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Conserved domains on  [gi|952543433|sp|A4KDP0|]
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RecName: Full=Acyl-lipid (8-3)-desaturase; AltName: Full=AN Delta(5)-fatty-acid desaturase; AltName: Full=Acyl-lipid 5-desaturase; AltName: Full=Delta-5 desaturase

Protein Classification

CYB5 and Delta6-FADS-like domain-containing protein( domain architecture ID 13427677)

CYB5 and Delta6-FADS-like domain-containing protein

Graphical summary

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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: ...
 146-395 8.72e-50

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: 167.43  E-value: 8.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 146 FAGIAMLGVVQGRCGWLMHEGGHYSLTGNIAFDRAIQVAcYGLGCGMSGAWWRNQHNKHHATPQKLQHDVDLDTLPLVAF 225
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLT-VGNLLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 226 HERIAakVKSPAMKAWLSMQAKLFAPVTTLLvalgwqlylhprhmlrtkhydelamlgirygLVGYLAANYGAGYVLacy 305
Cdd:cd03506   80 SEPAF--GKDQKKRFLHRYQHFYFFPLLALL-------------------------------LLAFLVVQLAGGLWL--- 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 306 llyvqlgAMYIFCN-FAVSHTHLPvvePNEHATWVEYAANHTTNCSPSWWCDWWMSYLNYQIEHHLYPSMPQFRHPKIAP 384
Cdd:cd03506  124 -------AVVFQLNhFGMPVEDPP---GESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPKVAP 193

                        250
                 ....*....|.
gi 952543433 385 RVKQLFEKHGL 395
Cdd:cd03506  194 LVRELCKKHGL 204
CYB5 super family cl34968
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 10-81 6.81e-12

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


The actual alignment was detected with superfamily member COG5274:

Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 61.21  E-value: 6.81e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 952543433  10 AAPPSAQLhEVDTPQEHDKKE---LVIGDRAYDVTNFVKRHPGG-KIIAYQVGTDATDAYKQFHVRSAKADKMLKS 81
Cdd:COG5274   11 AAAPEKTY-TLAEVATHNTLSdcwMAIDGNVYDLTEYIPKHPGGeAVILRWCGKDATEAFNTKHPHSPKAERLLES 85
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 146-395 8.72e-50

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: 167.43  E-value: 8.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 146 FAGIAMLGVVQGRCGWLMHEGGHYSLTGNIAFDRAIQVAcYGLGCGMSGAWWRNQHNKHHATPQKLQHDVDLDTLPLVAF 225
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLT-VGNLLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 226 HERIAakVKSPAMKAWLSMQAKLFAPVTTLLvalgwqlylhprhmlrtkhydelamlgirygLVGYLAANYGAGYVLacy 305
Cdd:cd03506   80 SEPAF--GKDQKKRFLHRYQHFYFFPLLALL-------------------------------LLAFLVVQLAGGLWL--- 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 306 llyvqlgAMYIFCN-FAVSHTHLPvvePNEHATWVEYAANHTTNCSPSWWCDWWMSYLNYQIEHHLYPSMPQFRHPKIAP 384
Cdd:cd03506  124 -------AVVFQLNhFGMPVEDPP---GESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPKVAP 193

                        250
                 ....*....|.
gi 952543433 385 RVKQLFEKHGL 395
Cdd:cd03506  194 LVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 4-423 4.06e-42

