FACR6_ARATH
ID FACR6_ARATH Reviewed; 548 AA.
AC B9TSP7; A0A1B1CQJ6; Q9LET6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Fatty acyl-CoA reductase 6, chloroplastic {ECO:0000303|PubMed:22166367, ECO:0000303|PubMed:22189440};
DE Short=AtFAR6 {ECO:0000303|PubMed:22166367};
DE EC=1.2.1.84 {ECO:0000269|PubMed:19062129};
DE Flags: Precursor;
GN Name=FAR6 {ECO:0000303|PubMed:22166367, ECO:0000303|PubMed:22189440};
GN OrderedLocusNames=At3g56700 {ECO:0000312|Araport:AT3G56700};
GN ORFNames=T8M16.30 {ECO:0000312|EMBL:CAC00733.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=19062129; DOI=10.1016/j.jplph.2008.10.003;
RA Doan T.P.T., Carlsson A.S., Hamberg M., Buelow L., Stymne S., Olsson P.;
RT "Functional expression of five Arabidopsis fatty acyl-CoA reductase genes
RT in Escherichia coli.";
RL J. Plant Physiol. 166:787-796(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Rutter C.D., Rao C.V.;
RT "Production of decanol by engineering yarrowia lipolytica.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16980563; DOI=10.1104/pp.106.086785;
RA Rowland O., Zheng H., Hepworth S.R., Lam P., Jetter R., Kunst L.;
RT "CER4 encodes an alcohol-forming fatty acyl-coenzyme A reductase involved
RT in cuticular wax production in Arabidopsis.";
RL Plant Physiol. 142:866-877(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22166367; DOI=10.1016/j.bbalip.2011.10.019;
RA Doan T.T.P., Domergue F., Fournier A.E., Vishwanath S.J., Rowland O.,
RA Moreau P., Wood C.C., Carlsson A.S., Hamberg M., Hofvander P.;
RT "Biochemical characterization of a chloroplast localized fatty acid
RT reductase from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1821:1244-1255(2012).
RN [8]
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP INDUCTION BY WOUNDING.
RC STRAIN=cv. Columbia;
RX PubMed=22189440; DOI=10.1007/s00299-011-1205-9;
RA Gupta N.C., Jain P.K., Bhat S.R., Srinivasan R.;
RT "Upstream sequence of fatty acyl-CoA reductase (FAR6) of Arabidopsis
RT thaliana drives wound-inducible and stem-specific expression.";
RL Plant Cell Rep. 31:839-850(2012).
RN [9]
RP REVIEW ON ACYL-LIPID METABOLISM.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA and -ACP (acyl
CC carrier protein) substrates to fatty alcohols (PubMed:19062129,
CC PubMed:22166367). Triggers the accumulation of C16 and, to a lower
CC extent, of C18 fatty alcohols; converts palmitoyl-acyl carrier protein
CC to the corresponding C16:0 alcohol with NAD(P)H as electron donor
CC (PubMed:22166367). Triggers also the formation of some C16:0 and C18:0
CC aldehydes (PubMed:22166367). May be involved in the generation of C30
CC primary alcohol (PubMed:16980563). {ECO:0000269|PubMed:16980563,
CC ECO:0000269|PubMed:19062129, ECO:0000269|PubMed:22166367}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2
CC NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.84;
CC Evidence={ECO:0000269|PubMed:22166367};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC Evidence={ECO:0000269|PubMed:22166367};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-[ACP] + 2 NADPH = hexadecan-1-ol + holo-
CC [ACP] + 2 NADP(+); Xref=Rhea:RHEA:54328, Rhea:RHEA-COMP:9652,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78483; Evidence={ECO:0000269|PubMed:22166367};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54329;
CC Evidence={ECO:0000269|PubMed:22166367};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC Evidence={ECO:0000269|PubMed:19062129};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.48 uM for C16:0-ACP (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:22166367};
CC KM=3.36 uM for C16:0-CoA (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:22166367};
CC Vmax=293 pmol/min/mg enzyme with C16:0-ACP as substrate (at pH 7 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:22166367};
CC Vmax=357.6 pmol/min/mg enzyme with C16:0-CoA as substrate (at pH 7
CC and 30 degrees Celsius) {ECO:0000269|PubMed:22166367};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:22166367}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B9TSP7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9TSP7-2; Sequence=VSP_037568;
CC -!- TISSUE SPECIFICITY: Highly expressed in stems (PubMed:16980563,
CC PubMed:22166367, PubMed:22189440). Also present in flowers, leaves,
CC siliques, pollen and roots (PubMed:22166367, PubMed:22189440).
CC {ECO:0000269|PubMed:16980563, ECO:0000269|PubMed:22166367,
CC ECO:0000269|PubMed:22189440}.
