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Conserved domains on  [gi|28371825|gb|AAO37753|]
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fatty acid conjugase [Punica granatum]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Membrane-FADS-like super family cl00615
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
1-395 0e+00

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.


The actual alignment was detected with superfamily member PLN02505:

Pssm-ID: 294412  Cd Length: 381  Bit Score: 604.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825    1 MGADGTMSPVLTKRRpdqeinkldikpnHEVDIARRAPHSKPPFTLSDLRSAIPPHCFHRSLLMSSSYLIRDFALAFLFY 80
Cdd:PLN02505   1 MGAGGRMSVPTSSKK-------------GSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   81 HSAVTYIPLLPKPLACMAWPVYWFLQGSNMLGIWVIAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSN 160
Cdd:PLN02505  68 YVATNYIPLLPGPLSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  161 TNSVEHDEVFVPRHKDGVQWYYRFFNNTPGRVLTLTLTLLVGWPSYLAFNASGRPYDGFASHYNPNAQIFNLRERFWVHV 240
Cdd:PLN02505 148 TGSLERDEVFVPKKKSALPWYSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  241 SNIGILAIYYILYRLATTKGLPWLLSIYGVPVLILNAFVVLITFLQHSHPALPHYNSDEWDWLRGALATVDRDYGFLNEV 320
Cdd:PLN02505 228 SDAGILAVSFGLYRLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKV 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28371825  321 FHDITDTHVIHHLFPTMPHYNAKEATVSIRPILKDYYKFDRTPIWRALWREAKECLYVEADGtGSKGVLWFKSKF 395
Cdd:PLN02505 308 FHNITDTHVAHHLFSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPDE-GGKGVFWYNNKF 381
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
1-395 0e+00

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 604.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825    1 MGADGTMSPVLTKRRpdqeinkldikpnHEVDIARRAPHSKPPFTLSDLRSAIPPHCFHRSLLMSSSYLIRDFALAFLFY 80
Cdd:PLN02505   1 MGAGGRMSVPTSSKK-------------GSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   81 HSAVTYIPLLPKPLACMAWPVYWFLQGSNMLGIWVIAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSN 160
Cdd:PLN02505  68 YVATNYIPLLPGPLSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  161 TNSVEHDEVFVPRHKDGVQWYYRFFNNTPGRVLTLTLTLLVGWPSYLAFNASGRPYDGFASHYNPNAQIFNLRERFWVHV 240
Cdd:PLN02505 148 TGSLERDEVFVPKKKSALPWYSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  241 SNIGILAIYYILYRLATTKGLPWLLSIYGVPVLILNAFVVLITFLQHSHPALPHYNSDEWDWLRGALATVDRDYGFLNEV 320
Cdd:PLN02505 228 SDAGILAVSFGLYRLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKV 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28371825  321 FHDITDTHVIHHLFPTMPHYNAKEATVSIRPILKDYYKFDRTPIWRALWREAKECLYVEADGtGSKGVLWFKSKF 395
Cdd:PLN02505 308 FHNITDTHVAHHLFSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPDE-GGKGVFWYNNKF 381
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
60-342 4.04e-65

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: 206.69  E-value: 4.04e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  60 RSLLMSSSYLIRDFALAFLFYHSAVTYIPLLpkplacmAWPVYWFLQGSNMLGIWVIAHECGHQAFSNYGWVNDAVGFFL 139
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAASLLLSWW-------LWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 140 HTSLLVPYFPFKYSHRRHHSNTNSVEHDEVFVP------RHKDGVQWYYRFFNntpgrvltLTLTLLVGWPSYLAFNasg 213
Cdd:cd03507  74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPvteeeyAELPKRLPYRLYRN--------PFLMLSLGWPYYLLLN--- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 214 rpydgfashynpnaqifnlrerfwvhvsnigilaiyyilyrlattkglpwLLSIYGVPVLILNAFVVLITFLQHSHPALP 293
Cdd:cd03507 143 --------------------------------------------------VLLYYLIPYLVVNAWLVLITYLQHTFPDIP 172
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 28371825 294 HYNSDEWDWL-RGALATVDRDYGFLNEVFHDITDTHVIHHLFPTMPHYNA 342
Cdd:cd03507 173 WYRADEWNFAqAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
36-375 7.75e-33