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 155.62  E-value: 4.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433   4 RDSYSYAAPPSAQLHEVDTPQEHDKKELVIGDRAYDVTNFVKRHPGGKIIAYQVGTDATDAYKQFHvrSAKADKMLKSLP 83
Cdd:PLN03198  95 RRSSKEKKSKSHLLSEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGSVISTYFGRDGTDAFSSFH--AASTWKILQDFY 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  84 SRPVHKgYSPRrADLIADFQEFTKQLEAEGMFEPSLPHVAYRLAEVIAMHVAGAALIWHGYTFAGI----AMLGVVQGRC 159
Cdd:PLN03198 173 IGDVDN-VEPT-PELLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAASIAIICCSKSISAVlasaCMMALCFQQC 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 160 GWLMHEGGHysltgNIAFDRAI--QVACYGLG---CGMSGAWWRNQHNKHHATPQKLQH-----DVDLDTLPLVAFHERI 229
Cdd:PLN03198 251 GWLSHDFLH-----NQVFETRWlnEVVGYLIGnavLGFSTGWWKEKHNLHHAAPNECDQlyqpiDEDIDTLPLIAWSKDI 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 230 AAKVKSPAMKAWLSMQAKLFAPVttLLVALGWQLYLHPRhmlrtkhYDELAMLGIRYGLV--GYLAANYGAGYVLACYLL 307
Cdd:PLN03198 326 LATVENKTFLRILQYQHLFFMAL--LFFARGSWLFWSWR-------YTSTAKLAPADRLLekGTILFHYFWFIGTACYLL 396

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 308 -----YVQLGAMYIFCN------FAVSHTHLPVVepNEHATWVEYAANHTTNCSPSWWCDWWMSYLNYQIEHHLYPSMPQ 376
Cdd:PLN03198 397 pgwkpLVWMAVTELMCGmllgfvFVLSHNGMEVY--NKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPR 474

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 952543433 377 FRHPKIAPRVKQLFEKHGLHYDVRGYFEAMADTFANLDNVAHAPEKK 423
Cdd:PLN03198 475 HNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKEVAEAAAEQ 521
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
92-420 6.31e-35

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 131.78  E-value: 6.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  92 SPRRADLIADFQEFTKQLEAEgMFEPSLPHVAYRLAEVIAMHVAGAALIWHGYTFAGIAMLGVVQGRCGWLMHEGGHYSL 171
Cdd:COG3239    5 TPLTPADEAELRALRARLRAL-LGRRDWRYLLKLALTLALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 172 TGNiAFDRAIQVACYGLGCGMSGAWWRNQHNKHHATPQKLQHDVDLdtlplvafHERIAAKVKSPAMKAWLSmqAKLFAP 251
Cdd:COG3239   84 FRS-RWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDI--------GYGVQAWRPLYLFQHLLR--FFLLGL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 252 VTTLLVALGWQLYLHPRHMLRTKHYDELAMLGIRYGLVGYLAAnYGAGYVLACYLLYVQLGAMYIFCNFAVSHTHLPVVE 331
Cdd:COG3239  153 GGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLLA-LGWWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 332 PNEHATWVeyaanHTTNCSPSWWCDWWMSYLNYQIEHHLYPSMPQFRHPKIAPRVKQLFEKHGLHYDVRGYFEAMADTFA 411
Cdd:COG3239  232 GEYRDQLL-----GSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLR 306


                 ....*....
gi 952543433 412 NLDNVAHAP 420
Cdd:COG3239  307 LLRRLGLPA 315
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 146-401 3.70e-24

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: 100.50  E-value: 3.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  146 FAGIAMLGVVQ-GRCGWLMHEGGHYSLTGNIAFDRAIQVA---CYGLGCGMSGAWWRNQHNKHHATPQKlqHDVDLDTLP 221
Cdd:pfam00487   5 LLLALLLGLFLlGITGSLAHEASHGALFKKRRLNRWLNDLlgrLAGLPLGISYSAWRIAHLVHHRYTNG--PDKDPDTAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  222 LVAFHERIAAKvkspamkawlsmqaklFAPVTTLLVALGWQLYLHPRHMLRTKHYDELAMLGIRYGLV---GYLAANYGA 298
Cdd:pfam00487  83 LASRFRGLLRY----------------LLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRliaWLLLLAAWL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  299 GYVLACYLLYVQLGAMYIFCNFAVSHTHLPVVEPNEHA--TWVEYAANHTTNC-SPSWWCDWWMSYLNYQIEHHLYPSMP 375
Cdd:pfam00487 147 GLWLGFLGLGGLLLLLWLLPLLVFGFLLALIFNYLEHYggDWGERPVETTRSIrSPNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 952543433  376 QFRHPKIAPRVKQLFEKHGLHYDVRG 401
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 10-81 6.81e-12

