIASALLLGLFFQQ 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  155 SAYIGHDSGHYVIMSNKSYNRFAQLLSGNCLTGISIAWWKWTHNAHH----LACNSL---DYDPDLQHIPVFAVSTKFFS 227
Cdd:PLN03199 175 CGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHavpnLHCSSAdaqDGDPDIDTMPLLAWSLKQAQ 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  228 SLTSRFYDRKLTfdPVARFLVSYQHFTYYPVMCFGRINLFIQTFLLLF--------SKREVPDRALNF-----AGILVFW 294
Cdd:PLN03199 255 SFREINADGKDS--GFVKFAIKFQAFFYFPILLLARISWLNESFKCAFglgaasenAALELEAKGLQYpllekAGILLHY 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  295 TWFPLLVSCLPNWPERFFFVFTSFTVTA---LQHIQFTLNHFAADVYvGPPTGSDWFEKQAAGTIDISC-----RSYMDW 366
Cdd:PLN03199 333 AWMFTLSSGFGRFSFAYSAFYFFTATAScgfFLAIVFGLGHNGMATY-DADARPDFWKLQVTTTRNIIGghgfpQAFVDW 411

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152  367 FFGGLQFQLEHHLFPRLPRCHLRKVSPVVQELCKKHNLPYRSMSWFEANVLTINTLKTAA 426
Cdd:PLN03199 412 FCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHLGKVA 471
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
114-430 2.30e-33

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 127.92  E-value: 2.30e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 114 TLYTLAFVAAMFLGVLYGVLACTSVFAHQIAAALLGLLWIQSAYIGHDSGHYVIMSNKSYNRFAQLLSGNcLTGISIAWW 193
Cdd:COG3239  30 DWRYLLKLALTLALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRLLGL-PLGTPYDAW 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 194 KWTHNAHHLACNSLDYDPDLqhipVFAVSTKFFSSLTSRFYDRKLTFDPVARFLVSYQHFTYYPVMCFGRINLFIQTFLL 273
Cdd:COG3239 109 RRSHNRHHAYTNDPGKDPDI----GYGVQAWRPLYLFQHLLRFFLLGLGGLYWLLALDFLPLRGRLELKERRLEALLLLL 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 274 LFskrevpdrALNFAGILVFWTWFPLLVSCLPNWPerfffvftsftVTALQHIQFTLNHFAADvyvgppTGSDWFEKQAA 353
Cdd:COG3239 185 FL--------AALLALLLALGWWAVLLFWLLPLLV-----------AGLLLGLRFYLEHRGED------TGDGEYRDQLL 239

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233152 354 GTIDISCRSYMDWFFGGLQFQLEHHLFPRLPRCHLRKVSPVVQELCKKHNLPYRSMSWFEANVLTINTLKTAAYQAR 430
Cdd:COG3239 240 GSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPAR 316
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 11-82 4.31e-25

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 97.69  E-value: 4.31e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233152    11 TNEDLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGDTVILNLVGQDVTDAFIAF-HPGT-AWHHLDHLFTGYHI 82
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIgHSEDaAEKLLKKYRIGELA 74
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 6-82 2.85e-18

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 79.31  E-value: 2.85e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233152   6 EKKYITNEDLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGDTVILNLVGQDVTDAFIAFHPGTawHHLDHLFTGYHI 82
Cdd:COG5274  14 PEKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPHS--PKAERLLESYRI 88
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 138-408 3.01e-18

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: 83.93  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   138 VFAHQIAAALLGLLW-IQSAYIGHDSGHYVIMSNKSYNRFAQLLSGN---CLTGISIAWWKWTHNAHHLACNSLDYDPDL 213
Cdd:pfam00487   1 SWLALLLALLLGLFLlGITGSLAHEASHGALFKKRRLNRWLNDLLGRlagLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   214 QHipvfavstkFFSSLTSRFYDRKLTFDPVARFLVSYQHFTYYPVMCFGRINLFIQTFLLLFSKREVPDRALNFAGILVF 293
Cdd:pfam00487  81 AP---------LASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152   294 WTWFPLLVSCLPNWPERFFFVFTSFTVTALQHiqftlnhfaadvyvgppTGSDWFEKQAAGTIDISCRS-YMDWFFGGLQ 372
Cdd:pfam00487 152 FLGLGGLLLLLWLLPLLVFGFLLALIFNYLEH-----------------YGGDWGERPVETTRSIRSPNwWLNLLTGNLN 214

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15233152   373 FQLEHHLFPRLPRCHLRKVSPVVQELCKKHNLPYRS 408
Cdd:pfam00487 215 YHIEHHLFPGVPWYRLPKLHRRLREALPEHGLPYRS 250
PLN02252 PLN02252
nitrate reductase [NADPH]
 1-91 2.45e-12

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 68.94  E-value: 2.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152    1 MAEETEKKYITNEDLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGDTVILNLVGQDVTDAFIAFHPGTAWHHLDhlftGY 80
Cdd:PLN02252 511 MNTNTGSKQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDKAKKMLE----DY 586

                         90
                 ....*....|.
gi 15233152   81 HIRDFQVSEVS 91
Cdd:PLN02252 587 RIGELVTTGAA 597
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 143-216 3.19e-08

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: 51.70  E-value: 3.19e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233152 143 IAAALLGLLWIQSAYIG-HDSGHYVIMSNKSYNRFAQLLSGNCLtGISIAWWKWTHNAHHLACNSLDYDPDLQHI 216
Cdd:cd01060   2 LLALLLGLLGGLGLTVLaHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDSAVN 75
COG4892 COG4892
Predicted heme/steroid binding protein [General function prediction only];
10-69 1.06e-04

Predicted heme/steroid binding protein [General function prediction only];


Pssm-ID: 443920 [Multi-domain]  Cd Length: 75  Bit Score: 40.58  E-value: 1.06e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233152  10 ITNEDLKKHN-KSGD-LWIAIQGKVYNVSD---WIK-THPGgdtvilNLVGQDVTDAFiAFHPGTA 69
Cdd:COG4892   4 FTLEELAKYNgKDGNpAYVAVNGKVYDVTNsrlWKNgTHYG------HWAGQDLTDEL-KDAPHGE 62
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 115-388 9.16e-04

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: 40.67  E-value: 9.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 115 LYTLAFVAAMFLGVLYGVLACTSVFAHQIAAALLGL----LWIqsayIGHDSGHYVIMSNKSYNRFAqllsgNCLTGISI 190
Cdd:cd03507   7 LSYLAPDILLLALLALAASLLLSWWLWPLYWIVQGLfltgLFV----LGHDCGHGSFSDNRRLNDIV-----GHILHSPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 191 AW----WKWTHNAHHLACNSLDYDPDlqHIPVFAVStkfFSSLTSRFYDRKLTfdpvarflvsyQHFTYYPVMcfGRINL 266
Cdd:cd03507  78 LVpyhsWRISHNRHHAHTGNLEGDEV--WVPVTEEE---YAELPKRLPYRLYR-----------NPFLMLSLG--WPYYL 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233152 267 FIQTFLLLFskreVPdrALNFAGILVFWTWfpllvsclpnwperfffvftsftvtaLQHIQFTLNHFAADVYvgpptgsD 346
Cdd:cd03507 140 LLNVLLYYL----IP--YLVVNAWLVLITY--------------------------LQHTFPDIPWYRADEW-------N 180

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15233152 347 WFEKQAAGTIDISCRSYMDWFFGGLQFQLEHHLFPRLPRCHL 388
Cdd:cd03507 181 FAQAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
 
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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