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Conserved domains on  [gi|126157490|ref|NP_001075133|]
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fatty acid desaturase 2-like protein FADS2B [Mus musculus]

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: ...
 206-456 4.75e-63

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: 203.64  E-value: 4.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 206 ILISFLLTVSQAQCSFLQHDLGHLSMFKKSKWNHLMHKFVMChLKGLSADWWNYRHFQHHVKPNIYPKDPDIDVGPLFLV 285
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 286 GDTQPIKYGKKKIKyidYEKQHLYFYMVALPFLMpvyfnlqsmqvmylrkywmdiawvssfyirYFItfgpfygifgtvl 365
Cdd:cd03506   80 SEPAFGKDQKKRFL---HRYQHFYFFPLLALLLL------------------------------AFL------------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 366 liyLVKFIESPWIAYVTQMSHIPMKM---SSEENHDWLSTQVVATCNIEQSFFNDWFTGHLNFQIEHHLFPTMPRHNYHK 442
Cdd:cd03506  114 ---VVQLAGGLWLAVVFQLNHFGMPVedpPGESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 126157490 443 VAPLVKSLCAKHGL 456
Cdd:cd03506  191 VAPLVRELCKKHGL 204
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 66-138 6.77e-23

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: 91.91  E-value: 6.77e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126157490   66 TWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRRVLNHYAGQDATDAFRAMHLDLGMVKLYLKPLLIGEL 138
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGEL 73
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 206-456 4.75e-63

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: 203.64  E-value: 4.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 206 ILISFLLTVSQAQCSFLQHDLGHLSMFKKSKWNHLMHKFVMChLKGLSADWWNYRHFQHHVKPNIYPKDPDIDVGPLFLV 285
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 286 GDTQPIKYGKKKIKyidYEKQHLYFYMVALPFLMpvyfnlqsmqvmylrkywmdiawvssfyirYFItfgpfygifgtvl 365
Cdd:cd03506   80 SEPAFGKDQKKRFL---HRYQHFYFFPLLALLLL------------------------------AFL------------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 366 liyLVKFIESPWIAYVTQMSHIPMKM---SSEENHDWLSTQVVATCNIEQSFFNDWFTGHLNFQIEHHLFPTMPRHNYHK 442
Cdd:cd03506  114 ---VVQLAGGLWLAVVFQLNHFGMPVedpPGESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 126157490 443 VAPLVKSLCAKHGL 456
Cdd:cd03506  191 VAPLVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 65-478 1.49e-56

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 196.45  E-value: 1.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  65 YTWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRrVLNHYAGQDATDAFRAMHLdlGMVKLYLKPLLIGELSPEEPS 144
Cdd:PLN03198 106 HLLSEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFHA--ASTWKILQDFYIGDVDNVEPT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 145 QEknknaqLVEDFRELRKTLEAMNMF-SANLRFFFLHLAQILILEISAWLIlhHFGSSWLVTILISFLLTVSQAQCSFLQ 223
Cdd:PLN03198 183 PE------LLKDFRDLRALFLREQLFkSSKLYYVFKLLTNIAIFAASIAII--CCSKSISAVLASACMMALCFQQCGWLS 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 224 HDLGHLSMFKKSKWNHLMHKFVMCHLKGLSADWWNYRHFQHHVKPN----IY-PKDPDIDVGPLFLVG-DTQPIKYGKKK 297
Cdd:PLN03198 255 HDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNecdqLYqPIDEDIDTLPLIAWSkDILATVENKTF 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 298 IKYIDYekQHLYFymVALPFlmpvyfnlqsmqvmYLRKYWMDIAWVSS------------------FYIRYFITFGpFYG 359
Cdd:PLN03198 335 LRILQY--QHLFF--MALLF--------------FARGSWLFWSWRYTstaklapadrllekgtilFHYFWFIGTA-CYL 395

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 360 IFGTVLLIYLV--KFIESPWIAYVTQMSHIPMKMSSEeNHDWLSTQVVATCNIEQSFFNDWFTGHLNFQIEHHLFPTMPR 437
Cdd:PLN03198 396 LPGWKPLVWMAvtELMCGMLLGFVFVLSHNGMEVYNK-SKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPR 474

