FAD12_MORAP
ID FAD12_MORAP Reviewed; 400 AA.
AC Q9Y8H5; Q96TH3; Q9UVV4;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Delta(12) fatty acid desaturase;
DE EC=1.14.19.6 {ECO:0000269|PubMed:10215899, ECO:0000269|PubMed:10478922};
DE AltName: Full=Delta-12 fatty acid desaturase;
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=1S-4;
RX PubMed=10215899; DOI=10.1046/j.1432-1327.1999.00333.x;
RA Sakuradani E., Kobayashi M., Ashikari T., Shimizu S.;
RT "Identification of delta12-fatty acid desaturase from arachidonic acid-
RT producing Mortierella fungus by heterologous expression in the yeast
RT Saccharomyces cerevisiae and the fungus Aspergillus oryzae.";
RL Eur. J. Biochem. 261:812-820(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 32221 / CBS 527.72 / M135;
RX PubMed=10478922; DOI=10.1007/s11745-999-0410-8;
RA Huang Y.-S., Chaudhary S., Thurmond J.M., Bobik E.G. Jr., Yuan L.,
RA Chan G.M., Kirchner S.J., Mukerji P., Knutzon D.S.;
RT "Cloning of delta12- and delta6-desaturases from Mortierella alpina and
RT recombinant production of gamma-linolenic acid in Saccharomyces
RT cerevisiae.";
RL Lipids 34:649-659(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 16266 / C 112;
RA Liu L., Li M., Xing L., Hu G.;
RT "Delta 12 fatty acid desaturase gene of Mortierella alpina.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND MUTAGENESIS OF HIS-116 AND PRO-166.
RX PubMed=19217543; DOI=10.1016/j.jbiosc.2008.10.011;
RA Sakuradani E., Abe T., Matsumura K., Tomi A., Shimizu S.;
RT "Identification of mutation sites on Delta12 desaturase genes from
RT Mortierella alpina 1S-4 mutants.";
RL J. Biosci. Bioeng. 107:99-101(2009).
CC -!- FUNCTION: Catalyzes the desaturation of oleic acid (Delta(9)-18:1) to
CC linoleic acid (Delta(9), Delta(12)-18:2). {ECO:0000269|PubMed:10215899,
CC ECO:0000269|PubMed:10478922, ECO:0000269|PubMed:19217543}.
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:0000269|PubMed:10215899, ECO:0000269|PubMed:10478922};
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:0000269|PubMed:10215899, ECO:0000269|PubMed:10478922};
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB020033; BAA81754.1; -; mRNA.
DR EMBL; AF110509; AAF08684.1; -; mRNA.
DR EMBL; AF417244; AAL13300.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y8H5; -.
DR BioCyc; MetaCyc:MON-16938; -.
DR BRENDA; 1.14.19.6; 3431.
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:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0102987; F:palmitoleic acid delta 12 desaturase activity; IEA:RHEA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein 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_0000185422"
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"
FT MUTAGEN 116
FT /note="H->Y: In SR88; exhibits a complete delta(12)
FT desaturation deficiency with accumulation of Mead acid."
FT /evidence="ECO:0000269|PubMed:19217543"
FT MUTAGEN 166
FT /note="P->L: In Mut48; exhibits a complete delta(12)
FT desaturation deficiency with accumulation of Mead acid."
FT /evidence="ECO:0000269|PubMed:19217543"
FT CONFLICT 17..19
FT /note="STS -> TTT (in Ref. 3; AAL13300)"
FT /evidence="ECO:0000305"
FT CONFLICT 21..23
FT /note="APT -> PN (in Ref. 2; AAF08684)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="A -> V (in Ref. 2; AAF08684)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="I -> V (in Ref. 2; AAF08684)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="N -> S (in Ref. 3; AAL13300)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..182
FT /note="AAA -> VAV (in Ref. 1; BAA81754)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="A -> T (in Ref. 1; BAA81754)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="V -> I (in Ref. 3; AAL13300)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="Y -> H (in Ref. 1; BAA81754)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="H -> Q (in Ref. 2; AAF08684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 46001 MW; 40B2FC1C1E01F93F CRC64;
MAPPNTIDAG LTQRHISTSA APTSAKPAFE RNYQLPEFTI KEIRECIPAH CFERSGLRGL
CHVAIDLTWA SLLFLAATQI DKFENPLIRY LAWPAYWIMQ GIVCTGIWVL AHECGHQSFS
TSKTLNNTVG WILHSMLLVP YHSWRISHSK HHKATGHMTK DQVFVPKTRS QVGLPPKENA
AAAVQEEDMS VHLDEEAPIV TLFWMVIQFL FGWPAYLIMN ASGQDYGRWT SHFHTYSPIF
EPRNFFDIII SDLGVLAALG ALIYASMQLS LLTVTKYYIV PYLFVNFWLV LITFLQHTDP
KLPHYREGAW NFQRGALCTV DRSFGKFLDH MFHGIVHTHV AHHLFSQMPF YHAEEATYHL
KKLLGEYYVY DPSPIVVAVW RSFRECRFVE DHGDVVFFKK
