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Conserved domains on  [gi|1190339459|ref|WP_085916991|]
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MULTISPECIES: acyl-CoA desaturase [Acinetobacter]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
9-360 5.45e-65

Fatty acid desaturase [Lipid transport and metabolism];


:

Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 209.59  E-value: 5.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459   9 SKSAHLTPEQIEEFgrrvEQIRQDVMQSLGEQDAKYIYKVRNFVRYTEIAsrgmLMFGGWiPPVWLLGTGLLGISKIVEN 88
Cdd:COG3239     2 TTATPLTPADEAEL----RALRARLRALLGRRDWRYLLKLALTLALLAAL----WLLLSW-SWLALLAALLLGLALAGLF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459  89 MeLGHNVMHGQFD---WLNEpsLNGNTYDWDTIASGDDWRETHNYvHHTYTNIVGKDHDVGYGIlrvsdqQKWEPRHLFN 165
Cdd:COG3239    73 S-LGHDAGHGSLFrsrWLND--LLGRLLGLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGV------QAWRPLYLFQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 166 IPLALQL--MFFFEWYVGVQNLHLEdalvyKTKSWKQVWKDAAKVRKKATRQILkDYVFFPvisgpmFLPVFAGNVVANI 243
Cdd:COG3239   143 HLLRFFLlgLGGLYWLLALDFLPLR-----GRLELKERRLEALLLLLFLAALLA-LLLALG------WWAVLLFWLLPLL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 244 IRNLWSSAVIFNGHFTEDAETFEpdntdtetkaewYLRQIRGSSNFSGTEWLHFMSGNLSHQIEHHLFPDMPANRYKEVA 323
Cdd:COG3239   211 VAGLLLGLRFYLEHRGEDTGDGE------------YRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAH 278

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1190339459 324 PKIKALCAEYGINYNEANFMRQFWSVWVRLAKCSLPN 360
Cdd:COG3239   279 RILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPA 315
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
9-360 5.45e-65

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 209.59  E-value: 5.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459   9 SKSAHLTPEQIEEFgrrvEQIRQDVMQSLGEQDAKYIYKVRNFVRYTEIAsrgmLMFGGWiPPVWLLGTGLLGISKIVEN 88
Cdd:COG3239     2 TTATPLTPADEAEL----RALRARLRALLGRRDWRYLLKLALTLALLAAL----WLLLSW-SWLALLAALLLGLALAGLF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459  89 MeLGHNVMHGQFD---WLNEpsLNGNTYDWDTIASGDDWRETHNYvHHTYTNIVGKDHDVGYGIlrvsdqQKWEPRHLFN 165
Cdd:COG3239    73 S-LGHDAGHGSLFrsrWLND--LLGRLLGLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGV------QAWRPLYLFQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 166 IPLALQL--MFFFEWYVGVQNLHLEdalvyKTKSWKQVWKDAAKVRKKATRQILkDYVFFPvisgpmFLPVFAGNVVANI 243
Cdd:COG3239   143 HLLRFFLlgLGGLYWLLALDFLPLR-----GRLELKERRLEALLLLLFLAALLA-LLLALG------WWAVLLFWLLPLL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 244 IRNLWSSAVIFNGHFTEDAETFEpdntdtetkaewYLRQIRGSSNFSGTEWLHFMSGNLSHQIEHHLFPDMPANRYKEVA 323
Cdd:COG3239   211 VAGLLLGLRFYLEHRGEDTGDGE------------YRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAH 278

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1190339459 324 PKIKALCAEYGINYNEANFMRQFWSVWVRLAKCSLPN 360
Cdd:COG3239   279 RILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPA 315
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 74-335 2.19e-51

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: 170.52  E-value: 2.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459  74 LLGTGLLGISKIVeNMELGHNVMHGQFD---WLNEpsLNGNTYDWDTIASGDDWRETHNyVHHTYTNIVGKDHDVGYGIL 150
Cdd:cd03506     1 LLLAILLGLFWAQ-GGFLAHDAGHGQVFknrWLNK--LLGLTVGNLLGASAGWWKNKHN-VHHAYTNILGHDPDIDTLPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 151 RVSDQQKWEPRHLFNIPLALQLMFFFewyvgvqnlhledalvyktkswkqvwkdaakvrkkatrqilkdyvffpvisgPM 230
Cdd:cd03506    77 LARSEPAFGKDQKKRFLHRYQHFYFF----------------------------------------------------PL 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 231 FLPVFAGNVVANIIRNLWSSAVIFNGHFTEDAETFEpdntdTETKAEWYLRQIRGSSNFSGTEWLHFMSGNLSHQIEHHL 310
Cdd:cd03506   105 LALLLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDPP-----GESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHL 179