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 125.67  E-value: 7.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  36 RAPHSKPPFTLSDLRSAIPPHCFHRSLLMSSSYLIRDFALAFLFYhSAVTYIPLLPkplacmAWPVYWFLQGSNMLGIWV 115
Cdd:COG3239   8 SAAVENLAAPLDSIRARLPKPRTRRDAIAILITFLALAGLWALLA-LSLAYWPSWW------LLPLALLLAGLLLTGLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 116 IAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSNTNSVEHD-EVFVPRHKDGVQWYYRFFNntpgrvlt 194
Cdd:COG3239  81 VGHDCGHGSFFKNRWINDLIGHLAAALLLAPPVFWRISHNQHHAHTNILDDDpETYVSYPEQLRRGPLRFQL-------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 195 ltltllvGWPSYLAFnasGRPYDGFASHYNPNAQIFNLRERFWVHVSNIGILAIyyILYRLAttkgLPWLLSIYGVPVLI 274
Cdd:COG3239 153 -------IRLPWLAF---GFGPRWALLHFELLEKLFKRSGKAPKAAALATLLAA--IGLAAL----LALAFFWGLIPLLL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 275 LNAFVVLITFLQHSHPALPHYNSDEWDWLRGAL-ATVDRDYG-FLNEVFHDITdTHVIHHLFPTMPHYNAKEATVSIRPI 352
Cdd:COG3239 217 VGLWLVLVLFVHHTFDLLPHHGLEDWQWSDRALnARSNVDAPpLLRFLTGNIN-YHVEHHLFPDVPWYRLPRAHRLIKEA 295
                       330       340       350
                ....*....|....*....|....*....|.
gi 28371825 353 L--------KDYYKFDRTPIWRALWREAKEC 375
Cdd:COG3239 296 LgergltiyTGYREFKLATLWQLRGEIFLPK 326
FA_desaturase pfam00487
Fatty acid desaturase;
97-357 6.98e-16

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 76.60  E-value: 6.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825    97 MAWPVYWFLQGSNMLGIWVIAHECGHQAFSN--YGWVNDAVGFFLHTsLLVPYFPFKYSHRRHHSNTNSVEHDEVFVPRH 174
Cdd:pfam00487   2 LALLLALLLGLFLLGILGVLAHEASHGALFRrrNRWLNDLLGLAGLP-LGISYSAWRIAHLVHHRYTNGPDEDPDTAPLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   175 KDGVQWYYRFFNNTPGrvltltlTLLVGWPSYLAFNASGRPYDGFASHynpnaqiFNLRERFWVHVSNIGILAIYYILYr 254
Cdd:pfam00487  81 SRFRGLLRYLLRWLLG-------LLVLAWLLALLLGLWLRRLARRKRP-------IKSRRRRWRLIAWLLLLAAWLGLW- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   255 LATTKGLPWLLSIYGVPVLILNAFVVLI-TFLQHSHPALPHYNSDewdwlrgALATVDRDYGFLNEVFHDITdTHVIHHL 333
Cdd:pfam00487 146 LGFLGLGGLLLLLWLLPLLVAGFLLALIfNYLEHYGGDWGERPVE-------TTRSIRSPNWWLNLLTGNLN-YHIEHHL 217
                         250       260
                  ....*....|....*....|....
gi 28371825   334 FPTMPHYNAKEATVSIRPILKDYY 357
Cdd:pfam00487 218 FPGVPWYRLPKLHRRLREALPEHG 241
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
1-395 0e+00

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 604.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825    1 MGADGTMSPVLTKRRpdqeinkldikpnHEVDIARRAPHSKPPFTLSDLRSAIPPHCFHRSLLMSSSYLIRDFALAFLFY 80
Cdd:PLN02505   1 MGAGGRMSVPTSSKK-------------GSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   81 HSAVTYIPLLPKPLACMAWPVYWFLQGSNMLGIWVIAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSN 160
Cdd:PLN02505  68 YVATNYIPLLPGPLSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  161 TNSVEHDEVFVPRHKDGVQWYYRFFNNTPGRVLTLTLTLLVGWPSYLAFNASGRPYDGFASHYNPNAQIFNLRERFWVHV 240
Cdd:PLN02505 148 TGSLERDEVFVPKKKSALPWYSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  241 SNIGILAIYYILYRLATTKGLPWLLSIYGVPVLILNAFVVLITFLQHSHPALPHYNSDEWDWLRGALATVDRDYGFLNEV 320
Cdd:PLN02505 228 SDAGILAVSFGLYRLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKV 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28371825  321 FHDITDTHVIHHLFPTMPHYNAKEATVSIRPILKDYYKFDRTPIWRALWREAKECLYVEADGtGSKGVLWFKSKF 395
Cdd:PLN02505 308 FHNITDTHVAHHLFSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAKECIYVEPDE-GGKGVFWYNNKF 381
PLN02498 PLN02498
omega-3 fatty acid desaturase
17-358 1.59e-68