CC -!- DEVELOPMENTAL STAGE: First observed in seedlings at rosette initiation
CC sites (PubMed:22189440). In stems, expressed in the epidermal layer and
CC the underlying few cell layers, but not in the inner cortex and
CC vascular bundles (PubMed:22166367, PubMed:22189440). In flowers,
CC observed in the epidermis, endothecium and tapetum of anthers, but not
CC in the microspores (PubMed:22166367). In siliques, accumulates in the
CC replum and receptacle (PubMed:22166367). In roots, present in emerging
CC root primordia and in the root cap throughout lateral and primary root
CC development (PubMed:22166367). Observed in pollen grains of anther
CC tissues at petal differentiation stage (PubMed:22189440).
CC {ECO:0000269|PubMed:22166367, ECO:0000269|PubMed:22189440}.
CC -!- INDUCTION: Induced by wounding in the epidermal layer of mature stem
CC internodes. {ECO:0000269|PubMed:22189440}.
CC -!- DISRUPTION PHENOTYPE: No discernible phenotypic alteration in the
CC growth and development. {ECO:0000269|PubMed:22189440}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
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DR EMBL; EU280151; ABZ10953.1; -; mRNA.
DR EMBL; EU280152; ABZ10954.1; -; mRNA.
DR EMBL; KU495933; ANP92048.1; -; mRNA.
DR EMBL; AL390921; CAC00733.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79553.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64770.1; -; Genomic_DNA.
DR EMBL; DQ056628; AAY78776.1; -; mRNA.
DR PIR; T51258; T51258.
DR RefSeq; NP_001326776.1; NM_001339805.1. [B9TSP7-1]
DR RefSeq; NP_191229.1; NM_115529.2. [B9TSP7-2]
DR AlphaFoldDB; B9TSP7; -.
DR STRING; 3702.AT3G56700.1; -.
DR PaxDb; B9TSP7; -.
DR PRIDE; B9TSP7; -.
DR ProteomicsDB; 222522; -. [B9TSP7-1]
DR EnsemblPlants; AT3G56700.1; AT3G56700.1; AT3G56700. [B9TSP7-2]
DR EnsemblPlants; AT3G56700.2; AT3G56700.2; AT3G56700. [B9TSP7-1]
DR GeneID; 824837; -.
DR Gramene; AT3G56700.1; AT3G56700.1; AT3G56700. [B9TSP7-2]
DR Gramene; AT3G56700.2; AT3G56700.2; AT3G56700. [B9TSP7-1]
DR KEGG; ath:AT3G56700; -.
DR Araport; AT3G56700; -.
DR TAIR; locus:2103575; AT3G56700.
DR eggNOG; KOG1221; Eukaryota.
DR InParanoid; B9TSP7; -.
DR OMA; LEMHEAD; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; B9TSP7; -.
DR BioCyc; ARA:AT3G56700-MON; -.
DR BRENDA; 1.2.1.42; 399.
DR BRENDA; 1.2.1.50; 399.
DR BRENDA; 1.2.1.B25; 399.
DR PRO; PR:B9TSP7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; B9TSP7; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0010345; P:suberin biosynthetic process; IBA:GO_Central.
DR CDD; cd09071; FAR_C; 1.
DR InterPro; IPR026055; FAR.
DR InterPro; IPR033640; FAR_C.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11011; PTHR11011; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Lipid biosynthesis; Lipid metabolism;
KW NADP; Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..548
FT /note="Fatty acyl-CoA reductase 6, chloroplastic"
FT /id="PRO_0000378346"
FT MOTIF 86..96
FT /note="NAD(P)H-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08891"
FT ACT_SITE 300
FT /evidence="ECO:0000250|UniProtKB:Q08891"
FT ACT_SITE 304
FT /evidence="ECO:0000250|UniProtKB:Q08891"
FT VAR_SEQ 212..232
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19062129, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.5"
FT /id="VSP_037568"
SQ SEQUENCE 548 AA; 61626 MW; F53E0BD4E8C74E9E CRC64;
MATTNVLATS HAFKLNGVSY FSSFPRKPNH YMPRRRLSHT TRRVQTSCFY GETSFEAVTS
LVTPKTETSR NSDGIGIVRF LEGKSYLVTG ATGFLAKVLI EKLLRESLEI GKIFLLMRSK
DQESANKRLY DEIISSDLFK LLKQMHGSSY EAFMKRKLIP VIGDIEEDNL GIKSEIANMI
SEEIDVIISC GGRTTFDDRY DSALSVNALG PGRLLSFGKG CRKLKLFLHF STAYVTGKRE
GTVLETPLCI GENITSDLNI KSELKLASEA VRKFRGREEI KKLKELGFER AQHYGWENSY
TFTKAIGEAV IHSKRGNLPV VIIRPSIIES SYNEPFPGWI QGTRMADPII LAYAKGQISD
FWADPQSLMD IIPVDMVANA AIAAMAKHGC GVPEFKVYNL TSSSHVNPMR AGKLIDLSHQ
HLCDFPLEET VIDLEHMKIH SSLEGFTSAL SNTIIKQERV IDNEGGGLST KGKRKLNYFV
SLAKTYEPYT FFQARFDNTN TTSLIQEMSM EEKKTFGFDI KGIDWEHYIV NVHLPGLKKE
FLSKKKTE
