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Conserved domains on  [gi|42476248|ref|NP_571720|]
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fatty acid desaturase 2 [Danio rerio]

Protein Classification

Cyt-b5 and Delta6-FADS-like domain-containing protein (domain architecture ID 10445761)

Cyt-b5 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: ...
162-412 4.41e-63

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


:

Pssm-ID: 239583  Cd Length: 204  Bit Score: 204.80  E-value: 4.41e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 162 LIVAVILATAQSQAGWLQHDFGHLSVFKTSGMNHLVHKFVIGhLKGASAGWWNHRHFQHHAKPNIFKKDPDVNMLNAFVV 241
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 242 GNVQPveyGVKKIKHLPYNHQHKYFFFIGPPLLipvyfqfqifhnmishgmwvdllwcisyyvryflcytqfygvfwaiI 321
Cdd:cd03506  80 SEPAF---GKDQKKRFLHRYQHFYFFPLLALLL----------------------------------------------L 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 322 LFNFVRFMESHWFVWVTQMSRIPMNIDYEQN---QDWLSMQLVATCNIEQSAFNDWFSGHLNFQIEHHLFPTMPRHNYWR 398
Cdd:cd03506 111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGeskNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190
                       250
                ....*....|....
gi 42476248 399 AAPRVRSLCEKYGV 412
Cdd:cd03506 191 VAPLVRELCKKHGL 204
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
21-94 9.69e-24

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: 278597  Cd Length: 74  Bit Score: 94.21  E-value: 9.69e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42476248    21 YTWEEMQKHTKHGDQWVVVERKVYNVSQWVKRHPGGLRILGHYAGEDATEAFT-AFHPNlqLMRKYLKPLLIGEL 94
Cdd:pfam00173   2 YTLEEVAKHNKEGDCWVVINGKVYDVTKFLKEHPGGADVILAAAGKDATDAFAnAYHSE--DAEELLEKYRVGVL 74
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
162-412 4.41e-63

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239583  Cd Length: 204  Bit Score: 204.80  E-value: 4.41e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 162 LIVAVILATAQSQAGWLQHDFGHLSVFKTSGMNHLVHKFVIGhLKGASAGWWNHRHFQHHAKPNIFKKDPDVNMLNAFVV 241
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 242 GNVQPveyGVKKIKHLPYNHQHKYFFFIGPPLLipvyfqfqifhnmishgmwvdllwcisyyvryflcytqfygvfwaiI 321
Cdd:cd03506  80 SEPAF---GKDQKKRFLHRYQHFYFFPLLALLL----------------------------------------------L 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 322 LFNFVRFMESHWFVWVTQMSRIPMNIDYEQN---QDWLSMQLVATCNIEQSAFNDWFSGHLNFQIEHHLFPTMPRHNYWR 398
Cdd:cd03506 111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGeskNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190
                       250
                ....*....|....
gi 42476248 399 AAPRVRSLCEKYGV 412
Cdd:cd03506 191 VAPLVRELCKKHGL 204
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
21-94 9.69e-24

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: 278597  Cd Length: 74  Bit Score: 94.21  E-value: 9.69e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42476248    21 YTWEEMQKHTKHGDQWVVVERKVYNVSQWVKRHPGGLRILGHYAGEDATEAFT-AFHPNlqLMRKYLKPLLIGEL 94
Cdd:pfam00173   2 YTLEEVAKHNKEGDCWVVINGKVYDVTKFLKEHPGGADVILAAAGKDATDAFAnAYHSE--DAEELLEKYRVGVL 74
COG4892 COG4892
Predicted heme/steroid binding protein [General function prediction only];
21-77 8.41e-03

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


Pssm-ID: 227229  Cd Length: 81  Bit Score: 34.48  E-value: 8.41e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42476248  21 YTWEEMQKHT-KHGDQWVVVERKVYNVS---QWvkrhPGGLRILGHYAGEDATEAFTAFHP 77
Cdd:COG4892   4 FTLEELSKYNgENGPAYIAVNGTVYDVSlspSW----GDGTHQGLHSAGKDLSSEFNSCAP 60
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
20-435 4.80e-59

