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MULTISPECIES: fatty acid desaturase [Pseudomonas].


LOCUS       WP_003114464             312 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_003114464
VERSION     WP_003114464.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Shen,J., Wu,G., Tsai,A.L. and Zhou,M.
  TITLE     Structure and Mechanism of a Unique Diiron Center in Mammalian
            Stearoyl-CoA Desaturase
  JOURNAL   J Mol Biol 432 (18), 5152-5161 (2020)
   PUBMED   32470559
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Wang,H., Klein,M.G., Zou,H., Lane,W., Snell,G., Levin,I., Li,K. and
            Sang,B.C.
  TITLE     Crystal structure of human stearoyl-coenzyme A desaturase in
            complex with substrate
  JOURNAL   Nat Struct Mol Biol 22 (7), 581-585 (2015)
   PUBMED   26098317
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Lindqvist,Y., Huang,W., Schneider,G. and Shanklin,J.
  TITLE     Crystal structure of delta9 stearoyl-acyl carrier protein
            desaturase from castor seed and its relationship to other di-iron
            proteins
  JOURNAL   EMBO J 15 (16), 4081-4092 (1996)
   PUBMED   8861937
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Shanklin,J. and Somerville,C.
  TITLE     Stearoyl-acyl-carrier-protein desaturase from higher plants is
            structurally unrelated to the animal and fungal homologs
  JOURNAL   Proc Natl Acad Sci U S A 88 (6), 2510-2514 (1991)
   PUBMED   2006187
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Wada,H., Gombos,Z. and Murata,N.
  TITLE     Enhancement of chilling tolerance of a cyanobacterium by genetic
            manipulation of fatty acid desaturation
  JOURNAL   Nature 347 (6289), 200-203 (1990)
   PUBMED   2118597
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Kaestner,K.H., Ntambi,J.M., Kelly,T.J. Jr. and Lane,M.D.
  TITLE     Differentiation-induced gene expression in 3T3-L1 preadipocytes. A
            second differentially expressed gene encoding stearoyl-CoA
            desaturase
  JOURNAL   J Biol Chem 264 (25), 14755-14761 (1989)
   PUBMED   2570068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF012699.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00487.30
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..312
                     /product="fatty acid desaturase"
                     /EC_number="1.14.19.-"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36292
     Region          25..311
                     /region_name="Membrane-FADS-like"
                     /note="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...;
                     cl00615"
                     /db_xref="CDD:445012"
     Site            order(69,73,104,107..108,255,258..259)
                     /site_type="other"
                     /note="putative di-iron ligands [ion binding]"
                     /db_xref="CDD:238511"
ORIGIN      
        1 mahylsgrqr tlvrrlqdtf qarsewptwl lvaclyggwa llasqyerwg wpvlaglvpf
       61 aslymslqhe lihghptrwp rfnamlgylp lavwypyply rdshlrhhld eqltypgldp
      121 esryvslsew prlgswrrrw lcldktllgr atlgpllala amarlegsrl rrgegaawrl
      181 wglhavllgg llaglwrwag ippwlylpav aypalglsml rsfyehrpar epaqrsvlvd
      241 agwpwrllfl nnnlhlvhhd lpglpwyllp rvysasrray rrrsgdfhlp gygrlwrrhg
      301 wrpvdapvhp eh