                         250       260
                  ....*....|....*....|....*
gi 1190339459 311 FPDMPANRYKEVAPKIKALCAEYGI 335
Cdd:cd03506   180 FPTMPRHNYPKVAPLVRELCKKHGL 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 72-339 9.01e-17

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: 79.31  E-value: 9.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459  72 VWLLGTG--LLGISKIVENMELGHNVMHGQF-------DWLNEpsLNGNTYDWDTIASGDDWRETHNyVHHTYTNivGKD 142
Cdd:pfam00487   1 SWLALLLalLLGLFLLGITGSLAHEASHGALfkkrrlnRWLND--LLGRLAGLPLGISYSAWRIAHL-VHHRYTN--GPD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 143 HDVGYGILRvsdqQKWEPRHlfniplalqlMFFFEWYVGVQNLHLEDALVYKtkswkqVWKDAAKVRKKATRQILKDYVF 222
Cdd:pfam00487  76 KDPDTAPLA----SRFRGLL----------RYLLRWLLGLLVLAWLLALVLP------LWLRRLARRKRPIKSRRRRWRL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 223 FPVIsgpMFLPVFAGNVVANIIRNLWSSAVIFNGHFTEDAETFEPDNTDTETKAEWYLRQIRGSSNF-SGTEWLHFMSGN 301
Cdd:pfam00487 136 IAWL---LLLAAWLGLWLGFLGLGGLLLLLWLLPLLVFGFLLALIFNYLEHYGGDWGERPVETTRSIrSPNWWLNLLTGN 212

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1190339459 302 LSHQIEHHLFPDMPANRYKEVAPKIKALCAEYGINYNE 339
Cdd:pfam00487 213 LNYHIEHHLFPGVPWYRLPKLHRRLREALPEHGLPYRS 250
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 277-339 5.93e-08

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 54.31  E-value: 5.93e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190339459 277 EWYLRQIRGSSNFSGTEWLHFMSGNLSHQIEHHLFPDMPANRYKEVAPKIKALCAEYGINYNE 339
Cdd:PLN03198  435 EFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYED 497
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
9-360 5.45e-65

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 209.59  E-value: 5.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459   9 SKSAHLTPEQIEEFgrrvEQIRQDVMQSLGEQDAKYIYKVRNFVRYTEIAsrgmLMFGGWiPPVWLLGTGLLGISKIVEN 88
Cdd:COG3239     2 TTATPLTPADEAEL----RALRARLRALLGRRDWRYLLKLALTLALLAAL----WLLLSW-SWLALLAALLLGLALAGLF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459  89 MeLGHNVMHGQFD---WLNEpsLNGNTYDWDTIASGDDWRETHNYvHHTYTNIVGKDHDVGYGIlrvsdqQKWEPRHLFN 165
Cdd:COG3239    73 S-LGHDAGHGSLFrsrWLND--LLGRLLGLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGV------QAWRPLYLFQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 166 IPLALQL--MFFFEWYVGVQNLHLEdalvyKTKSWKQVWKDAAKVRKKATRQILkDYVFFPvisgpmFLPVFAGNVVANI 243
Cdd:COG3239   143 HLLRFFLlgLGGLYWLLALDFLPLR-----GRLELKERRLEALLLLLFLAALLA-LLLALG------WWAVLLFWLLPLL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 244 IRNLWSSAVIFNGHFTEDAETFEpdntdtetkaewYLRQIRGSSNFSGTEWLHFMSGNLSHQIEHHLFPDMPANRYKEVA 323
Cdd:COG3239   211 VAGLLLGLRFYLEHRGEDTGDGE------------YRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAH 278

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1190339459 324 PKIKALCAEYGINYNEANFMRQFWSVWVRLAKCSLPN 360
Cdd:COG3239   279 RILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPA 315
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 74-335 2.19e-51