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 203.38  E-value: 4.80e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   20 SYTWEEMQKHTKHGDQWVVVERKVYNVSQWVKRHPGGlRILGHYAGEDATEAFTAFHPNLQLmrKYLKPLLIGELEASEP 99
Cdd:PLN03198 105 SHLLSEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGG-SVISTYFGRDGTDAFSSFHAASTW--KILQDFYIGDVDNVEP 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  100 SQDrqknaaLVEDFRALRERLEAEGCFKTQPLFFALHLGHILLLEAIAFVMVWYFGTGWInTLIVAVILATAQSQAGWLQ 179
Cdd:PLN03198 182 TPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAASIAIICCSKSISA-VLASACMMALCFQQCGWLS 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  180 HDFGHLSVFKTSGMNHLVhKFVIGH-LKGASAGWWNHRHFQHHAKPNIFKK-----DPDVNMLnafvvgnvqPVEYGVKK 253
Cdd:PLN03198 255 HDFLHNQVFETRWLNEVV-GYLIGNaVLGFSTGWWKEKHNLHHAAPNECDQlyqpiDEDIDTL---------PLIAWSKD 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  254 IKHLPYNH------QHKYFFFIGppLLipvyfqfqifhnMISHGMWvdLLWCISYYVRYFLCytqfyGVFWAI----ILF 323
Cdd:PLN03198 325 ILATVENKtflrilQYQHLFFMA--LL------------FFARGSW--LFWSWRYTSTAKLA-----PADRLLekgtILF 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  324 NFVRFMESHWF--------VW--VTQ------------MSRIPMNIdYEQNQDWLSMQLVATCNIEQSAFNDWFSGHLNF 381
Cdd:PLN03198 384 HYFWFIGTACYllpgwkplVWmaVTElmcgmllgfvfvLSHNGMEV-YNKSKEFVNAQIVSTRDIKANIFNDWFTGGLNR 462
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42476248  382 QIEHHLFPTMPRHNYWRAAPRVRSLCEKYGVKYQEKTLYGAFADIIRSLEKSGE 435
Cdd:PLN03198 463 QIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKEVAE 516
FA_desaturase pfam00487
Fatty acid desaturase;
157-416 1.74e-21

Fatty acid desaturase;


Pssm-ID: 278890 [Multi-domain]  Cd Length: 249  Bit Score: 92.38  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   157 GWINTLIVAVILATAQSQAGWLQHDFGHLSVFKTS-GMNHLVHKFvIGHLKGASAGWWNHRHFQHHAKPNIFKKDPDVNM 235
Cdd:pfam00487   1 SWLALLLALLLGLFQLGILFVLAHEAAHGALFRSNrWLNDLLGRL-AGLPLGISYSAWRIAHLVHHRYTNGPDEDPDTAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   236 LNAFVVGNVQPVeygvkkiKHLPYNHQHKYFFFIGPPLLIPVYFQFQIFHNMISHGMWVDLLWCISYYVRYFLCYTQFYG 315
Cdd:pfam00487  80 LASRFRGLYRYL-------LRWLLGLLVLAWLLALLLGLWLRRLARRKRPAKSRRRRWVLIAWLLLLAAWLGLWLGFLGL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   316 VFWAIILFNFVRFMESHWFVWVtqmsripMNIDYEQNQDWLSMQLVATCNIEQ-SAFNDWFSGHLNFQIEHHLFPTMPRH 394
Cdd:pfam00487 153 GGLLLLLWLLPLLTAGFLLALV-------RNYLEHYGGDWGERPVETTRSINSnGWWLNLLTGNLNYHIEHHLFPGVPWY 225
                         250       260
                  ....*....|....*....|..
gi 42476248   395 NYWRAAPRVRSLCEKYGVKYQE 416
Cdd:pfam00487 226 RLPKLHRRLREALPEHGLPYRS 247
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
140-414 1.21e-15