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


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 61.21  E-value: 6.81e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 952543433  10 AAPPSAQLhEVDTPQEHDKKE---LVIGDRAYDVTNFVKRHPGG-KIIAYQVGTDATDAYKQFHVRSAKADKMLKS 81
Cdd:COG5274   11 AAAPEKTY-TLAEVATHNTLSdcwMAIDGNVYDLTEYIPKHPGGeAVILRWCGKDATEAFNTKHPHSPKAERLLES 85
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 24-80 2.13e-10

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: 56.48  E-value: 2.13e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 952543433   24 QEHDKKE---LVIGDRAYDVTNFVKRHPGG-KIIAYQVGTDATDAYKQFHVRSAKADKMLK 80
Cdd:pfam00173   6 SKHNGDGdcwVAINGKVYDVTKFLKEHPGGeDVILSAAGKDATDAFEAIGHSEDAAEKLLK 66
PLN02252 PLN02252
nitrate reductase [NADPH]
 10-79 3.00e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 52.76  E-value: 3.00e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 952543433  10 AAPPSAQLHEVDTPQEHDKKE---LVIGDRAYDVTNFVKRHPGG-KIIAYQVGTDATDAYKQFHvrSAKADKML 79
Cdd:PLN02252 512 NTNTGSKQYTMSEVRKHNSEDscwIVVHGHVYDCTRFLKDHPGGaDSILINAGTDCTEEFDAIH--SDKAKKML 583
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 146-395 8.72e-50

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: 167.43  E-value: 8.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 146 FAGIAMLGVVQGRCGWLMHEGGHYSLTGNIAFDRAIQVAcYGLGCGMSGAWWRNQHNKHHATPQKLQHDVDLDTLPLVAF 225
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLT-VGNLLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 226 HERIAakVKSPAMKAWLSMQAKLFAPVTTLLvalgwqlylhprhmlrtkhydelamlgirygLVGYLAANYGAGYVLacy 305
Cdd:cd03506   80 SEPAF--GKDQKKRFLHRYQHFYFFPLLALL-------------------------------LLAFLVVQLAGGLWL--- 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 306 llyvqlgAMYIFCN-FAVSHTHLPvvePNEHATWVEYAANHTTNCSPSWWCDWWMSYLNYQIEHHLYPSMPQFRHPKIAP 384
Cdd:cd03506  124 -------AVVFQLNhFGMPVEDPP---GESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPKVAP 193

                        250
                 ....*....|.
gi 952543433 385 RVKQLFEKHGL 395
Cdd:cd03506  194 LVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 4-423 4.06e-42

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 155.62  E-value: 4.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433   4 RDSYSYAAPPSAQLHEVDTPQEHDKKELVIGDRAYDVTNFVKRHPGGKIIAYQVGTDATDAYKQFHvrSAKADKMLKSLP 83
Cdd:PLN03198  95 RRSSKEKKSKSHLLSEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGSVISTYFGRDGTDAFSSFH--AASTWKILQDFY 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  84 SRPVHKgYSPRrADLIADFQEFTKQLEAEGMFEPSLPHVAYRLAEVIAMHVAGAALIWHGYTFAGI----AMLGVVQGRC 159
Cdd:PLN03198 173 IGDVDN-VEPT-PELLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAASIAIICCSKSISAVlasaCMMALCFQQC 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 160 GWLMHEGGHysltgNIAFDRAI--QVACYGLG---CGMSGAWWRNQHNKHHATPQKLQH-----DVDLDTLPLVAFHERI 229
Cdd:PLN03198 251 GWLSHDFLH-----NQVFETRWlnEVVGYLIGnavLGFSTGWWKEKHNLHHAAPNECDQlyqpiDEDIDTLPLIAWSKDI 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 230 AAKVKSPAMKAWLSMQAKLFAPVttLLVALGWQLYLHPRhmlrtkhYDELAMLGIRYGLV--GYLAANYGAGYVLACYLL 307
Cdd:PLN03198 326 LATVENKTFLRILQYQHLFFMAL--LFFARGSWLFWSWR-------YTSTAKLAPADRLLekGTILFHYFWFIGTACYLL 396