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: 170.52  E-value: 2.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459  74 LLGTGLLGISKIVeNMELGHNVMHGQFD---WLNEpsLNGNTYDWDTIASGDDWRETHNyVHHTYTNIVGKDHDVGYGIL 150
Cdd:cd03506     1 LLLAILLGLFWAQ-GGFLAHDAGHGQVFknrWLNK--LLGLTVGNLLGASAGWWKNKHN-VHHAYTNILGHDPDIDTLPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 151 RVSDQQKWEPRHLFNIPLALQLMFFFewyvgvqnlhledalvyktkswkqvwkdaakvrkkatrqilkdyvffpvisgPM 230
Cdd:cd03506    77 LARSEPAFGKDQKKRFLHRYQHFYFF----------------------------------------------------PL 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 231 FLPVFAGNVVANIIRNLWSSAVIFNGHFTEDAETFEpdntdTETKAEWYLRQIRGSSNFSGTEWLHFMSGNLSHQIEHHL 310
Cdd:cd03506   105 LALLLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDPP-----GESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHL 179

                         250       260
                  ....*....|....*....|....*
gi 1190339459 311 FPDMPANRYKEVAPKIKALCAEYGI 335
Cdd:cd03506   180 FPTMPRHNYPKVAPLVRELCKKHGL 204
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 72-339 9.01e-17

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: 79.31  E-value: 9.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459  72 VWLLGTG--LLGISKIVENMELGHNVMHGQF-------DWLNEpsLNGNTYDWDTIASGDDWRETHNyVHHTYTNivGKD 142
Cdd:pfam00487   1 SWLALLLalLLGLFLLGITGSLAHEASHGALfkkrrlnRWLND--LLGRLAGLPLGISYSAWRIAHL-VHHRYTN--GPD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 143 HDVGYGILRvsdqQKWEPRHlfniplalqlMFFFEWYVGVQNLHLEDALVYKtkswkqVWKDAAKVRKKATRQILKDYVF 222
Cdd:pfam00487  76 KDPDTAPLA----SRFRGLL----------RYLLRWLLGLLVLAWLLALVLP------LWLRRLARRKRPIKSRRRRWRL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 223 FPVIsgpMFLPVFAGNVVANIIRNLWSSAVIFNGHFTEDAETFEPDNTDTETKAEWYLRQIRGSSNF-SGTEWLHFMSGN 301
Cdd:pfam00487 136 IAWL---LLLAAWLGLWLGFLGLGGLLLLLWLLPLLVFGFLLALIFNYLEHYGGDWGERPVETTRSIrSPNWWLNLLTGN 212

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1190339459 302 LSHQIEHHLFPDMPANRYKEVAPKIKALCAEYGINYNE 339
Cdd:pfam00487 213 LNYHIEHHLFPGVPWYRLPKLHRRLREALPEHGLPYRS 250
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 277-339 5.93e-08

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 54.31  E-value: 5.93e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190339459 277 EWYLRQIRGSSNFSGTEWLHFMSGNLSHQIEHHLFPDMPANRYKEVAPKIKALCAEYGINYNE 339
Cdd:PLN03198  435 EFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYED 497
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 74-150 5.85e-07

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: 47.85  E-value: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459  74 LLGTGLLGISKIVENMELGHNVMHGQFD---WLNEpsLNGNTYDWDTIASGDDWRETHNyVHHTYTNIVGKDHDVGYGIL 150
Cdd:cd01060     1 LLLALLLGLLGGLGLTVLAHELGHRSFFrsrWLNR--LLGALLGLALGGSYGWWRRSHR-RHHRYTNTPGKDPDSAVNYL 77
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 271-357 6.35e-07

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 51.19  E-value: 6.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190339459 271 DTETKAEWYLRQIRGSSNFSGTE-----WLHFMSGNLSHQIEHHLFPDMPANRYKEVAPKIKALCAEYGINYNEANFMRQ 345
Cdd:PLN03199  380 DADARPDFWKLQVTTTRNIIGGHgfpqaFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDG 459

                          90
                  ....*....|..
gi 1190339459 346 FWSVWVRLAKCS 357
Cdd:PLN03199  460 TMEVLHHLGKVA 471
 
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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