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 76.36  E-value: 1.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 140 ILLLEAIAFVMVWYFGT---GWINTLIVAVILATAQ-SQAGWLQHDFGHLSVFKTSGMNHLvhkfvIGHLKGA----SAG 211
Cdd:COG3239  39 ITFLALAGLWALLALSLaywPSWWLLPLALLLAGLLlTGLFSVGHDCGHGSFFKNRWINDL-----IGHLAAAlllaPPV 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 212 WWNHRHFQHHAKPNIFKKDPDvnmlnafvvgnvQPVEYGvKKIKHLPYNHQ------HKYFFFIGPPLLIPVYFQFQIFH 285
Cdd:COG3239 114 FWRISHNQHHAHTNILDDDPE------------TYVSYP-EQLRRGPLRFQlirlpwLAFGFGPRWALLHFELLEKLFKR 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 286 NMISHGM-WVDLLWCISYYVrYFLCYTQFYGVFWAIILFNfvrfmeshWFVWVTQMSRIPMNIDY--EQNQDWLSMQLVA 362
Cdd:COG3239 181 SGKAPKAaALATLLAAIGLA-ALLALAFFWGLIPLLLVGL--------WLVLVLFVHHTFDLLPHhgLEDWQWSDRALNA 251
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42476248 363 TCNIEQSAFNDWFSGHLNFQIEHHLFPTMPRHNYWRAAPRVRSLCEKYGVKY 414
Cdd:COG3239 252 RSNVDAPPLLRFLTGNINYHVEHHLFPDVPWYRLPRAHRLIKEALGERGLTI 303
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
162-412 4.41e-63

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239583  Cd Length: 204  Bit Score: 204.80  E-value: 4.41e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 162 LIVAVILATAQSQAGWLQHDFGHLSVFKTSGMNHLVHKFVIGhLKGASAGWWNHRHFQHHAKPNIFKKDPDVNMLNAFVV 241
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 242 GNVQPveyGVKKIKHLPYNHQHKYFFFIGPPLLipvyfqfqifhnmishgmwvdllwcisyyvryflcytqfygvfwaiI 321
Cdd:cd03506  80 SEPAF---GKDQKKRFLHRYQHFYFFPLLALLL----------------------------------------------L 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 322 LFNFVRFMESHWFVWVTQMSRIPMNIDYEQN---QDWLSMQLVATCNIEQSAFNDWFSGHLNFQIEHHLFPTMPRHNYWR 398
Cdd:cd03506 111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGeskNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190
                       250
                ....*....|....
gi 42476248 399 AAPRVRSLCEKYGV 412
Cdd:cd03506 191 VAPLVRELCKKHGL 204
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
21-94 9.69e-24

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: 278597  Cd Length: 74  Bit Score: 94.21  E-value: 9.69e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42476248    21 YTWEEMQKHTKHGDQWVVVERKVYNVSQWVKRHPGGLRILGHYAGEDATEAFT-AFHPNlqLMRKYLKPLLIGEL 94
Cdd:pfam00173   2 YTLEEVAKHNKEGDCWVVINGKVYDVTKFLKEHPGGADVILAAAGKDATDAFAnAYHSE--DAEELLEKYRVGVL 74
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
162-237 2.86e-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  Cd Length: 122  Bit Score: 54.40  E-value: 2.86e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42476248 162 LIVAVILATAQSQAGWLQHDFGHLSVFKTSGMNHLVHKFVIGHLkGASAGWWNHRHFQHHAKPNIFKKDPD--VNMLN 237
Cdd:cd01060   2 LLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDsaVNYLE 78
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
110-233 1.12e-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: 42.36  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 110 VEDFRALRERLEAEGCFKTqplffALHLGHILLleaIAFVMVWYFGTGWINTLIVA--VILATAQSqagwLQHDFGHLSV 187
Cdd:cd03511   3 RQELKQLMQRSDAPGLLDT-----ALWLGALAV---SGILIAWTWGSWWALPAFLVygVLYAALFA----RWHECVHGTA 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42476248 188 FKTSGMNHLVHkFVIGHLKGASAGWWNHRHFQHHAKPNIFKKDPDV 233
Cdd:cd03511  71 FATRWLNDAVG-QIAGLMILLPPDFFRWSHARHHRYTQIPGRDPEL 115
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
140-395 1.26e-04

