ID   FAD3E_MORAP             Reviewed;         403 AA.
AC   Q59J82;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Acyl-lipid omega-3 desaturase (cytochrome b5), endoplasmic reticulum {ECO:0000303|PubMed:15538555};
DE            EC=1.14.19.25 {ECO:0000269|PubMed:15538555};
DE   AltName: Full=Omega-3 fatty acid desaturase 3, endoplasmic reticulum {ECO:0000303|PubMed:15538555};
GN   Name=MAW3 {ECO:0000303|PubMed:15538555};
OS   Mortierella alpina (Oleaginous fungus) (Mortierella renispora).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Mortierella.
OX   NCBI_TaxID=64518 {ECO:0000312|EMBL:BAD91495.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=15538555; DOI=10.1007/s00253-004-1760-x;
RA   Sakuradani E., Abe T., Iguchi K., Shimizu S.;
RT   "A novel fungal omega3-desaturase with wide substrate specificity from
RT   arachidonic acid-producing Mortierella alpina 1S-4.";
RL   Appl. Microbiol. Biotechnol. 66:648-654(2005).
CC   -!- FUNCTION: omega(3) desaturase that uses both 18-carbon and 20-carbon n-
CC       6 polyunsaturated fatty acids as substrates.
CC       {ECO:0000269|PubMed:15538555}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC         [cytochrome b5] + 2 H(+) + O2 = (9Z,12Z,15Z)-octadecatrienoyl-
CC         containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:46404, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88351,
CC         ChEBI:CHEBI:90078; EC=1.14.19.25;
CC         Evidence={ECO:0000269|PubMed:15538555};
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC       {ECO:0000269|PubMed:15538555}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC       involved in metal ion binding. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AB182163; BAD91495.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59J82; -.
DR   BioCyc; MetaCyc:MON-16937; -.
DR   BRENDA; 1.14.19.25; 3431.
DR   UniPathway; UPA00658; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0102872; F:1-16:0-2-18:2-phosphatidylcholine desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102859; F:1-18:1-2-18:2-phosphatidylcholine desaturase activity (SN2-18:3 forming); IEA:UniProtKB-EC.
DR   GO; GO:0102856; F:1-18:2-2-18:2-sn-glycerol-3-phosphocholine desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102862; F:1-18:2-2-18:2-sn-glycerol-3-phosphocholine desaturase activity (SN2-18:3 forming); IEA:UniProtKB-EC.
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; IDA:UniProtKB.
DR   GO; GO:0036109; P:alpha-linolenic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   Pfam; PF00487; FA_desaturase; 1.
PE   1: Evidence at protein level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..403
FT                   /note="Acyl-lipid omega-3 desaturase (cytochrome b5),
FT                   endoplasmic reticulum"
FT                   /id="PRO_0000435456"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           110..114
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           146..150
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           342..346
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   403 AA;  46465 MW;  A0F5CEF4E61E25B9 CRC64;
     MAPPHVVDEQ VRRRIVVEDE IKSKKQFERN YVPMDFTIKE IRDAIPAHLF IRDTTKSILH
     VVKDLVTIAI VFYCATFIET LPSLALRVPA WITYWIIQGT VMVGPWILAH ECGHGAFSDS
     KTINTIFGWV LHSALLVPYQ AWAMSHSKHH KGTGSMTKDV VFIPATRSYK GLPALEKPAV
     EEEVSEQEHH HHEESIFAET PIYTLGALLF VLTFGWPLYL IVNFSGHEAP HWVNHFQTVA
     PLYEPHQRKN IFYSNCGIVA MGSILTYLSM VFSPLTVFMY YGIPYLGVNA WIVCITYLQH
     TDPKVPHFRD NEWNFQRGAA CTIDRSFGTI VNHLHHHIGD SHQCHHMFSQ MPFYNAVEAT
     KYLKAKLGKY YIFDDTPIAK ALYRNWRECK FVEDEGDVVF YKH