D5FAD_MORAP
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 03-AUG-2022, entry version 96.
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; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Mortierella.
OX NCBI_TaxID=64518;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CBS 210.32 / BCRC 32738 / CECT 2981;
RX PubMed=9668087; DOI=10.1074/jbc.273.30.19055;
RA Michaelson L.V., Lazarus C.M., Griffiths G., Napier J.A., 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., Bobik E.G. Jr.,
RA 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 at
CC the 5-position in 20-carbon polyunsaturated fatty acids incorporated in
CC a glycerolipid that contain a Delta(8) double bond. Involved in the
CC conversion of di-homo-Delta-linolenic acid to arachidonic acid.
CC Essential in the production of eicosanoids.
CC {ECO:0000269|PubMed:9668087, ECO:0000269|PubMed:9792636}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (8Z,11Z,14Z)-icosatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46260, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:90076,
CC ChEBI:CHEBI:90077; EC=1.14.19.30;
CC Evidence={ECO:0000269|PubMed:9668087};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (8Z,11Z,14Z,17Z)-eicosatetraenoyl-containing glycerolipid +
CC 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46264, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:90082,
CC ChEBI:CHEBI:90083; EC=1.14.19.30;
CC Evidence={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}.
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DR EMBL; AF054824; AAC39508.1; -; mRNA.
DR EMBL; AF067654; AAC72755.1; -; mRNA.
DR AlphaFoldDB; O74212; -.
DR SMR; O74212; -.
DR BioCyc; MetaCyc:MON-19037; -.
DR BRENDA; 1.14.19.30; 3431.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102866; F:di-homo-gamma-linolenate delta5 desaturase activity; IEA:RHEA.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; 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; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 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 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; Heme;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..446
FT /note="Acyl-lipid (8-3)-desaturase"
FT /id="PRO_0000185409"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 6..82
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 171..175
FT /note="Histidine box-1"
FT MOTIF 207..212
FT /note="Histidine box-2"
FT MOTIF 387..391
FT /note="Histidine box-3"
FT BINDING 41
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 64
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT VARIANT 21
FT /note="G -> D (in strain: ATCC 32221)"
FT VARIANT 88
FT /note="V -> I (in strain: ATCC 32221)"
FT VARIANT 111
FT /note="D -> N (in strain: ATCC 32221)"
FT VARIANT 227
FT /note="F -> S (in strain: ATCC 32221)"
FT VARIANT 248
FT /note="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
