FABI_ARATH
ID FABI_ARATH Reviewed; 390 AA.
AC Q9SLA8; O04942; Q9FEF2; Q9M672;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic;
DE Short=ENR;
DE EC=1.3.1.9;
DE AltName: Full=NADH-dependent enoyl-ACP reductase 1;
DE AltName: Full=Protein MOSAIC DEATH 1;
DE Flags: Precursor;
GN Name=MOD1; Synonyms=ENR-A, ENR1; OrderedLocusNames=At2g05990;
GN ORFNames=T6P5.19;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10380806; DOI=10.1023/a:1006129924683;
RA de Boer G.J., Testerink C., Pielage G., Nijkamp H.J., Stuitje A.R.;
RT "Sequences surrounding the transcription initiation site of the Arabidopsis
RT enoyl-acyl carrier protein reductase gene control seed expression in
RT transgenic tobacco.";
RL Plant Mol. Biol. 39:1197-1207(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF THR-226.
RC STRAIN=cv. Columbia;
RX PubMed=10715326; DOI=10.2307/3870945;
RA Mou Z., He Y., Dai Y., Liu X., Li J.;
RT "Deficiency in fatty acid synthase leads to premature cell death and
RT dramatic alterations in plant morphology.";
RL Plant Cell 12:405-418(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18467464; DOI=10.1104/pp.108.118372;
RA Dayan F.E., Ferreira D., Wang Y.H., Khan I.A., McInroy J.A., Pan Z.;
RT "A pathogenic fungi diphenyl ether phytotoxin targets plant enoyl (acyl
RT carrier protein) reductase.";
RL Plant Physiol. 147:1062-1071(2008).
CC -!- FUNCTION: Catalyzes the NAD-dependent reduction of a carbon-carbon
CC double bond in an enoyl moiety that is covalently linked to an acyl
CC carrier protein (ACP). Catalyzes the last reduction step in the de novo
CC synthesis cycle of fatty acids. Involved in the elongation cycle of
CC fatty acids which are used in lipid metabolism. Required for normal
CC plant growth. {ECO:0000269|PubMed:10715326,
CC ECO:0000269|PubMed:18467464}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC -!- ACTIVITY REGULATION: Inhibited by the phytotoxin cyperin and the
CC synthetic antimicrobial compound triclosan.
CC {ECO:0000269|PubMed:18467464}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=288 uM for crotonyl-CoA {ECO:0000269|PubMed:18467464};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and siliques and at lower
CC levels in roots and leaves (at protein level).
CC {ECO:0000269|PubMed:10380806, ECO:0000269|PubMed:10715326}.
CC -!- DISRUPTION PHENOTYPE: Premature cell death in several organs, chlorotic
CC and curly leaves, semidwarfism, distorted siliques, premature
CC senescence of primary inflorescences, reduced fertility and decrease in
CC total lipid content. {ECO:0000269|PubMed:10715326}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG40070.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y13860; CAA74175.1; -; Genomic_DNA.
DR EMBL; AF207593; AAF37208.1; -; mRNA.
DR EMBL; AC005970; AAC95176.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05988.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05989.1; -; Genomic_DNA.
DR EMBL; AF324719; AAG40070.1; ALT_FRAME; mRNA.
DR EMBL; AY056192; AAL07041.1; -; mRNA.
DR EMBL; AY113962; AAM45010.1; -; mRNA.
DR PIR; H84473; H84473.
DR RefSeq; NP_565331.1; NM_126612.3.
DR RefSeq; NP_849940.1; NM_179609.1.
DR AlphaFoldDB; Q9SLA8; -.
DR SMR; Q9SLA8; -.
DR BioGRID; 551; 10.
DR IntAct; Q9SLA8; 1.
DR STRING; 3702.AT2G05990.2; -.
DR iPTMnet; Q9SLA8; -.
DR PaxDb; Q9SLA8; -.
DR PRIDE; Q9SLA8; -.
DR ProMEX; Q9SLA8; -.
DR ProteomicsDB; 231007; -.
DR EnsemblPlants; AT2G05990.1; AT2G05990.1; AT2G05990.
DR EnsemblPlants; AT2G05990.2; AT2G05990.2; AT2G05990.
DR GeneID; 815152; -.
DR Gramene; AT2G05990.1; AT2G05990.1; AT2G05990.
DR Gramene; AT2G05990.2; AT2G05990.2; AT2G05990.
DR KEGG; ath:AT2G05990; -.
DR Araport; AT2G05990; -.
DR TAIR; locus:2064681; AT2G05990.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_10_0_1; -.
DR InParanoid; Q9SLA8; -.
DR OMA; GLNIMFG; -.
DR OrthoDB; 913128at2759; -.
DR PhylomeDB; Q9SLA8; -.
DR BioCyc; ARA:AT2G05990-MON; -.
DR SABIO-RK; Q9SLA8; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9SLA8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLA8; baseline and differential.
DR Genevisible; Q9SLA8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005835; C:fatty acid synthase complex; TAS:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IGI:TAIR.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IMP:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
DR CDD; cd05372; ENR_SDR; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..74
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 75..390
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH],
FT chloroplastic"
FT /id="PRO_0000420278"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 165..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 212..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 312..316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MUTAGEN 226
FT /note="T->I: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10715326"
FT CONFLICT 24
FT /note="I -> V (in Ref. 1; CAA74175)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="N -> Y (in Ref. 1; CAA74175)"
FT /evidence="ECO:0000305"
FT CONFLICT 59..60
FT /note="HS -> NT (in Ref. 1; CAA74175)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="A -> V (in Ref. 1; CAA74175)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="V -> R (in Ref. 1; AAF37208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 41214 MW; 95E549A6E64BE5BC CRC64;
MAATAASSLQ IATRRPSMSS PSKILKAGTY IVGANPGNAS WDKLSCTRQL SNLGCLRNHS
AVPTCKRPFS FSTRAMSESS ENKAPSGLPI DLRGKRAFIA GIADDNGYGW AIAKSLAAAG
AEILVGTWVP ALNIFETSLR RGKFDQSRVL PDGSLMEIKK VYALDAVFDN PEDVPEDVKT
NKRYAGSSNW TVQEAAECVK KDFGSIDILV HSLANGPEVS KPLLETSRKG YLAAISASSY
SFVSLLRHFL PIMNPGGASI SLTYIASERI IPGYGGGMSS AKAALESDTR VLAYEAGRKS
NIRVNTISAG PLGSRAAKAI GFIDTMIEYS YNNGPIQKTL TADEVGNAAA FLASPLASAI
TGATIYVDNG LNAMGVALDS PVFKDLNSKN