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 126157490 438 HNYHKVAPLVKSLCAKHGLQYINKPILKAFGDIVRSLKKSA 478
Cdd:PLN03198 475 HNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKEVA 515
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
144-478 2.49e-42

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 152.96  E-value: 2.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 144 SQEKNKNAQLVEDFRELRKTLEAmNMFSANLRFFFLhLAQILILEISAWLIlhhFGSSWLVtILISFLLTVSQAQCSFLQ 223
Cdd:COG3239    2 TTATPLTPADEAELRALRARLRA-LLGRRDWRYLLK-LALTLALLAALWLL---LSWSWLA-LLAALLLGLALAGLFSLG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 224 HDLGHLSMFKKSKWNHLMHkFVMCHLKGLSADWWNYRHFQHHVKPNIYPKDPDIDVGplflvgdtqpikygkkkikYIDY 303
Cdd:COG3239   76 HDAGHGSLFRSRWLNDLLG-RLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYG-------------------VQAW 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 304 EKQHLYFYMVALPFLMPVYFN-------LQSMQVMYLRKYWMDIAWVSSFYIRYFITFgpFYGIFGTVLLIYLV-KFIES 375
Cdd:COG3239  136 RPLYLFQHLLRFFLLGLGGLYwllaldfLPLRGRLELKERRLEALLLLLFLAALLALL--LALGWWAVLLFWLLpLLVAG 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 376 PWIAYVTQMSHIPMKMSSEENHDwlstQVVATCNIEQSFFNDWFTGHLNFQIEHHLFPTMPRHNYHKVAPLVKSLCAKHG 455
Cdd:COG3239  214 LLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYG 289

                        330       340
                 ....*....|....*....|...
gi 126157490 456 LQYINKPILKAFGDIVRSLKKSA 478
Cdd:COG3239  290 LPYTEGSLLRSYREVLRLLRRLG 312
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 201-459 6.93e-25

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: 103.19  E-value: 6.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  201 SWLVTILISFLLTVSQAQCSFLQHDLGHLSMFKKSKWNHLMHKFVMCH---LKGLSADWWNYRHFQHHVKPNIYPKDPDI 277
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLGRLaglPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  278 DVGPLFLVGDTQPIKYGKKKIkyidyekQHLYFYMVALPFLMPVYFNLQSMQVMYLRKYWMDIAWVSsFYIRYFITFGPF 357
Cdd:pfam00487  81 APLASRFRGLLRYLLRWLLGL-------LVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLL-LLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  358 YGIFGTVLLIYLVKFIE-SPWIAYV-TQMSHIPmkmsseenHDWLSTQVVATCNIEQ-SFFNDWFTGHLNFQIEHHLFPT 434
Cdd:pfam00487 153 LGLGGLLLLLWLLPLLVfGFLLALIfNYLEHYG--------GDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPG 224

                         250       260
                  ....*....|....*....|....*
gi 126157490  435 MPRHNYHKVAPLVKSLCAKHGLQYI 459
Cdd:pfam00487 225 VPWYRLPKLHRRLREALPEHGLPYR 249
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 66-138 6.77e-23

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: 91.91  E-value: 6.77e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126157490   66 TWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRRVLNHYAGQDATDAFRAMHLDLGMVKLYLKPLLIGEL 138
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGEL 73
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 65-138 9.86e-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: 78.16  E-value: 9.86e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126157490  65 YTWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRRVLNHYAGQDATDAFRAMHLDLGMVKLYLKPLLIGEL 138
Cdd:COG5274   18 YTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPHSPKAERLLESYRIGRL 91
PLN02252 PLN02252
nitrate reductase [NADPH]
 63-148 2.40e-09

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 59.69  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  63 NLYTWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRRVLNHYAGQDATDAFRAMHLDlgMVKLYLKPLLIGELSPEE 142
Cdd:PLN02252 518 KQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSD--KAKKMLEDYRIGELVTTG 595


                 ....*.
gi 126157490 143 PSQEKN 148
Cdd:PLN02252 596 AAASSS 601
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 206-456 4.75e-63

