Conserved Protein Domain Family
Membrane-FADS-like

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cd01060: Membrane-FADS-like 
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.
Statistics
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PSSM-Id: 238511
View PSSM: cd01060
Aligned: 363 rows
Threshold Bit Score: 30.1306
Threshold Setting Gi: 83945023
Created: 12-Aug-2003
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
putative
Feature 1:putative di-iron ligands [ion binding site]
Evidence:
  • Comment:Putative catalytically essential di-iron binding histidine residues; based on sequence similarity to stearoyl-CoA desaturase.
  • Comment:Mutation of any one of these eight histidines in stearoyl-CoA desaturase resulted in complete inactivity.
  • Citation:PMID 7947684
  • Comment:Site-directed mutagenesis of borage delta-6 desaturase revealed that the glutamine residue (of the third His-box) is essential for its activity.
  • Comment:Mutation of any one of four histidines (H90, H129, H287, H290) in the Synechocystis sp. PCC 6803 delta-12 acyl-lipid desaturase resulted in complete inactivity.
  • Citation:PMID 7890027

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                             #    #                                   #  ##            
30315959     90 YLAWPAYWIMQgivctgIWVLAHEC-GHQSFstsKTLNNTVGwilhs----mllvpYHSWRISHSkHHKATGhmtkDQVF 164 Mortierella alpina
AAN51627      5 LSFFIGHWFLSaf---vQSFFLHRYaAHAMFk-mNKFWEKFFyiftcvaqgssflnPRAYAIMHRqHHAYSDtg-kDPHS 79  Leptospira inter...
ZP_00308095   9 IIFFVAHWYLSlf---sQTFFLHRYsAHAMFk-mNKFWEKFFfiflyltqgssylvPRAYGALHRmHHAYSDte-kDPHS 83  Cytophaga hutchi...
ZP_00554017  57 AAFLILSGATLca---gHSVGMHRLlIHRSFt-aPKWLERGLvwlgtl---vgmagPFGMIRAHDmRDWHQRq--aDCPP 127 Jannaschia sp. CCS1
ZP_00554018  55 GVTLVLMLLTLcl---gHSVGMHRLlIHRSFr-tPRWLEYVLmylgtl---vgmagPIGMFQIHEiRDWQQQq--pDCHS 125 Jannaschia sp. CCS1
YP_434334    54 LVFVVFTAATLcl---gHSLGMHRRlIHGSYe-cPKWMEYFFvhlgvl---vgmagPLGMVYQHDlRDWAQRk--aKCHS 124 Hahella chejuens...
YP_467975    52 IVFVLSTAITIcl---gHSVGMHRLlIHRSFs-aPLWLEHLLvylgtl---vgmagPFGMIYAHDiRDWAQRq--rDCHD 122 Rhizobium etli C...
ZP_01040221  71 VVVGLGLTGAMvl--lgHSVGFHRLlIHGSFe-tTPFLRRFLiwcgav---agmsgPIWIVKTHDlRDWAQRq--dDCHD 142 Erythrobacter sp...
AAY55583     73 ILFTALLTLLGtl---gVTVGVHRLwAHRTFt-aSKPLKVFLmfcqtt---agqgsIYSVVQAHRlHHAKFQqd-eDPYY 144 fruit fly
EAA07943     53 CVFTFLLTLFGil---gVTAGAHRLwAHRTYe-aTALLRFTLmicqtl---agqgsIYDWVRMHRlHHEKFRtv-dDPYY 124 Anopheles gambia...
Feature 1                                                                                       
30315959    165 Vpktrsqvglppkenaaaavqeedmsvhldeeapivtlfwmviqflfgwpaylimnasgqdygrwtshfhtyspifeprn 244 Mortierella alpina
AAN51627     80 Pvaskgfldmmwktalnyeaileettnvekefkgnypewpaidvls---------------------------------- 125 Leptospira inter...
ZP_00308095  84 Plysrnafvmmwktkdiynavlrreaqvedkfnknlpewafidnig---------------------------------- 129 Cytophaga hutchi...
