ID   FAD12_CREAL             Reviewed;         375 AA.
AC   O81931;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Delta(12) fatty acid dehydrogenase;
DE            EC=1.14.19.39 {ECO:0000269|PubMed:9572738};
DE   AltName: Full=Crepenynate synthase;
DE   AltName: Full=Delta-12 fatty acid acetylenase;
OS   Crepis alpina (Hawksbeard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Crepidinae; Crepis.
OX   NCBI_TaxID=72610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9572738; DOI=10.1126/science.280.5365.915;
RA   Lee M., Lenman M., Banas A., Bafor M., Singh S., Schweizer M., Nilsson R.,
RA   Liljenberg C., Dahlqvist A., Gummeson P.O., Sjoedahl S., Green A.,
RA   Stymne S.;
RT   "Identification of non-heme diiron proteins that catalyze triple bond and
RT   epoxy group formation.";
RL   Science 280:915-918(1998).
CC   -!- FUNCTION: Changes the delta-12 double bond of linoleic acid into a
CC       triple bond in the biosynthesis of crepenynic acid.
CC       {ECO:0000269|PubMed:9572738}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC         [cytochrome b5] + 2 H(+) + O2 = a (9Z)-octadec-9-en-12-ynoyl-
CC         containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:46552, 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:88260,
CC         ChEBI:CHEBI:88351; EC=1.14.19.39;
CC         Evidence={ECO:0000269|PubMed:9572738};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Seed.
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; Y16285; CAA76158.2; -; mRNA.
DR   AlphaFoldDB; O81931; -.
DR   KEGG; ag:CAA76158; -.
DR   BioCyc; MetaCyc:MON-14155; -.
DR   UniPathway; UPA00658; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..375
FT                   /note="Delta(12) fatty acid dehydrogenase"
FT                   /id="PRO_0000185424"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           98..102
FT                   /note="Histidine box-1"
FT   MOTIF           134..138
FT                   /note="Histidine box-2"
FT   MOTIF           308..312
FT                   /note="Histidine box-3"
SQ   SEQUENCE   375 AA;  43382 MW;  B31F5A64DD0C2926 CRC64;
     MGGGGRGRTS QKPLMERVSV DPPFTVSDLK QAIPPHCFKR SVIRSSYYIV HDAIIAYIFY
     FLADKYIPIL PAPLAYLAWP LYWFCQASIL TGLWVIGHEC GHHAFSDYQW VDDTVGFILH
     SFLMTPYFSW KYSHRNHHAN TNSLDNDEVY IPKSKAKVAL YYKVLNHPPG RLLIMFITFT
     LGFPLYLFTN ISGKKYERFA NHFDPMSPIF KERERFQVLL SDLGLLAVLY GVKLAVAAKG
     AAWVTCIYGI PVLGVFIFFD IITYLHHTHL SLPHYDSSEW NWLRGALSTI DRDFGFLNSV
     LHDVTHTHVM HHLFSYIPHY HAKEARDAIN TVLGDFYKID RTPILKAMWR EAKECIFIEP
     EKGRGSKGVY WYNKF