omega-3 fatty acid desaturase


Pssm-ID: 215275  Cd Length: 450  Bit Score: 222.78  E-value: 1.59e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   17 DQEINKLDIKPNHEVDIARRAPHSKPPFTLSDLRSAIPPHCFHRSLLMSSSYLIRDFALAFLFYHSAVTYIPLLpkplac 96
Cdd:PLN02498  75 EEEEDEEGVNGVGEDEEGEFDPGAPPPFNLADIRAAIPKHCWVKNPWRSMSYVVRDVAVVFGLAAAAAYFNNWV------ 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   97 mAWPVYWFLQGSNMLGIWVIAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSNTNSVEHDEVFVP---- 172
Cdd:PLN02498 149 -VWPLYWFAQGTMFWALFVLGHDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPlsek 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  173 --RHKDGVQWYYRFFNNTPgrvltltltlLVGWPSYLAFNASGRPydgfASHYNPNAQIFNLRERFWVHVSNIGILAIYY 250
Cdd:PLN02498 228 iyKSLDKVTRTLRFTLPFP----------MLAYPFYLWSRSPGKK----GSHFHPDSDLFVPKERKDVITSTACWTAMAA 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  251 ILYRLATTKGLPWLLSIYGVPVLILNAFVVLITFLQH--SHPALPHYNSDEWDWLRGALATVDRDYGFLNEVFHDItDTH 328
Cdd:PLN02498 294 LLVCLSFVMGPIQMLKLYGIPYWIFVMWLDFVTYLHHhgHEDKLPWYRGKEWSYLRGGLTTLDRDYGWINNIHHDI-GTH 372
                        330       340       350
                 ....*....|....*....|....*....|
gi 28371825  329 VIHHLFPTMPHYNAKEATVSIRPILKDYYK 358
Cdd:PLN02498 373 VIHHLFPQIPHYHLVEATEAAKPVLGKYYR 402
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
60-342 4.04e-65

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: 206.69  E-value: 4.04e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  60 RSLLMSSSYLIRDFALAFLFYHSAVTYIPLLpkplacmAWPVYWFLQGSNMLGIWVIAHECGHQAFSNYGWVNDAVGFFL 139
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALAASLLLSWW-------LWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 140 HTSLLVPYFPFKYSHRRHHSNTNSVEHDEVFVP------RHKDGVQWYYRFFNntpgrvltLTLTLLVGWPSYLAFNasg 213
Cdd:cd03507  74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPvteeeyAELPKRLPYRLYRN--------PFLMLSLGWPYYLLLN--- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 214 rpydgfashynpnaqifnlrerfwvhvsnigilaiyyilyrlattkglpwLLSIYGVPVLILNAFVVLITFLQHSHPALP 293
Cdd:cd03507 143 --------------------------------------------------VLLYYLIPYLVVNAWLVLITYLQHTFPDIP 172
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 28371825 294 HYNSDEWDWL-RGALATVDRDYGFLNEVFHDITDTHVIHHLFPTMPHYNA 342
Cdd:cd03507 173 WYRADEWNFAqAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
36-375 7.75e-33

