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Conserved domains on  [gi|1897919083|ref|WP_187404311|]
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MULTISPECIES: acyl-CoA desaturase [unclassified Corynebacterium]

Protein Classification

fatty acid desaturase family protein( domain architecture ID 11461513)

fatty acid desaturase family protein may remove two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; such as Mycobacterium tuberculosis NADPH-dependent stearoyl-CoA 9-desaturase

EC:  1.14.19.-
Gene Ontology:  GO:0046872|GO:0016020|GO:0006633|GO:0016717
PubMed:  15189125

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
18-376 4.01e-66

Fatty acid desaturase [Lipid transport and metabolism];


:

Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 214.59  E-value: 4.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  18 AEIGRRFAEIEKQHRDSLGQKDARYIRTLIRIQRTLEVTgrgllmlptagmalnkLGMLPKSWkntahwgVKWAGASALG 97
Cdd:COG3239     9 PADEAELRALRARLRALLGRRDWRYLLKLALTLALLAAL----------------WLLLSWSW-------LALLAALLLG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  98 LAKILENLeIGHNTMHGQWDWMN-DPEIHSATWEWDNSCPSSGWKHSHNfVHHKYTNVLGMDNDVGYGIlrvtrdRRWKP 176
Cdd:COG3239    66 LALAGLFS-LGHDAGHGSLFRSRwLNDLLGRLLGLPLGTPYDAWRRSHN-RHHAYTNDPGKDPDIGYGV------QAWRP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 177 STLLQ-PVTNVVLA-SLFQWAVAFYDVElgrvFAGKKSWDEARPQLMEVLNKSGRQVLkDYVLFPAMAgpryreVAFANM 254
Cdd:COG3239   138 LYLFQhLLRFFLLGlGGLYWLLALDFLP----LRGRLELKERRLEALLLLLFLAALLA-LLLALGWWA------VLLFWL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 255 MANLARNLWAYAVIFCGHFPDDAEtftkeqyntedkSEWYLRQMLGSANFHGGLALSVLSGNLNYQIEHHLFPDMPSNRL 334
Cdd:COG3239   207 LPLLVAGLLLGLRFYLEHRGEDTG------------DGEYRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRL 274

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1897919083 335 AQISKQVQQICREYDLPYNTGSFPKQFFQVQRTLLKLSLPDR 376
Cdd:COG3239   275 PEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPAR 316
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
18-376 4.01e-66

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 214.59  E-value: 4.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  18 AEIGRRFAEIEKQHRDSLGQKDARYIRTLIRIQRTLEVTgrgllmlptagmalnkLGMLPKSWkntahwgVKWAGASALG 97
Cdd:COG3239     9 PADEAELRALRARLRALLGRRDWRYLLKLALTLALLAAL----------------WLLLSWSW-------LALLAALLLG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  98 LAKILENLeIGHNTMHGQWDWMN-DPEIHSATWEWDNSCPSSGWKHSHNfVHHKYTNVLGMDNDVGYGIlrvtrdRRWKP 176
Cdd:COG3239    66 LALAGLFS-LGHDAGHGSLFRSRwLNDLLGRLLGLPLGTPYDAWRRSHN-RHHAYTNDPGKDPDIGYGV------QAWRP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 177 STLLQ-PVTNVVLA-SLFQWAVAFYDVElgrvFAGKKSWDEARPQLMEVLNKSGRQVLkDYVLFPAMAgpryreVAFANM 254
Cdd:COG3239   138 LYLFQhLLRFFLLGlGGLYWLLALDFLP----LRGRLELKERRLEALLLLLFLAALLA-LLLALGWWA------VLLFWL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 255 MANLARNLWAYAVIFCGHFPDDAEtftkeqyntedkSEWYLRQMLGSANFHGGLALSVLSGNLNYQIEHHLFPDMPSNRL 334
Cdd:COG3239   207 LPLLVAGLLLGLRFYLEHRGEDTG------------DGEYRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRL 274

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1897919083 335 AQISKQVQQICREYDLPYNTGSFPKQFFQVQRTLLKLSLPDR 376
Cdd:COG3239   275 PEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPAR 316
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 90-350 5.79e-49

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: 165.89  E-value: 5.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  90 WAGASALGLAKILeNLEIGHNTMHGQWD-WMNDPEIHSATWEWDNSCPSSGWKHSHNfVHHKYTNVLGMDNDVGYGILRV 168
Cdd:cd03506     1 LLLAILLGLFWAQ-GGFLAHDAGHGQVFkNRWLNKLLGLTVGNLLGASAGWWKNKHN-VHHAYTNILGHDPDIDTLPLLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 169 TRDRRWKPSTLLQPVTNvvlaslFQWavafydvelgrvfagkkswdearpqlmevlnksgrqvlkdyVLFPAMAGPryre 248
Cdd:cd03506    79 RSEPAFGKDQKKRFLHR------YQH-----------------------------------------FYFFPLLAL---- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 249 VAFANMMANLARNLWAYAVIFCGHFPDDAETFtkeqyNTEDKSEWYLRQMLGSANFHGGLALSVLSGNLNYQIEHHLFPD 328
Cdd:cd03506   108 LLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDP-----PGESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPT 182