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 308 -----YVQLGAMYIFCN------FAVSHTHLPVVepNEHATWVEYAANHTTNCSPSWWCDWWMSYLNYQIEHHLYPSMPQ 376
Cdd:PLN03198 397 pgwkpLVWMAVTELMCGmllgfvFVLSHNGMEVY--NKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPR 474

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 952543433 377 FRHPKIAPRVKQLFEKHGLHYDVRGYFEAMADTFANLDNVAHAPEKK 423
Cdd:PLN03198 475 HNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKEVAEAAAEQ 521
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
92-420 6.31e-35

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 131.78  E-value: 6.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  92 SPRRADLIADFQEFTKQLEAEgMFEPSLPHVAYRLAEVIAMHVAGAALIWHGYTFAGIAMLGVVQGRCGWLMHEGGHYSL 171
Cdd:COG3239    5 TPLTPADEAELRALRARLRAL-LGRRDWRYLLKLALTLALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 172 TGNiAFDRAIQVACYGLGCGMSGAWWRNQHNKHHATPQKLQHDVDLdtlplvafHERIAAKVKSPAMKAWLSmqAKLFAP 251
Cdd:COG3239   84 FRS-RWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDI--------GYGVQAWRPLYLFQHLLR--FFLLGL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 252 VTTLLVALGWQLYLHPRHMLRTKHYDELAMLGIRYGLVGYLAAnYGAGYVLACYLLYVQLGAMYIFCNFAVSHTHLPVVE 331
Cdd:COG3239  153 GGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLLA-LGWWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 332 PNEHATWVeyaanHTTNCSPSWWCDWWMSYLNYQIEHHLYPSMPQFRHPKIAPRVKQLFEKHGLHYDVRGYFEAMADTFA 411
Cdd:COG3239  232 GEYRDQLL-----GSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLR 306


                 ....*....
gi 952543433 412 NLDNVAHAP 420
Cdd:COG3239  307 LLRRLGLPA 315
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 18-417 1.74e-31

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 125.54  E-value: 1.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  18 HEVDTPQEHDKKELVIGDRAYDVTNFVKrHPGGKIIAYQVGTDATDAYKQFHVRSAKAdkMLKS------LPSRPVHKgy 91
Cdd:PLN03199  29 QEVKKHASPDDAWIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHAPGSQA--LMKKfyigdlIPESTEHK-- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  92 SPRRADLIADFQEFTKQLEAEGMFEPSLPHVAYRLAEVIAMHVAGAALIWHGYTF----AGIAMLGVVQGRCGWLMHEGG 167
Cdd:PLN03199 104 DPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLFNMAIWAAACALVFYSDRFamhiASALLLGLFFQQCGWLAHDFL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 168 HYSLTGNIAFDRAIQVACYGLGCGMSGAWWRNQHNKHHATPQ-------KLQHDVDLDTLPLVA--------FHERIAAK 232
Cdd:PLN03199 184 HHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNlhcssadAQDGDPDIDTMPLLAwslkqaqsFREINADG 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 233 VKSPAMKAWLSMQAKLFAPVtTLLVALGW------------------QLYLHPRHMlrtkHYDELAMLGI--RYGLVGYL 292
Cdd:PLN03199 264 KDSGFVKFAIKFQAFFYFPI-LLLARISWlnesfkcafglgaasenaALELEAKGL----QYPLLEKAGIllHYAWMFTL 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 293 AANYGA---GYVLACYLLYVQLGAMYIFCNFAVSHTHLPVVEPNEHATWVEYAANHTTNCS-----PSWWCDWWMSYLNY 364
Cdd:PLN03199 339 SSGFGRfsfAYSAFYFFTATASCGFFLAIVFGLGHNGMATYDADARPDFWKLQVTTTRNIIgghgfPQAFVDWFCGGLQY 418