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: 203.64  E-value: 4.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 206 ILISFLLTVSQAQCSFLQHDLGHLSMFKKSKWNHLMHKFVMChLKGLSADWWNYRHFQHHVKPNIYPKDPDIDVGPLFLV 285
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 286 GDTQPIKYGKKKIKyidYEKQHLYFYMVALPFLMpvyfnlqsmqvmylrkywmdiawvssfyirYFItfgpfygifgtvl 365
Cdd:cd03506   80 SEPAFGKDQKKRFL---HRYQHFYFFPLLALLLL------------------------------AFL------------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 366 liyLVKFIESPWIAYVTQMSHIPMKM---SSEENHDWLSTQVVATCNIEQSFFNDWFTGHLNFQIEHHLFPTMPRHNYHK 442
Cdd:cd03506  114 ---VVQLAGGLWLAVVFQLNHFGMPVedpPGESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                        250
                 ....*....|....
gi 126157490 443 VAPLVKSLCAKHGL 456
Cdd:cd03506  191 VAPLVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 65-478 1.49e-56

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 196.45  E-value: 1.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  65 YTWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRrVLNHYAGQDATDAFRAMHLdlGMVKLYLKPLLIGELSPEEPS 144
Cdd:PLN03198 106 HLLSEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFHA--ASTWKILQDFYIGDVDNVEPT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 145 QEknknaqLVEDFRELRKTLEAMNMF-SANLRFFFLHLAQILILEISAWLIlhHFGSSWLVTILISFLLTVSQAQCSFLQ 223
Cdd:PLN03198 183 PE------LLKDFRDLRALFLREQLFkSSKLYYVFKLLTNIAIFAASIAII--CCSKSISAVLASACMMALCFQQCGWLS 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 224 HDLGHLSMFKKSKWNHLMHKFVMCHLKGLSADWWNYRHFQHHVKPN----IY-PKDPDIDVGPLFLVG-DTQPIKYGKKK 297
Cdd:PLN03198 255 HDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNecdqLYqPIDEDIDTLPLIAWSkDILATVENKTF 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 298 IKYIDYekQHLYFymVALPFlmpvyfnlqsmqvmYLRKYWMDIAWVSS------------------FYIRYFITFGpFYG 359
Cdd:PLN03198 335 LRILQY--QHLFF--MALLF--------------FARGSWLFWSWRYTstaklapadrllekgtilFHYFWFIGTA-CYL 395

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 360 IFGTVLLIYLV--KFIESPWIAYVTQMSHIPMKMSSEeNHDWLSTQVVATCNIEQSFFNDWFTGHLNFQIEHHLFPTMPR 437
Cdd:PLN03198 396 LPGWKPLVWMAvtELMCGMLLGFVFVLSHNGMEVYNK-SKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPR 474

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 126157490 438 HNYHKVAPLVKSLCAKHGLQYINKPILKAFGDIVRSLKKSA 478
Cdd:PLN03198 475 HNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKEVA 515
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 65-458 1.74e-48

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 173.69  E-value: 1.74e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  65 YTWQEIQRHSQEADQWLVIDRKVYNVTDWAgKHPGGRRVLNHyAGQDATDAFRAMHLDlGMVKLyLKPLLIGELSPEEPS 144
Cdd:PLN03199  26 ISWQEVKKHASPDDAWIIHQNKVYDVSNWH-DHPGGAVIFTH-AGDDMTDIFAAFHAP-GSQAL-MKKFYIGDLIPESTE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 145 QEKNKNAQLVEDFRELRKTLEAMNMFSANLRFFFLHLAQILILEISAWLILHHFGSSWlVTILISFLLTVSQAQCSFLQH 224
Cdd:PLN03199 102 HKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLFNMAIWAAACALVFYSDRFA-MHIASALLLGLFFQQCGWLAH 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 225 DLGHLSMFKKSKWNHLMHKFVMCHLKGLSADWWNYRHFQHHVKPNIYPK-------DPDIDVGPLFLVGDTQPIKYGKKK 297
Cdd:PLN03199 181 DFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqdgDPDIDTMPLLAWSLKQAQSFREIN 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 298 IKYIDYE------KQHLYFYMVALPFLMPVYFN-------------------LQSMQVMY---------LRKYWMDIawV 343
Cdd:PLN03199 261 ADGKDSGfvkfaiKFQAFFYFPILLLARISWLNesfkcafglgaasenaaleLEAKGLQYpllekagilLHYAWMFT--L 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 344 SSFYIRYFITFGPFYGIFGTVLLIYLvkfiespwIAYVTQMSHIPMKM-SSEENHDWLSTQVVATCNIE-----QSFFND 417
Cdd:PLN03199 339 SSGFGRFSFAYSAFYFFTATASCGFF--------LAIVFGLGHNGMATyDADARPDFWKLQVTTTRNIIgghgfPQAFVD 410