The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes, delta-12 acyl-lipid desaturases, oleate 12-hydroxylases, omega3 and omega6 fatty acid desaturases, and other related proteins, found in a wide range of organisms including higher plants, green algae, diatoms, nematodes, fungi, and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase, cytochrome b, and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6), omega-3 desaturase (FAD8), omega-6 desaturase (FAD6)), as well as, the cyanobacterial thylakoid-bound FADSs require oxygen, ferredoxin, and ferredoxin oxidoreductase for activity. As in higher plants, the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3), respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four, and carbons six and seven, respectively, from the methyl end of fatty acids. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXX(X)HH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homologue, stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity.


Pssm-ID: 239584  Cd Length: 222  Bit Score: 41.83  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 140 ILLLEAIAFVMVWYFGtgWINTLIVAVILATAQSQAGWLQHDFGHLSVFKTSGMNHLVhkfviGHLKGASAGW----WNH 215
Cdd:cd03507  14 ILLLALLALAASLLLS--WWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIV-----GHILHSPLLVpyhsWRI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 216 RHFQHHAKPNifkkdpdvNMLNAFVVGNVQPVEYGvKKIKHLPYNH--QHKYFFFIGPPLlipvyfqfqifhnmishgmw 293
Cdd:cd03507  87 SHNRHHAHTG--------NLEGDEVWVPVTEEEYA-ELPKRLPYRLyrNPFLMLSLGWPY-------------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 294 vdllwcisYYVRYFLCYtqfYGVFWAIIlfnfvrfmeSHWFVWVTQMSRIPMNIDYEQNQDW--LSMQLVATCNIEQSAF 371
Cdd:cd03507 138 --------YLLLNVLLY---YLIPYLVV---------NAWLVLITYLQHTFPDIPWYRADEWnfAQAGLLGTVDRDYGGW 197
                       250       260
                ....*....|....*....|....
gi 42476248 372 NDWFSGHLNFQIEHHLFPTMPRHN 395
Cdd:cd03507 198 LNWLTHIIGTHVAHHLFPRIPHYN 221
COG4892 COG4892
Predicted heme/steroid binding protein [General function prediction only];
21-77 8.41e-03

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


Pssm-ID: 227229  Cd Length: 81  Bit Score: 34.48  E-value: 8.41e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42476248  21 YTWEEMQKHT-KHGDQWVVVERKVYNVS---QWvkrhPGGLRILGHYAGEDATEAFTAFHP 77
Cdd:COG4892   4 FTLEELSKYNgENGPAYIAVNGTVYDVSlspSW----GDGTHQGLHSAGKDLSSEFNSCAP 60
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
20-435 4.80e-59