ZP_00554017 128 Hpshgagwvrdawwqlccrfdlthpprfeieqevtedpw----------------------------------------- 166 Jannaschia sp. CCS1
ZP_00554018 126 Fakhdvgfwrdamwqmhceqrldhppalhiedrvaqdpf----------------------------------------- 164 Jannaschia sp. CCS1
YP_434334   125 Ylrhgtrfltdgwrqlncdlrlehppefcpesaikddpv----------------------------------------- 163 Hahella chejuens...
YP_467975   123 Lyahrrsffvdalwqmhcavaldepprfvveerarhdrfyrll------------------------------------- 165 Rhizobium etli C...
ZP_01040221 143 Ylahrrpmlqdawwqlhctlnldnpprynvarleesrfirwl-------------------------------------- 184 Erythrobacter sp...
AAY55583    145 Skhsfmyaqvrggllkyspqqeellkdvdmsdlesdpvvmfqkrfy---------------------------------- 190 fruit fly
EAA07943    125 Sdkdfmhaqvfanirklsprqeqllaavdmsdleadgivmfqrrfy---------------------------------- 170 Anopheles gambia...
Feature 1                                                                                       
30315959    245 ffdiiisdlgvlaalgaliyasmqlslltvtkyyivpylfvnfwlvlITFLQHTDpklphyregawnfqrgalctvdrsf 324 Mortierella alpina
AAN51627    126 --nswtfrlfcgtlytlfyfyfvpegqyawylllpihwlmgplhgaiVNWCGHMYgyrnhkkn------------pdnsk 191 Leptospira inter...
ZP_00308095 130 --dmwisriiwgtlyvlfyiyfvpadmwylylllpihflmgpvhgaiVNWFGHKLgyqnfdnk-------------dasr 194 Cytophaga hutchi...
ZP_00554017 167 ----------yhwmerhwraqqlipaivlfalggvglmlwgvclrvsVSLIGHWAvghaahkgghqgs--evrglpvqgy 234 Jannaschia sp. CCS1
ZP_00554018 165 ----------yrwleatwrwqqlplaallfamggvgfvlwgiglrvaVSLAGHWVtvhfahtrgerpf--vqddiavdgr 232 Jannaschia sp. CCS1
YP_434334   164 ----------yrfmertwmwqqlpwalllywlgdigwvvwgisariaVSVTGHWLigyfahnsgerdw--hvngaavqgh 231 Hahella chejuens...
YP_467975   166 ------eatwmaqqiplalllfslgglpwlvwgiavrisvsltghwlVGHFAHRNghqgwsvdd----------vavqgy 229 Rhizobium etli C...
ZP_01040221 185 ------ertwmlqqlpiaallywlggwpfvvwgvfvrvtltvhghwfVGHLAHRRgpqswevrg----------agvqah 248 Erythrobacter sp...
AAY55583    191 --vllyiflnvllsvntpfqyfgdslatsmfvgfwlrslivinlgnlVHSSHFIWsihkgf----------------kpt 252 fruit fly
EAA07943    171 --wamylvlfvllpinapleywgdtvqaaifvafslrylvvlnvawlINSAHFVWgldknh----------------kqs 232 Anopheles gambia...
Feature 1                     #  ##   
30315959    325 gkfLDHMfhgivhTHVAHHLFS 346 Mortierella alpina
AAN51627    192 ntlFVDFmiagelYQNNHHAHP 213 Leptospira interrogans serovar Lai str. 56601
ZP_00308095 195 ntlALDVllggelFQNNHHMYG 216 Cytophaga hutchinsonii
ZP_00554017 235 nlrGLGLlsfgecFHGNHHAFP 256 Jannaschia sp. CCS1
ZP_00554018 233 nlpALGFvtfgeaFHNNHHAFP 254 Jannaschia sp. CCS1
YP_434334   232 nvrFAGLltmgesWHNNHHAFP 253 Hahella chejuensis KCTC 2396
YP_467975   230 nlpRFGLvtfgesFHGNHHAFP 251 Rhizobium etli CFN 42
ZP_01040221 249 dvpWAGVptmgeaWHNNHHAYP 270 Erythrobacter sp. NAP1
AAY55583    253 dsnSIFLitk-syWPQYHYLLP 273 fruit fly
EAA07943    233 dsnMVFLvtk-syWPQYHYLLP 253 Anopheles gambiae str. PEST

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