ID FAD5_MORAP Reviewed; 446 AA.
AC O74212;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-APR-2013, entry version 66.
DE RecName: Full=Delta(5) fatty acid desaturase;
DE Short=Delta-5 fatty acid desaturase;
DE EC=1.14.19.-;
GN Name=DES1;
OS Mortierella alpina (Mortierella renispora).
OC Eukaryota; Fungi; Fungi incertae sedis;
OC Early diverging fungal lineages; Mortierellomycotina; Mortierellales;
OC Mortierellaceae; Mortierella.
OX NCBI_TaxID=64518;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CBS 210.32 / CCRC 32738;
RX PubMed=9668087; DOI=10.1074/jbc.273.30.19055;
RA Michaelson L.V., Lazarus C.M., Griffiths G., Napier J.A.,
RA Stobart A.K.;
RT "Isolation of a delta5-fatty acid desaturase gene from Mortierella
RT alpina.";
RL J. Biol. Chem. 273:19055-19059(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 32221 / CBS 527.72 / M135;
RX PubMed=9792636; DOI=10.1074/jbc.273.45.29360;
RA Knutzon D.S., Thurmond J.M., Huang Y.-S., Chaudhary S.,
RA Bobik E.G. Jr., Chan G.M., Kirchner S.J., Mukerji P.;
RT "Identification of delta5-desaturase from Mortierella alpina by
RT heterologous expression in baker's yeast and canola.";
RL J. Biol. Chem. 273:29360-29366(1998).
CC -!- FUNCTION: Involved in the conversion of di-homo-Delta-linolenic
CC acid to arachidonic acid. Essential in the production of
CC eicosanoids.
CC -!- COFACTOR: Iron (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- DOMAIN: The histidine box domains may contain the active site
CC and/or be involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase family.
CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
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DR EMBL; AF054824; AAC39508.1; -; mRNA.
DR EMBL; AF067654; AAC72755.1; -; mRNA.
DR ProteinModelPortal; O74212; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR012171; Fatty_acid/sphinglp_desaturase.
DR InterPro; IPR005804; Fatty_acid_desaturase-1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SUPFAM; SSF55856; Cyt_B5; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Fatty acid biosynthesis; Fatty acid metabolism;
KW Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Metal-binding; Oxidoreductase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 446 Delta(5) fatty acid desaturase.
FT /FTId=PRO_0000185409.
FT TRANSMEM 125 145 Helical; (Potential).
FT TRANSMEM 150 170 Helical; (Potential).
FT DOMAIN 6 82 Cytochrome b5 heme-binding.
FT MOTIF 171 175 Histidine box-1.
FT MOTIF 207 212 Histidine box-2.
FT MOTIF 387 391 Histidine box-3.
FT METAL 41 41 Iron (heme axial ligand) (By similarity).
FT METAL 64 64 Iron (heme axial ligand) (By similarity).
FT VARIANT 21 21 G -> D (in strain: ATCC 32221).
FT VARIANT 88 88 V -> I (in strain: ATCC 32221).
FT VARIANT 111 111 D -> N (in strain: ATCC 32221).
FT VARIANT 227 227 F -> S (in strain: ATCC 32221).
FT VARIANT 248 248 D -> H (in strain: ATCC 32221).
SQ SEQUENCE 446 AA; 51288 MW; 8395741C5A3CC9A2 CRC64;
MGTDQGKTFT WEELAAHNTK GDLFLAIRGR VYDVTKFLSR HPGGVDTLLL GAGRDVTPVF
EMYHAFGAAD AIMKKYYVGT LVSNELPVFP EPTVFHKTIK TRVEGYFTDR DIDPKNRPEI
WGRYALIFGS LIASYYAQLF VPFVVERTWL QVVFAIIMGF ACAQVGLNPL HDASHFSVTH
NPTVWKILGA THDFFNGASY LVWMYQHMLG HHPYTNIAGA DPDVSTFEPD VRRIKPNQKW
FVNHINQDMF VPFLYGLLAF KVRIQDINIL YFVKTNDAIR VNPISTWHTV MFWGGKAFFV
WYRLIVPLQY LPLGKVLLLF TVADMVSSYW LALTFQANHV VEEVQWPLPD ENGIIQKDWA
AMQVETTQDY AHDSHLWTSI TGSLNYQAVH HLFPNVSQHH YPDILAIIKN TCSEYKVPYL
VKDTFWQAFA SHLEHLRVLG LRPKEE
//