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 952543433 365 QIEHHLYPSMPQFRHPKIAPRVKQLFEKHGLHYDVRGYFEAMADTFANLDNVA 417
Cdd:PLN03199 419 QVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHLGKVA 471
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 146-401 3.70e-24

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: 100.50  E-value: 3.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  146 FAGIAMLGVVQ-GRCGWLMHEGGHYSLTGNIAFDRAIQVA---CYGLGCGMSGAWWRNQHNKHHATPQKlqHDVDLDTLP 221
Cdd:pfam00487   5 LLLALLLGLFLlGITGSLAHEASHGALFKKRRLNRWLNDLlgrLAGLPLGISYSAWRIAHLVHHRYTNG--PDKDPDTAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  222 LVAFHERIAAKvkspamkawlsmqaklFAPVTTLLVALGWQLYLHPRHMLRTKHYDELAMLGIRYGLV---GYLAANYGA 298
Cdd:pfam00487  83 LASRFRGLLRY----------------LLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRliaWLLLLAAWL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433  299 GYVLACYLLYVQLGAMYIFCNFAVSHTHLPVVEPNEHA--TWVEYAANHTTNC-SPSWWCDWWMSYLNYQIEHHLYPSMP 375
Cdd:pfam00487 147 GLWLGFLGLGGLLLLLWLLPLLVFGFLLALIFNYLEHYggDWGERPVETTRSIrSPNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 952543433  376 QFRHPKIAPRVKQLFEKHGLHYDVRG 401
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 10-81 6.81e-12

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


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 61.21  E-value: 6.81e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 952543433  10 AAPPSAQLhEVDTPQEHDKKE---LVIGDRAYDVTNFVKRHPGG-KIIAYQVGTDATDAYKQFHVRSAKADKMLKS 81
Cdd:COG5274   11 AAAPEKTY-TLAEVATHNTLSdcwMAIDGNVYDLTEYIPKHPGGeAVILRWCGKDATEAFNTKHPHSPKAERLLES 85
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 24-80 2.13e-10

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: 56.48  E-value: 2.13e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 952543433   24 QEHDKKE---LVIGDRAYDVTNFVKRHPGG-KIIAYQVGTDATDAYKQFHVRSAKADKMLK 80
Cdd:pfam00173   6 SKHNGDGdcwVAINGKVYDVTKFLKEHPGGeDVILSAAGKDATDAFEAIGHSEDAAEKLLK 66
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 146-217 4.74e-09

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: 54.01  E-value: 4.74e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 952543433 146 FAGIAMLGVVQG-RCGWLMHEGGHYSLTGNIAFDRAIQVACyGLGCGMSGAWWRNQHNKHHATPQKLQHDVDL 217
Cdd:cd01060    1 LLLALLLGLLGGlGLTVLAHELGHRSFFRSRWLNRLLGALL-GLALGGSYGWWRRSHRRHHRYTNTPGKDPDS 72
PLN02252 PLN02252
nitrate reductase [NADPH]
 10-79 3.00e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 52.76  E-value: 3.00e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 952543433  10 AAPPSAQLHEVDTPQEHDKKE---LVIGDRAYDVTNFVKRHPGG-KIIAYQVGTDATDAYKQFHvrSAKADKML 79
Cdd:PLN02252 512 NTNTGSKQYTMSEVRKHNSEDscwIVVHGHVYDCTRFLKDHPGGaDSILINAGTDCTEEFDAIH--SDKAKKML 583
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 118-375 7.16e-05

