ID   FAD12_MORIS             Reviewed;         400 AA.
AC   P59668;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Delta(12) fatty acid desaturase;
DE            EC=1.14.19.6 {ECO:0000250|UniProtKB:Q9Y8H5};
DE   AltName: Full=Delta-12 fatty acid desaturase;
OS   Mortierella isabellina (Filamentous fungus) (Umbelopsis isabellina).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Umbelopsidomycetes; Umbelopsidales; Umbelopsidaceae; Umbelopsis.
OX   NCBI_TaxID=91625;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=M6-22;
RA   Liu L., Li M., Xing L., Hu G.;
RT   "Delta 12 fatty acid desaturase mRNA of Mortierella isabellina.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the desaturation of oleic acid (Delta(9)-18:1) to
CC       linoleic acid (Delta(9), Delta(12)-18:2).
CC       {ECO:0000250|UniProtKB:Q9Y8H5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC         = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:25856, 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:57383,
CC         ChEBI:CHEBI:57387; EC=1.14.19.6;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y8H5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC         = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:45096, 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:61540,
CC         ChEBI:CHEBI:76552; EC=1.14.19.6;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y8H5};
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC       involved in metal ion binding.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF417245; AAL13301.1; -; mRNA.
DR   AlphaFoldDB; P59668; -.
DR   BRENDA; 1.14.19.6; 9352.
DR   UniPathway; UPA00658; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0102985; F:delta12-fatty-acid desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102987; F:palmitoleic acid delta 12 desaturase activity; IEA:RHEA.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   Pfam; PF00487; FA_desaturase; 1.
PE   2: Evidence at transcript level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Oxidoreductase; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..400
FT                   /note="Delta(12) fatty acid desaturase"
FT                   /id="PRO_0000185423"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           112..116
FT                   /note="Histidine box-1"
FT   MOTIF           148..152
FT                   /note="Histidine box-2"
FT   MOTIF           339..343
FT                   /note="Histidine box-3"
SQ   SEQUENCE   400 AA;  46016 MW;  F5512D3F8210DBD2 CRC64;
     MAPPNTIDAG LTQRHITTTA APTSAKPAFE RNYQLPEFTI KEIRECIPAH CFERSGLRGL
     CHVAIDLTWA SLLFLAATQI DKFENPLIRY LAWPAYWIMQ GIVCTGIWVL AHECGHQSFS
     TSKTLNNTVG WILHSMLLVP YHSWRISHSK HHKATGHMTK DQVFVPKTRS QVGLPPKESA
     AAAVQEEDMS VHLDEEAPIV TLFWMVIQFL FGWPAYLIMN ASGQDYGRWT SHFHTYSPIF
     EPRNFFDIII SDLGVLAALG ALIYASMQLS LLTVTKYYII PYLFVNFWLV LITFLQHTDP
     KLPHYREGAW NFQRGALCTV DRSFGKFLDH MFHGIVHTHV AHHLFSQMPF YHAEEATYHL
     KKLLGEYYVY DPSPIVVAVW RSFRECRFVE DHGDVVFFKK