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   27-MAR-2024, entry version 150.
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=10.1105/tpc.12.3.405;
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.Q9SLA8; -.
DR   iPTMnet; Q9SLA8; -.
DR   PaxDb; 3702-AT2G05990-2; -.
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; AT2G05990; MOD1.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_10_0_1; -.
DR   InParanoid; Q9SLA8; -.
DR   OMA; GTMFTMS; -.
DR   OrthoDB; 5485040at2759; -.
DR   PhylomeDB; Q9SLA8; -.
DR   BioCyc; ARA:AT2G05990-MONOMER; -.
DR   SABIO-RK; Q9SLA8; -.
DR   UniPathway; UPA00094; -.
DR   PRO; PR:Q9SLA8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SLA8; baseline and differential.
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   Gene3D; 1.10.8.400; Enoyl acyl carrier protein reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR   PANTHER; PTHR43159:SF6; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH], CHLOROPLASTIC; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; Q9SLA8; AT.
PE   1: Evidence at protein level;
KW   Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; NADP; 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        239
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   ACT_SITE        282
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   BINDING         53
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT   BINDING         170
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   BINDING         282
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   BINDING         314
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:L0E2Z4"
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
//