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: 43.75  E-value: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 118 SLPHVAYRLAEVIAMHVAGAALIWhgytFAGIAMLGVVQGRCGW----LMHEGGHYSLTGNIAFDRAIqvacyglGCGMS 193
Cdd:cd03507    6 SLSYLAPDILLLALLALAASLLLS----WWLWPLYWIVQGLFLTglfvLGHDCGHGSFSDNRRLNDIV-------GHILH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 194 GAW------WRNQHNKHHATPQKLQHDVdlDTLPLVAFHERIAAKVKSPAMKAWLSMQAKlfapvttllvaLGWQLYLHp 267
Cdd:cd03507   75 SPLlvpyhsWRISHNRHHAHTGNLEGDE--VWVPVTEEEYAELPKRLPYRLYRNPFLMLS-----------LGWPYYLL- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 268 rhmlrtkhydeLAMLgiRYGLVGYLAANYGAGyvlacYLLYVQlgamyifcnfavsHTH--LPVVEPNEHaTWVEYAANH 345
Cdd:cd03507  141 -----------LNVL--LYYLIPYLVVNAWLV-----LITYLQ-------------HTFpdIPWYRADEW-NFAQAGLLG 188

                        250       260       270
                 ....*....|....*....|....*....|
gi 952543433 346 TTNCSPSWWCDWWMSYLNYQIEHHLYPSMP 375
Cdd:cd03507  189 TVDRDYGGWLNWLTHIIGTHVAHHLFPRIP 218
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 131-405 7.24e-04

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: 41.20  E-value: 7.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 131 AMHVAGA-ALIWHGYTFAGIAML--GVVQGRCGWLMHEGGHYSltgniAFD-RAIQVACY---GLGCGMSGAWWRNQHNK 203
Cdd:cd03511   27 ALAVSGIlIAWTWGSWWALPAFLvyGVLYAALFARWHECVHGT-----AFAtRWLNDAVGqiaGLMILLPPDFFRWSHAR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 204 HH---------------ATPQKLQHDVDLDTLPLVAFHERIAAKVKSPAMkawlSMQAKLFAPVTTllvalgwqlylHPR 268
Cdd:cd03511  102 HHrytqipgrdpelavpRPPTLREYLLALSGLPYWWGKLRTVFRHAFGAV----SEAEKPFIPAEE-----------RPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 269 hMLRtkhyDELAMLGIrYGLVGYLAANYGAGYVLACYLLYVQLGAMYIFCNFAVSHTHLPVVEPNEHATWVEYaanhtTN 348
Cdd:cd03511  167 -VVR----EARAMLAV-YAGLIALSLYLGSPLLVLVWGLPLLLGQPILRLFLLAEHGGCPEDANDLRNTRTTL-----TN 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 952543433 349 cSPSWWCDWWMsylNYQIEHHLYPSMPQFRHPKIAPRVkqlfeKHGLHYDVRGYFEA 405
Cdd:cd03511  236 -PPLRFLYWNM---PYHAEHHMYPSVPFHALPKLHELI-----KDDLPVPYPGYIAV 283
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 343-381 7.15e-03

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


Pssm-ID: 239587 [Multi-domain]  Cd Length: 175  Bit Score: 37.26  E-value: 7.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 952543433 343 ANHTTNCSPSWWCDW--WMSYLNYQIEHHLYPSMPQFRHPK 381
Cdd:cd03510  130 ARNTRTTFGGWIERLlfAPHNINYHLEHHLFPAVPFYNLPK 170
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 129-223 9.63e-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: 36.88  E-value: 9.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952543433 129 VIAMHVAGAALIWHGYTFAgIAML--GVVQGRCGWLMHEGGHYSLTGNIAF-DRAIQVACyGLGCGMSGAWWRNQHNKHH 205
Cdd:cd03510    4 VIAAAVALALAWPNWLAYL-LAVLliGARQRALAILMHDAAHGLLFRNRRLnDFLGNWLA-AVPIFQSLAAYRRSHLKHH 81

                         90
                 ....*....|....*...
gi 952543433 206 ATPQKLQhDVDLDTLPLV 223
Cdd:cd03510   82 RHLGTED-DPDLALYLLL 98
 
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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