                         250       260
                  ....*....|....*....|..
gi 1897919083 329 MPSNRLAQISKQVQQICREYDL 350
Cdd:cd03506   183 MPRHNYPKVAPLVRELCKKHGL 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 90-356 6.23e-19

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: 85.86  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  90 WAGASALGLAKILENLEIGHNTMHGQ-------WDWMNDPEIHSATWEWDNscPSSGWKHSHNfVHHKYTNvlGMDNDVG 162
Cdd:pfam00487   5 LLLALLLGLFLLGITGSLAHEASHGAlfkkrrlNRWLNDLLGRLAGLPLGI--SYSAWRIAHL-VHHRYTN--GPDKDPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 163 YGILRVTRDRRWKPSTLLqpvtnVVLASLFQWAVAFYDVELGRVFAgkkswdeaRPQLMEVLNKSGRQVLKDYVLFPAMA 242
Cdd:pfam00487  80 TAPLASRFRGLLRYLLRW-----LLGLLVLAWLLALVLPLWLRRLA--------RRKRPIKSRRRRWRLIAWLLLLAAWL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 243 GPryreVAFANMMANLARNLWAYAVIFCGHFpddaeTFTKEQYNTEDKSEWYLRQMLGSANFH-GGLALSVLSGNLNYQI 321
Cdd:pfam00487 147 GL----WLGFLGLGGLLLLLWLLPLLVFGFL-----LALIFNYLEHYGGDWGERPVETTRSIRsPNWWLNLLTGNLNYHI 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1897919083 322 EHHLFPDMPSNRLAQISKQVQQICREYDLPYNTGS 356
Cdd:pfam00487 218 EHHLFPGVPWYRLPKLHRRLREALPEHGLPYRSLG 252
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 285-379 3.61e-08

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 55.43  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 285 YNTEDKSEWYLRQMLGSANFHGGLALSV-----LSGNLNYQIEHHLFPDMPSNRLAQISKQVQQICREYDLPYNTGSFPK 359
Cdd:PLN03199  379 YDADARPDFWKLQVTTTRNIIGGHGFPQafvdwFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVD 458

                          90       100
                  ....*....|....*....|
gi 1897919083 360 QFFQVQRTLLKLSlpDRFLV 379
Cdd:PLN03199  459 GTMEVLHHLGKVA--DDFLV 476
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
18-376 4.01e-66

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 214.59  E-value: 4.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  18 AEIGRRFAEIEKQHRDSLGQKDARYIRTLIRIQRTLEVTgrgllmlptagmalnkLGMLPKSWkntahwgVKWAGASALG 97
Cdd:COG3239     9 PADEAELRALRARLRALLGRRDWRYLLKLALTLALLAAL----------------WLLLSWSW-------LALLAALLLG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  98 LAKILENLeIGHNTMHGQWDWMN-DPEIHSATWEWDNSCPSSGWKHSHNfVHHKYTNVLGMDNDVGYGIlrvtrdRRWKP 176
Cdd:COG3239    66 LALAGLFS-LGHDAGHGSLFRSRwLNDLLGRLLGLPLGTPYDAWRRSHN-RHHAYTNDPGKDPDIGYGV------QAWRP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 177 STLLQ-PVTNVVLA-SLFQWAVAFYDVElgrvFAGKKSWDEARPQLMEVLNKSGRQVLkDYVLFPAMAgpryreVAFANM 254
Cdd:COG3239   138 LYLFQhLLRFFLLGlGGLYWLLALDFLP----LRGRLELKERRLEALLLLLFLAALLA-LLLALGWWA------VLLFWL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 255 MANLARNLWAYAVIFCGHFPDDAEtftkeqyntedkSEWYLRQMLGSANFHGGLALSVLSGNLNYQIEHHLFPDMPSNRL 334
Cdd:COG3239   207 LPLLVAGLLLGLRFYLEHRGEDTG------------DGEYRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRL 274

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1897919083 335 AQISKQVQQICREYDLPYNTGSFPKQFFQVQRTLLKLSLPDR 376
Cdd:COG3239   275 PEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPAR 316
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 90-350 5.79e-49