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 125.67  E-value: 7.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  36 RAPHSKPPFTLSDLRSAIPPHCFHRSLLMSSSYLIRDFALAFLFYhSAVTYIPLLPkplacmAWPVYWFLQGSNMLGIWV 115
Cdd:COG3239   8 SAAVENLAAPLDSIRARLPKPRTRRDAIAILITFLALAGLWALLA-LSLAYWPSWW------LLPLALLLAGLLLTGLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 116 IAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSNTNSVEHD-EVFVPRHKDGVQWYYRFFNntpgrvlt 194
Cdd:COG3239  81 VGHDCGHGSFFKNRWINDLIGHLAAALLLAPPVFWRISHNQHHAHTNILDDDpETYVSYPEQLRRGPLRFQL-------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 195 ltltllvGWPSYLAFnasGRPYDGFASHYNPNAQIFNLRERFWVHVSNIGILAIyyILYRLAttkgLPWLLSIYGVPVLI 274
Cdd:COG3239 153 -------IRLPWLAF---GFGPRWALLHFELLEKLFKRSGKAPKAAALATLLAA--IGLAAL----LALAFFWGLIPLLL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 275 LNAFVVLITFLQHSHPALPHYNSDEWDWLRGAL-ATVDRDYG-FLNEVFHDITdTHVIHHLFPTMPHYNAKEATVSIRPI 352
Cdd:COG3239 217 VGLWLVLVLFVHHTFDLLPHHGLEDWQWSDRALnARSNVDAPpLLRFLTGNIN-YHVEHHLFPDVPWYRLPRAHRLIKEA 295
                       330       340       350
                ....*....|....*....|....*....|.
gi 28371825 353 L--------KDYYKFDRTPIWRALWREAKEC 375
Cdd:COG3239 296 LgergltiyTGYREFKLATLWQLRGEIFLPK 326
PLN02598 PLN02598
omega-6 fatty acid desaturase
100-350 1.92e-19

omega-6 fatty acid desaturase


Pssm-ID: 215323  Cd Length: 421  Bit Score: 89.11  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  100 PVYWFLQGSNMLGIWVIAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSNTNSVEHDEVFVPrhkdgvQ 179
Cdd:PLN02598 126 PLAWAWLGTAITGFFVIGHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNTHHAHTNKLVMDTAWQP------F 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  180 WYYRFFNNTPgrvltltltllVGWPSYLAFNASGRPYDGFAS----HYNPNAqiFNLRERFWVHVSNIGILAIYYILYRL 255
Cdd:PLN02598 200 RPHQFDNADP-----------LRKAMMRAGMGPLWWWASIGHwlfwHFDLNK--FRPQEVPRVKISLAAVFAFMALGLPP 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  256 ATTKGLPW-LLSIYGVPVLILNAFVVLITFLQHSHPALPHYNSDEWDWLRGALA-TVDRDY-GFLNEVFHDITdTHVIHH 332
Cdd:PLN02598 267 LLYTTGPVgFVKWWLMPWLGYHFWMSTFTMVHHTAPHIPFKQAREWNAAQAQLNgTVHCDYpAWIEFLCHDIS-VHIPHH 345
                        250
                 ....*....|....*...
gi 28371825  333 LFPTMPHYNAKEATVSIR 350
Cdd:PLN02598 346 ISSKIPSYNLRKAHASLQ 363
FA_desaturase pfam00487
Fatty acid desaturase;
97-357 6.98e-16

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 76.60  E-value: 6.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825    97 MAWPVYWFLQGSNMLGIWVIAHECGHQAFSN--YGWVNDAVGFFLHTsLLVPYFPFKYSHRRHHSNTNSVEHDEVFVPRH 174
Cdd:pfam00487   2 LALLLALLLGLFLLGILGVLAHEASHGALFRrrNRWLNDLLGLAGLP-LGISYSAWRIAHLVHHRYTNGPDEDPDTAPLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   175 KDGVQWYYRFFNNTPGrvltltlTLLVGWPSYLAFNASGRPYDGFASHynpnaqiFNLRERFWVHVSNIGILAIYYILYr 254
Cdd:pfam00487  81 SRFRGLLRYLLRWLLG-------LLVLAWLLALLLGLWLRRLARRKRP-------IKSRRRRWRLIAWLLLLAAWLGLW- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825   255 LATTKGLPWLLSIYGVPVLILNAFVVLI-TFLQHSHPALPHYNSDewdwlrgALATVDRDYGFLNEVFHDITdTHVIHHL 333
Cdd:pfam00487 146 LGFLGLGGLLLLLWLLPLLVAGFLLALIfNYLEHYGGDWGERPVE-------TTRSIRSPNWWLNLLTGNLN-YHIEHHL 217
                         250       260
                  ....*....|....*....|....
gi 28371825   334 FPTMPHYNAKEATVSIRPILKDYY 357
Cdd:pfam00487 218 FPGVPWYRLPKLHRRLREALPEHG 241
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
97-171 4.17e-15

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: 70.96  E-value: 4.17e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28371825  97 MAWPVYWFLQGsnmLGIWVIAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSNTNSVEHDEVFV 171
Cdd:cd01060   2 LLALLLGLLGG---LGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKDPDSA 73
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
116-358 3.80e-12