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 126157490 418 WFTGHLNFQIEHHLFPTMPRHNYHKVAPLVKSLCAKHGLQY 458
Cdd:PLN03199 411 WFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKY 451
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
144-478 2.49e-42

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 152.96  E-value: 2.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 144 SQEKNKNAQLVEDFRELRKTLEAmNMFSANLRFFFLhLAQILILEISAWLIlhhFGSSWLVtILISFLLTVSQAQCSFLQ 223
Cdd:COG3239    2 TTATPLTPADEAELRALRARLRA-LLGRRDWRYLLK-LALTLALLAALWLL---LSWSWLA-LLAALLLGLALAGLFSLG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 224 HDLGHLSMFKKSKWNHLMHkFVMCHLKGLSADWWNYRHFQHHVKPNIYPKDPDIDVGplflvgdtqpikygkkkikYIDY 303
Cdd:COG3239   76 HDAGHGSLFRSRWLNDLLG-RLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYG-------------------VQAW 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 304 EKQHLYFYMVALPFLMPVYFN-------LQSMQVMYLRKYWMDIAWVSSFYIRYFITFgpFYGIFGTVLLIYLV-KFIES 375
Cdd:COG3239  136 RPLYLFQHLLRFFLLGLGGLYwllaldfLPLRGRLELKERRLEALLLLLFLAALLALL--LALGWWAVLLFWLLpLLVAG 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 376 PWIAYVTQMSHIPMKMSSEENHDwlstQVVATCNIEQSFFNDWFTGHLNFQIEHHLFPTMPRHNYHKVAPLVKSLCAKHG 455
Cdd:COG3239  214 LLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYG 289

                        330       340
                 ....*....|....*....|...
gi 126157490 456 LQYINKPILKAFGDIVRSLKKSA 478
Cdd:COG3239  290 LPYTEGSLLRSYREVLRLLRRLG 312
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 201-459 6.93e-25

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: 103.19  E-value: 6.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  201 SWLVTILISFLLTVSQAQCSFLQHDLGHLSMFKKSKWNHLMHKFVMCH---LKGLSADWWNYRHFQHHVKPNIYPKDPDI 277
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLGRLaglPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  278 DVGPLFLVGDTQPIKYGKKKIkyidyekQHLYFYMVALPFLMPVYFNLQSMQVMYLRKYWMDIAWVSsFYIRYFITFGPF 357
Cdd:pfam00487  81 APLASRFRGLLRYLLRWLLGL-------LVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLL-LLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  358 YGIFGTVLLIYLVKFIE-SPWIAYV-TQMSHIPmkmsseenHDWLSTQVVATCNIEQ-SFFNDWFTGHLNFQIEHHLFPT 434
Cdd:pfam00487 153 LGLGGLLLLLWLLPLLVfGFLLALIfNYLEHYG--------GDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPG 224

                         250       260
                  ....*....|....*....|....*
gi 126157490  435 MPRHNYHKVAPLVKSLCAKHGLQYI 459
Cdd:pfam00487 225 VPWYRLPKLHRRLREALPEHGLPYR 249
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 66-138 6.77e-23

