FAC2A_CALOF
ID FAC2A_CALOF Reviewed; 374 AA.
AC Q9FPP8;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Fatty acid conjugase FAC2 A {ECO:0000303|PubMed:11161042};
DE Short=CoFac2 {ECO:0000303|PubMed:11161042};
DE EC=1.14.19.14 {ECO:0000269|PubMed:11067856, ECO:0000269|PubMed:11161042, ECO:0000269|PubMed:12383261};
DE AltName: Full=CoFadX-1 {ECO:0000303|PubMed:11067856};
GN Name=FAC2A {ECO:0000303|PubMed:11161042};
OS Calendula officinalis (Pot marigold).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Calenduleae;
OC Calendula.
OX NCBI_TaxID=41496 {ECO:0000312|EMBL:AAG42259.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11067856; DOI=10.1074/jbc.m009188200;
RA Cahoon E.B., Ripp K.G., Hall S.E., Kinney A.J.;
RT "Formation of conjugated delta8,delta10-double bonds by delta12-oleic-acid
RT desaturase-related enzymes: biosynthetic origin of calendic acid.";
RL J. Biol. Chem. 276:2637-2643(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=11161042; DOI=10.1104/pp.125.2.847;
RA Qiu X., Reed D.W., Hong H., MacKenzie S.L., Covello P.S.;
RT "Identification and analysis of a gene from Calendula officinalis encoding
RT a fatty acid conjugase.";
RL Plant Physiol. 125:847-855(2001).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12383261; DOI=10.1046/j.1432-1033.2002.03209.x;
RA Reed D.W., Savile C.K., Qiu X., Buist P.H., Covello P.S.;
RT "Mechanism of 1,4-dehydrogenation catalyzed by a fatty acid (1,4)-
RT desaturase of Calendula officinalis.";
RL Eur. J. Biochem. 269:5024-5029(2002).
CC -!- FUNCTION: Fatty acid conjugase converting 18:2(9Z, 12Z) to calendic
CC acid 18:3(8E, 10E, 12Z) (PubMed:11067856, PubMed:11161042,
CC PubMed:12383261). Converts alpha-linolenic acid (18:3(9Z, 12Z, 15Z))
CC into 18:4(8E, 10E, 12Z, 15Z) (PubMed:11067856). Also has weak activity
CC on the mono-unsaturates 16:1(9Z) and 18:1(9Z) producing two conjugated
CC double bonds at delta(8) and delta(10) position (PubMed:11161042).
CC {ECO:0000269|PubMed:11067856, ECO:0000269|PubMed:11161042,
CC ECO:0000269|PubMed:12383261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + AH2 + O2
CC = A + a (8E,10E,12Z)-octadecatrienoyl-containing glycerolipid + 2
CC H2O; Xref=Rhea:RHEA:46440, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:88257,
CC ChEBI:CHEBI:88351; EC=1.14.19.14;
CC Evidence={ECO:0000269|PubMed:11067856, ECO:0000269|PubMed:11161042};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:11067856};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the developing seeds. Not
CC detected in leaves or flower buds. {ECO:0000269|PubMed:11067856,
CC ECO:0000269|PubMed:11161042}.
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; AF310155; AAG42259.1; -; mRNA.
DR EMBL; AF343064; AAK26632.1; -; mRNA.
DR AlphaFoldDB; Q9FPP8; -.
DR KEGG; ag:AAG42259; -.
DR BRENDA; 1.14.19.14; 13728.
DR UniPathway; UPA00658; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
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 Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Microsome; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..374
FT /note="Fatty acid conjugase FAC2 A"
FT /id="PRO_0000435418"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 95..99
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 131..135
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 306..310
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 43625 MW; C64AE2A9DF6D3126 CRC64;
MGKGASNKKV LERVPITKPP FEYNDLKKAV PPHCFSRPLF RSFYFLLHDI IVTCILFYVA
SNYIPMLPGF LSYIVWPVYW ISQGVFLGRL WMIGHECGHH SFSNYRWVDD SVGFLIHTAT
LTPYFSFKYS HRNHHAHTNS MEYDEVHIPK RKSEALDLYF EFLGNNPMGL MITMLCKLTF
GYAAYIMFNY TGKKHKSGGL ASHFYPQSPL FNDSERNHVL FSDVGICIVL YACYRIVMVT
GAMSAFYVYG IPWVIMSAIL FAATYLQHTH PSIPHYDTTE WNWLRGALST IDRDLGFFNM
NKTHYHVIHH LFPVIPEYHA QEATEAIKPI LGQYYKYDGT PFLKALWREM KDCIYVESDQ
GQKKQGIYWF KNKI
