FAC2B_CALOF
ID FAC2B_CALOF Reviewed; 372 AA.
AC Q9FPP7;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Fatty acid conjugase FAC2 B {ECO:0000305};
DE Short=CoFac2 {ECO:0000305};
DE EC=1.14.19.14 {ECO:0000269|PubMed:11067856};
DE AltName: Full=CoFadX-1 {ECO:0000303|PubMed:11067856};
GN Name=FAC2A {ECO:0000305};
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:AAG42260.1};
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).
CC -!- FUNCTION: Fatty acid conjugase converting 18:2(9Z, 12Z) to calendic
CC acid 18:3(8E, 10E, 12Z) (PubMed:11067856). Converts alpha-linolenic
CC acid (18:3(9Z, 12Z, 15Z)) into 18:4(8E, 10E, 12Z, 15Z)
CC (PubMed:11067856). Also has weak activity on the mono-unsaturates
CC 16:1(9Z) and 18:1(9Z) producing two conjugated double bonds at delta(8)
CC and delta(10) position (By similarity). {ECO:0000250|UniProtKB:Q9FPP8,
CC ECO:0000269|PubMed:11067856}.
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};
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. {ECO:0000269|PubMed:11067856}.
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; AF310156; AAG42260.1; -; mRNA.
DR AlphaFoldDB; Q9FPP7; -.
DR KEGG; ag:AAG42260; -.
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: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..372
FT /note="Fatty acid conjugase FAC2 B"
FT /id="PRO_0000435419"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
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 304..308
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 43365 MW; 351A040348199C7E CRC64;
MGKAASAKKV LERVPISKPP FEYNDLKKAV PPHCFSRPLS RSLYFLFHDI IVTCILFYVA
SNYIHMLPRF LSCIVWPVYW ISQGVFLGRL WMIGHECGHH SFSNYRWVDD TVGFLIHTAT
LTPYFSFKYS HRNHHAHTNS MEYDEVHIPK RKSEALYFEF LGNNPIGLMI TMLCKLTFGY
AAYIMFNYTG KKHKSGGLAS HFYPQSPLFN DSERNHVLFS DIGICIVLYA CYRIVTVTGA
MPAFYVYGIP WVIMSAILFA ATYLQHTHPS IPHYDTTEWN WLRGALSTID RDLGFFNMNK
THYHVIHHLF PVIPEYHAQE ATEAIKPILG QYYKYDGTPF LKALWREMKE CIYVESDEGQ
KKQGIYWFKN KT