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: 165.89  E-value: 5.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  90 WAGASALGLAKILeNLEIGHNTMHGQWD-WMNDPEIHSATWEWDNSCPSSGWKHSHNfVHHKYTNVLGMDNDVGYGILRV 168
Cdd:cd03506     1 LLLAILLGLFWAQ-GGFLAHDAGHGQVFkNRWLNKLLGLTVGNLLGASAGWWKNKHN-VHHAYTNILGHDPDIDTLPLLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 169 TRDRRWKPSTLLQPVTNvvlaslFQWavafydvelgrvfagkkswdearpqlmevlnksgrqvlkdyVLFPAMAGPryre 248
Cdd:cd03506    79 RSEPAFGKDQKKRFLHR------YQH-----------------------------------------FYFFPLLAL---- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 249 VAFANMMANLARNLWAYAVIFCGHFPDDAETFtkeqyNTEDKSEWYLRQMLGSANFHGGLALSVLSGNLNYQIEHHLFPD 328
Cdd:cd03506   108 LLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDP-----PGESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPT 182

                         250       260
                  ....*....|....*....|..
gi 1897919083 329 MPSNRLAQISKQVQQICREYDL 350
Cdd:cd03506   183 MPRHNYPKVAPLVRELCKKHGL 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 90-356 6.23e-19

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: 85.86  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  90 WAGASALGLAKILENLEIGHNTMHGQ-------WDWMNDPEIHSATWEWDNscPSSGWKHSHNfVHHKYTNvlGMDNDVG 162
Cdd:pfam00487   5 LLLALLLGLFLLGITGSLAHEASHGAlfkkrrlNRWLNDLLGRLAGLPLGI--SYSAWRIAHL-VHHRYTN--GPDKDPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 163 YGILRVTRDRRWKPSTLLqpvtnVVLASLFQWAVAFYDVELGRVFAgkkswdeaRPQLMEVLNKSGRQVLKDYVLFPAMA 242
Cdd:pfam00487  80 TAPLASRFRGLLRYLLRW-----LLGLLVLAWLLALVLPLWLRRLA--------RRKRPIKSRRRRWRLIAWLLLLAAWL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 243 GPryreVAFANMMANLARNLWAYAVIFCGHFpddaeTFTKEQYNTEDKSEWYLRQMLGSANFH-GGLALSVLSGNLNYQI 321
Cdd:pfam00487 147 GL----WLGFLGLGGLLLLLWLLPLLVFGFL-----LALIFNYLEHYGGDWGERPVETTRSIRsPNWWLNLLTGNLNYHI 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1897919083 322 EHHLFPDMPSNRLAQISKQVQQICREYDLPYNTGS 356
Cdd:pfam00487 218 EHHLFPGVPWYRLPKLHRRLREALPEHGLPYRSLG 252
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 285-379 3.61e-08

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 55.43  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 285 YNTEDKSEWYLRQMLGSANFHGGLALSV-----LSGNLNYQIEHHLFPDMPSNRLAQISKQVQQICREYDLPYNTGSFPK 359
Cdd:PLN03199  379 YDADARPDFWKLQVTTTRNIIGGHGFPQafvdwFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVD 458

                          90       100
                  ....*....|....*....|
gi 1897919083 360 QFFQVQRTLLKLSlpDRFLV 379
Cdd:PLN03199  459 GTMEVLHHLGKVA--DDFLV 476
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 283-352 8.61e-08

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 54.31  E-value: 8.61e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083 283 EQYNTEdkSEWYLRQMLGSANFHGGLALSVLSGNLNYQIEHHLFPDMPSNRLAQISKQVQQICREYDLPY 352
Cdd:PLN03198  428 EVYNKS--KEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVY 495
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 90-198 1.23e-06

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: 47.46  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897919083  90 WAGASALGLAKILENLEIGHNTMHGQWD---WMNDpeIHSATWEWDNSCPSSGWKHSHNfVHHKYTNVLGMDNDVGYGIL 166
Cdd:cd01060     1 LLLALLLGLLGGLGLTVLAHELGHRSFFrsrWLNR--LLGALLGLALGGSYGWWRRSHR-RHHRYTNTPGKDPDSAVNYL 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1897919083 167 -RVTRDRRWKPSTLLQPVTNVVLASLFQWAVAF 198
Cdd:cd01060    78 eHYGGDRPFDTDGEWLRTTDNSRNGWLNLLLTG 110
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 265-327 1.35e-03

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: 38.61  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1897919083 265 YAVIFCGHFPDDAETFTKEQYNTedksewylrqmlGSANFHGGLALSVLSGNLNYQIEHHLFP 327
Cdd:cd01060    72 SAVNYLEHYGGDRPFDTDGEWLR------------TTDNSRNGWLNLLLTGGLGYHNEHHLFP 122
 
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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