FADX_PUNGR
ID FADX_PUNGR Reviewed; 395 AA.
AC Q84UB8; Q84VT1;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Bifunctional fatty acid conjugase/Delta(12)-oleate desaturase {ECO:0000303|PubMed:12464604};
DE Short=PgFAC {ECO:0000303|PubMed:12464604};
DE AltName: Full=Delta(12)-acyl-lipid-conjugase FADX {ECO:0000305|PubMed:12354116};
DE AltName: Full=Delta(12)-linoleic acid (1,4)-acyl-lipid-desaturase {ECO:0000303|PubMed:12354116};
DE AltName: Full=Delta(12)-oleate desaturase {ECO:0000303|PubMed:12464604};
DE EC=1.14.19.- {ECO:0000305};
DE AltName: Full=Fatty acid conjugase {ECO:0000303|PubMed:12464604};
DE AltName: Full=Linoleoyl-lipid Delta(12) conjugase (11E,13Z-forming) {ECO:0000303|PubMed:12354116};
DE EC=1.14.19.16 {ECO:0000269|PubMed:12354116};
GN Name=FADX {ECO:0000305}; Synonyms=FAC {ECO:0000303|PubMed:12464604};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000312|EMBL:AAO37753.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=12354116; DOI=10.1046/j.1432-1033.2002.03184.x;
RA Hornung E., Pernstich C., Feussner I.;
RT "Formation of conjugated Delta11Delta13-double bonds by Delta12-linoleic
RT acid (1,4)-acyl-lipid-desaturase in pomegranate seeds.";
RL Eur. J. Biochem. 269:4852-4859(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=12464604; DOI=10.1074/jbc.m210748200;
RA Iwabuchi M., Kohno-Murase J., Imamura J.;
RT "Delta 12-oleate desaturase-related enzymes associated with formation of
RT conjugated trans-delta 11, cis-delta 13 double bonds.";
RL J. Biol. Chem. 278:4603-4610(2003).
RN [3]
RP FUNCTION.
RX PubMed=25000918; DOI=10.1007/s00425-014-2109-z;
RA Mietkiewska E., Miles R., Wickramarathna A., Sahibollah A.F., Greer M.S.,
RA Chen G., Weselake R.J.;
RT "Combined transgenic expression of Punica granatum conjugase (FADX) and
RT FAD2 desaturase in high linoleic acid Arabidopsis thaliana mutant leads to
RT increased accumulation of punicic acid.";
RL Planta 240:575-583(2014).
CC -!- FUNCTION: Converts a single cis double bond at position 12 of linoleate
CC incorporated into phosphatidylcholine into conjugated 11-trans and 13-
CC cis double bonds (PubMed:12354116, PubMed:12464604, PubMed:25000918).
CC Produces punicic acid (18:3(9Z,11E,13Z)) from linoleic acid and
CC conjugated octadecatetraenoic fatty acid from gamma-linolenic acid
CC (PubMed:12354116, PubMed:25000918). No activity with cis- and trans-
CC vaccenic acid, alpha-linolenic acid or homo-gamma-linolenic acid
CC (PubMed:12354116). 16:2(9Z,12Z), 18:3(9Z,12Z,15Z) and 18:2(9Z,12Z) are
CC substrates for the conjugase to form trans-Delta(11) and cis-Delta(13)
CC double bonds (PubMed:12464604). No activity on the cis-Delta(9) double
CC bonds of oleic and palmitoleic acids (PubMed:12464604).
CC {ECO:0000269|PubMed:12354116, ECO:0000269|PubMed:12464604,
CC ECO:0000269|PubMed:25000918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a (9Z,11E,13Z)-octadeca-9,11,13-
CC trienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46532, 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:88259,
CC ChEBI:CHEBI:88351; EC=1.14.19.16;
CC Evidence={ECO:0000269|PubMed:12354116};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD24672.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ437140; CAD24672.1; ALT_SEQ; mRNA.
DR EMBL; AY178446; AAO37753.1; -; mRNA.
DR AlphaFoldDB; Q84UB8; -.
DR KEGG; ag:AAO37753; -.
DR KEGG; ag:CAD24672; -.
DR BioCyc; MetaCyc:MON-12610; -.
DR BRENDA; 1.14.19.16; 14164.
DR BRENDA; 1.14.19.33; 14164.
DR UniPathway; UPA00658; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR Pfam; PF11960; DUF3474; 1.
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..395
FT /note="Bifunctional fatty acid conjugase/Delta(12)-oleate
FT desaturase"
FT /id="PRO_0000434635"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 118..122
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 154..158
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 328..332
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="P -> S (in Ref. 1; CAD24672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 45828 MW; F0E6BA0435A3F220 CRC64;
MGADGTMSPV LTKRRPDQEI NKLDIKPNHE VDIARRAPHS KPPFTLSDLR SAIPPHCFHR
SLLMSSSYLI RDFALAFLFY HSAVTYIPLL PKPLACMAWP VYWFLQGSNM LGIWVIAHEC
GHQAFSNYGW VNDAVGFFLH TSLLVPYFPF KYSHRRHHSN TNSVEHDEVF VPRHKDGVQW
YYRFFNNTPG RVLTLTLTLL VGWPSYLAFN ASGRPYDGFA SHYNPNAQIF NLRERFWVHV
SNIGILAIYY ILYRLATTKG LPWLLSIYGV PVLILNAFVV LITFLQHSHP ALPHYNSDEW
DWLRGALATV DRDYGFLNEV FHDITDTHVI HHLFPTMPHY NAKEATVSIR PILKDYYKFD
RTPIWRALWR EAKECLYVEA DGTGSKGVLW FKSKF