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 203.38  E-value: 4.80e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   20 SYTWEEMQKHTKHGDQWVVVERKVYNVSQWVKRHPGGlRILGHYAGEDATEAFTAFHPNLQLmrKYLKPLLIGELEASEP 99
Cdd:PLN03198 105 SHLLSEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGG-SVISTYFGRDGTDAFSSFHAASTW--KILQDFYIGDVDNVEP 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  100 SQDrqknaaLVEDFRALRERLEAEGCFKTQPLFFALHLGHILLLEAIAFVMVWYFGTGWInTLIVAVILATAQSQAGWLQ 179
Cdd:PLN03198 182 TPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAASIAIICCSKSISA-VLASACMMALCFQQCGWLS 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  180 HDFGHLSVFKTSGMNHLVhKFVIGH-LKGASAGWWNHRHFQHHAKPNIFKK-----DPDVNMLnafvvgnvqPVEYGVKK 253
Cdd:PLN03198 255 HDFLHNQVFETRWLNEVV-GYLIGNaVLGFSTGWWKEKHNLHHAAPNECDQlyqpiDEDIDTL---------PLIAWSKD 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  254 IKHLPYNH------QHKYFFFIGppLLipvyfqfqifhnMISHGMWvdLLWCISYYVRYFLCytqfyGVFWAI----ILF 323
Cdd:PLN03198 325 ILATVENKtflrilQYQHLFFMA--LL------------FFARGSW--LFWSWRYTSTAKLA-----PADRLLekgtILF 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  324 NFVRFMESHWF--------VW--VTQ------------MSRIPMNIdYEQNQDWLSMQLVATCNIEQSAFNDWFSGHLNF 381
Cdd:PLN03198 384 HYFWFIGTACYllpgwkplVWmaVTElmcgmllgfvfvLSHNGMEV-YNKSKEFVNAQIVSTRDIKANIFNDWFTGGLNR 462
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42476248  382 QIEHHLFPTMPRHNYWRAAPRVRSLCEKYGVKYQEKTLYGAFADIIRSLEKSGE 435
Cdd:PLN03198 463 QIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKEVAE 516
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
21-439 9.25e-53

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 185.63  E-value: 9.25e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   21 YTWEEMQKHTKHGDQWVVVERKVYNVSQWVKrHPGGLRILGHyAGEDATEAFTAFH-PNLQLMrkyLKPLLIGELEASEP 99
Cdd:PLN03199  26 ISWQEVKKHASPDDAWIIHQNKVYDVSNWHD-HPGGAVIFTH-AGDDMTDIFAAFHaPGSQAL---MKKFYIGDLIPEST 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  100 SQDRQKNAALVEDFRALRERLEAEGCFKTQPLFFALHLGHILLLEAIAFVMVWYFGTGWINtLIVAVILATAQSQAGWLQ 179
Cdd:PLN03199 101 EHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLFNMAIWAAACALVFYSDRFAMH-IASALLLGLFFQQCGWLA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  180 HDFGHLSVFKTSGMNHLVHKFVIGHLKGASAGWWNHRHFQHHAKPNIFKK-------DPDVNM--LNAFVVGNVQP---- 246
Cdd:PLN03199 180 HDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqdgDPDIDTmpLLAWSLKQAQSfrei 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  247 ---------VEYGVKKIKHLPY-----------NHQHKYFFFIGPPL------LIPVYFQFQIFHN--MISHGMWVDLL- 297
Cdd:PLN03199 260 nadgkdsgfVKFAIKFQAFFYFpilllariswlNESFKCAFGLGAASenaaleLEAKGLQYPLLEKagILLHYAWMFTLs 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  298 -----WCISYYVRYFLCYTQFYGVFWAIIlfnfvrFMESHwfvwvTQMSripmNIDYEQNQDWLSMQLVATCNIE----- 367
Cdd:PLN03199 340 sgfgrFSFAYSAFYFFTATASCGFFLAIV------FGLGH-----NGMA----TYDADARPDFWKLQVTTTRNIIgghgf 404
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42476248  368 QSAFNDWFSGHLNFQIEHHLFPTMPRHNYWRAAPRVRSLCEKYGVKYQEKTLYGAFADIIRSLEK-SGELWLD 439
Cdd:PLN03199 405 PQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHLGKvADDFLVD 477
FA_desaturase pfam00487
Fatty acid desaturase;
157-416 1.74e-21

Fatty acid desaturase;