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: 91.91  E-value: 6.77e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126157490   66 TWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRRVLNHYAGQDATDAFRAMHLDLGMVKLYLKPLLIGEL 138
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGEL 73
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 65-138 9.86e-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: 78.16  E-value: 9.86e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126157490  65 YTWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRRVLNHYAGQDATDAFRAMHLDLGMVKLYLKPLLIGEL 138
Cdd:COG5274   18 YTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPHSPKAERLLESYRIGRL 91
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 206-279 2.38e-10

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: 57.86  E-value: 2.38e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126157490 206 ILISFLLTVSQAQCSFLQHDLGHLSMFKKSKWNHLMHKFVMCHLkGLSADWWNYRHFQHHVKPNIYPKDPDIDV 279
Cdd:cd01060    2 LLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDSAV 74
PLN02252 PLN02252
nitrate reductase [NADPH]
 63-148 2.40e-09

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 59.69  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490  63 NLYTWQEIQRHSQEADQWLVIDRKVYNVTDWAGKHPGGRRVLNHYAGQDATDAFRAMHLDlgMVKLYLKPLLIGELSPEE 142
Cdd:PLN02252 518 KQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSD--KAKKMLEDYRIGELVTTG 595


                 ....*.
gi 126157490 143 PSQEKN 148
Cdd:PLN02252 596 AAASSS 601
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 177-441 3.94e-06

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: 47.99  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 177 FFLHLAQILILEISAWLILHHFgSSWLVTILISFLLTVSQAQCSFLQHDLGHLSMFKKSKWN----HLMHKFVMC--HLk 250
Cdd:cd03507    6 SLSYLAPDILLLALLALAASLL-LSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNdivgHILHSPLLVpyHS- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 251 glsadwWNYRHFQHHVKPNiypkdpdidvgplFLVGD--TQPIKygkkkikyidyEKQhlyfymVALPFLMPVYFNLQSM 328
Cdd:cd03507   84 ------WRISHNRHHAHTG-------------NLEGDevWVPVT-----------EEE------YAELPKRLPYRLYRNP 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 329 QVMYLrkywmdiawvssfyiryfitFGPFYGIFGTVLLIYLVkfiesPWIAYVTQMS----------HIPMKmsSEENHD 398
Cdd:cd03507  128 FLMLS--------------------LGWPYYLLLNVLLYYLI-----PYLVVNAWLVlitylqhtfpDIPWY--RADEWN 180

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 126157490 399 WLSTQVVATCNIEQSFFNDWFTGHLNFQIEHHLFPTMPrhNYH 441
Cdd:cd03507  181 FAQAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIP--HYN 221
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 174-281 8.98e-06

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: 47.37  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 174 LRFFFLHLAQILIleiSAWLILHHFGSSWLVTILisFLLTVSQAQCSFLQHDLGHLSMFKkSKWNHLMHKFVMCHLKGLS 253
Cdd:cd03511   18 LLDTALWLGALAV---SGILIAWTWGSWWALPAF--LVYGVLYAALFARWHECVHGTAFA-TRWLNDAVGQIAGLMILLP 91

                         90       100
                 ....*....|....*....|....*...
gi 126157490 254 ADWWNYRHFQHHVKPNIYPKDPDIDVGP 281
Cdd:cd03511   92 PDFFRWSHARHHRYTQIPGRDPELAVPR 119
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 198-285 2.50e-03

This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in Bradyrhizobium japonicum USDA110, and other related proteins. Dihydrorhizobitoxine desaturase is reported to be involved in the final step of rhizobitoxine biosynthesis. This domain family appears to be structurally related to the membrane fatty acid desaturases and the alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXX(X)HH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239587 [Multi-domain]  Cd Length: 175  Bit Score: 38.80  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157490 198 FGSSWLVtILISFLLTVSQAQCSF-LQHDLGHLSMFKKSKWNhlmhKFVMCHLKG--LSADWWNYR--HFQHHVKPNIyP 272
Cdd:cd03510   14 AWPNWLA-YLLAVLLIGARQRALAiLMHDAAHGLLFRNRRLN----DFLGNWLAAvpIFQSLAAYRrsHLKHHRHLGT-E 87

                         90
                 ....*....|...
gi 126157490 273 KDPDIDVGPLFLV 285
Cdd:cd03510   88 DDPDLALYLLLWL 100
 
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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