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: 64.59  E-value: 3.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 116 IAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSNTNSVEHDEVFvprhkdgvqwyyrffnntpgrvltl 195
Cdd:cd03506  17 LAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHDPDI------------------------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 196 tltllvgWPSYLAFNASGRPYDGFASHYNPNAQIFnlrerfwvhvsnigilaIYYILYrlattkglPWLLSIYGVPVLIL 275
Cdd:cd03506  72 -------DTLPLLARSEPAFGKDQKKRFLHRYQHF-----------------YFFPLL--------ALLLLAFLVVQLAG 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 276 NAFVVLITFLQH-SHPALPHYNSDEWDWL-RGALATVDRDYGFLNEVFHDITDTHVIHHLFPTMPHYNAKEatvsIRPIL 353
Cdd:cd03506 120 GLWLAVVFQLNHfGMPVEDPPGESKNDWLeRQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK----VAPLV 195

                ....*
gi 28371825 354 KDYYK 358
Cdd:cd03506 196 RELCK 200
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
94-338 1.97e-08

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  Cd Length: 285  Bit Score: 54.69  E-value: 1.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825  94 LACMAWPVYW-----FLQGSNMLGIWVIAHECGHQAFSNYGWVNDAVGFFLHTSLLVPYFPFKYSHRRHHSNTNSVEHD- 167
Cdd:cd03511  34 LIAWTWGSWWalpafLVYGVLYAALFARWHECVHGTAFATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRYTQIPGRDp 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 168 EVFVPRHKDGVQWYYRFFNntpgrvltltltlLVGWPSYL------AFNASGRPYDGFAShynPNAQIFNLRE-RFWvhv 240
Cdd:cd03511 114 ELAVPRPPTLREYLLALSG-------------LPYWWGKLrtvfrhAFGAVSEAEKPFIP---AEERPKVVREaRAM--- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28371825 241 snigiLAIYYILYRLATTKGLPWLLSIYGVPVLILNAFVVLITFLQHSHpaLPHynsDEWDWLRGALATVDRDYGFL--N 318
Cdd:cd03511 175 -----LAVYAGLIALSLYLGSPLLVLVWGLPLLLGQPILRLFLLAEHGG--CPE---DANDLRNTRTTLTNPPLRFLywN 244
                       250       260
                ....*....|....*....|
gi 28371825 319 EVFhditdtHVIHHLFPTMP 338
Cdd:cd03511 245 MPY------HAEHHMYPSVP 258
DUF3474 pfam11960
Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. ...
9-77 2.28e-08

Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 126 to 140 amino acids in length. This domain is found associated with pfam00487.


Pssm-ID: 314784  Cd Length: 139  Bit Score: 52.46  E-value: 2.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28371825     9 PVLTKRRPDQEINKLDIKPNHEVDIARRAPHSKPPFTLSDLRSAIPPHCFHRSLLMSSSYLIRDFALAF 77
Cdd:pfam11960  67 PLRVASVEGEEDKETEGFNGGEEEGGEFDPGAPPPFKLADIRAAIPKHCWVKDPWRSMSYVVRDVAVVF 135
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
118-167 2.61e-04

Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the addition of hydroxyl groups to the beta-ionone rings of beta-carotene to form zeaxanthin and is found in bacteria and red algae. Carotenoids are important natural pigments; zeaxanthin and lutein are the only dietary carotenoids that accumulate in the macular region of the retina and lens. It is proposed that these carotenoids protect ocular tissues against photooxidative damage. CrtR does not show overall amino acid sequence similarity to the beta-carotene hydroxylases similar to CrtZ, an astaxanthin biosynthetic beta-carotene hydroxylase. However, CrtR does show sequence similarity to the green alga, Haematococcus pluvialis, beta-carotene ketolase (CrtW), which converts beta-carotene to canthaxanthin. Sequences of the CrtR_beta-carotene-hydroxylase domain family, as well as, the CrtW_beta-carotene-ketolase domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common 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: 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: 239591  Cd Length: 207  Bit Score: 41.58  E-value: 2.61e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 28371825 118 HECGHQAFSNYGWVNDAVGfflHTSLLVPYFPF---KYSHRRHHSNTNSVEHD 167
Cdd:cd03514  43 HDASHKAASRNRWINELIG---HVSAFFLGFPFpvfRRVHMQHHAHTNDPEKD 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
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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