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Database: UniProt
Entry: O74212
LinkDB: O74212
Original site: O74212 
ID   D5FAD_MORAP             Reviewed;         446 AA.
AC   O74212;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   11-MAY-2016, entry version 77.
DE   RecName: Full=Acyl-lipid (8-3)-desaturase;
DE            EC=1.14.19.30 {ECO:0000269|PubMed:9668087};
DE   AltName: Full=Delta(5) fatty acid desaturase {ECO:0000303|PubMed:9668087};
DE            Short=Delta-5 fatty acid desaturase {ECO:0000303|PubMed:9668087};
GN   Name=DES1;
OS   Mortierella alpina (Oleaginous fungus) (Mortierella renispora).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mortierellomycotina;
OC   Mortierellales; Mortierellaceae; Mortierella.
OX   NCBI_TaxID=64518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
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], AND FUNCTION.
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: Fatty acid desaturase that introduces a cis double bond
CC       at the 5-position in 20-carbon polyunsaturated fatty acids
CC       incorporated in a glycerolipid that contain a Delta(8) double
CC       bond. Involved in the conversion of di-homo-Delta-linolenic acid
CC       to arachidonic acid. Essential in the production of eicosanoids.
CC       {ECO:0000269|PubMed:9668087, ECO:0000269|PubMed:9792636}.
CC   -!- CATALYTIC ACTIVITY: An (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-
CC       [glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) = a
CC       (5Z,8Z,11Z,14Z)-icosatetra-5,8,11,14-tetraenoyl-[glycerolipid] + 2
CC       ferricytochrome b5 + 2 H(2)O. {ECO:0000269|PubMed:9668087}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:O00767};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DOMAIN: The cytochrome b5 heme-binding domain acts as the direct
CC       electron donor to the active site of the desaturase, and does not
CC       require an external cytochrome. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00279}.
DR   EMBL; AF054824; AAC39508.1; -; mRNA.
DR   EMBL; AF067654; AAC72755.1; -; mRNA.
DR   ProteinModelPortal; O74212; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; 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_desaturase.
DR   InterPro; IPR005804; Fatty_acid_desaturase_dom.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   1: Evidence at protein 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       Acyl-lipid (8-3)-desaturase.
FT                                /FTId=PRO_0000185409.
FT   TRANSMEM    125    145       Helical. {ECO:0000255}.
FT   TRANSMEM    150    170       Helical. {ECO:0000255}.
FT   DOMAIN        6     82       Cytochrome b5 heme-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
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).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
FT   METAL        64     64       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
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
//
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