Pssm-ID: 278890 [Multi-domain]  Cd Length: 249  Bit Score: 92.38  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   157 GWINTLIVAVILATAQSQAGWLQHDFGHLSVFKTS-GMNHLVHKFvIGHLKGASAGWWNHRHFQHHAKPNIFKKDPDVNM 235
Cdd:pfam00487   1 SWLALLLALLLGLFQLGILFVLAHEAAHGALFRSNrWLNDLLGRL-AGLPLGISYSAWRIAHLVHHRYTNGPDEDPDTAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   236 LNAFVVGNVQPVeygvkkiKHLPYNHQHKYFFFIGPPLLIPVYFQFQIFHNMISHGMWVDLLWCISYYVRYFLCYTQFYG 315
Cdd:pfam00487  80 LASRFRGLYRYL-------LRWLLGLLVLAWLLALLLGLWLRRLARRKRPAKSRRRRWVLIAWLLLLAAWLGLWLGFLGL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   316 VFWAIILFNFVRFMESHWFVWVtqmsripMNIDYEQNQDWLSMQLVATCNIEQ-SAFNDWFSGHLNFQIEHHLFPTMPRH 394
Cdd:pfam00487 153 GGLLLLLWLLPLLTAGFLLALV-------RNYLEHYGGDWGERPVETTRSINSnGWWLNLLTGNLNYHIEHHLFPGVPWY 225
                         250       260
                  ....*....|....*....|..
gi 42476248   395 NYWRAAPRVRSLCEKYGVKYQE 416
Cdd:pfam00487 226 RLPKLHRRLREALPEHGLPYRS 247
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
140-414 1.21e-15

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 76.36  E-value: 1.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 140 ILLLEAIAFVMVWYFGT---GWINTLIVAVILATAQ-SQAGWLQHDFGHLSVFKTSGMNHLvhkfvIGHLKGA----SAG 211
Cdd:COG3239  39 ITFLALAGLWALLALSLaywPSWWLLPLALLLAGLLlTGLFSVGHDCGHGSFFKNRWINDL-----IGHLAAAlllaPPV 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 212 WWNHRHFQHHAKPNIFKKDPDvnmlnafvvgnvQPVEYGvKKIKHLPYNHQ------HKYFFFIGPPLLIPVYFQFQIFH 285
Cdd:COG3239 114 FWRISHNQHHAHTNILDDDPE------------TYVSYP-EQLRRGPLRFQlirlpwLAFGFGPRWALLHFELLEKLFKR 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248 286 NMISHGM-WVDLLWCISYYVrYFLCYTQFYGVFWAIILFNfvrfmeshWFVWVTQMSRIPMNIDY--EQNQDWLSMQLVA 362
Cdd:COG3239 181 SGKAPKAaALATLLAAIGLA-ALLALAFFWGLIPLLLVGL--------WLVLVLFVHHTFDLLPHhgLEDWQWSDRALNA 251
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42476248 363 TCNIEQSAFNDWFSGHLNFQIEHHLFPTMPRHNYWRAAPRVRSLCEKYGVKY 414
Cdd:COG3239 252 RSNVDAPPLLRFLTGNINYHVEHHLFPDVPWYRLPRAHRLIKEALGERGLTI 303
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
20-100 1.33e-12

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


Pssm-ID: 227599 [Multi-domain]  Cd Length: 164  Bit Score: 64.84  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248  20 SYTWEEMQKHTKHGDQWVVVERKVYNVSQWVKRHPGGLRILGHYAGEDATEAFTAFHPNLQLMRkYLKPLLIGELEASEP 99
Cdd:COG5274  51 PITAEEVAKHNKSEDCWIVINGKVYDVSQFLDEHPGGEDIIKDTAGKDATKAFNFLHHSHQIGN-LLKDVYVDQVHRPEE 129

                .
gi 42476248 100 S 100
Cdd:COG5274 130 E 130
PLN02252 PLN02252
nitrate reductase [NADPH]
14-100 3.53e-12

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 67.01  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42476248   14 TNGRFSSYTWEEMQKHTKHGDQWVVVERKVYNVSQWVKRHPGGLRILGHYAGEDATEAFTAFHPNLQlmRKYLKPLLIGE 93
Cdd:PLN02252 513 TNTGSKQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDKA--KKMLEDYRIGE 590

                 ....*..
gi 42476248   94 LEASEPS 100
Cdd:PLN02252 591 LVTTGAA 597
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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