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Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic (ENR) (EC 1.3.1.9) (NADH-dependent enoyl-ACP reductase 1) (Protein MOSAIC DEATH 1)

 FABI_ARATH              Reviewed;         390 AA.
Q9SLA8; O04942; Q9FEF2; Q9M672;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-DEC-2017, entry version 121.
RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic;
Short=ENR;
EC=1.3.1.9;
AltName: Full=NADH-dependent enoyl-ACP reductase 1;
AltName: Full=Protein MOSAIC DEATH 1;
Flags: Precursor;
Name=MOD1; Synonyms=ENR-A, ENR1; OrderedLocusNames=At2g05990;
ORFNames=T6P5.19;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Landsberg erecta;
PubMed=10380806; DOI=10.1023/A:1006129924683;
de Boer G.J., Testerink C., Pielage G., Nijkamp H.J., Stuitje A.R.;
"Sequences surrounding the transcription initiation site of the
Arabidopsis enoyl-acyl carrier protein reductase gene control seed
expression in transgenic tobacco.";
Plant Mol. Biol. 39:1197-1207(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF THR-226.
STRAIN=cv. Columbia;
PubMed=10715326; DOI=10.1105/tpc.12.3.405;
Mou Z., He Y., Dai Y., Liu X., Li J.;
"Deficiency in fatty acid synthase leads to premature cell death and
dramatic alterations in plant morphology.";
Plant Cell 12:405-418(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18467464; DOI=10.1104/pp.108.118372;
Dayan F.E., Ferreira D., Wang Y.H., Khan I.A., McInroy J.A., Pan Z.;
"A pathogenic fungi diphenyl ether phytotoxin targets plant enoyl
(acyl carrier protein) reductase.";
Plant Physiol. 147:1062-1071(2008).
-!- FUNCTION: Catalyzes the NAD-dependent reduction of a carbon-carbon
double bond in an enoyl moiety that is covalently linked to an
acyl carrier protein (ACP). Catalyzes the last reduction step in
the de novo synthesis cycle of fatty acids. Involved in the
elongation cycle of fatty acids which are used in lipid
metabolism. Required for normal plant growth.
{ECO:0000269|PubMed:10715326, ECO:0000269|PubMed:18467464}.
-!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
-!- ENZYME REGULATION: Inhibited by the phytotoxin cyperin and the
synthetic antimicrobial compound triclosan.
{ECO:0000269|PubMed:18467464}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=288 uM for crotonyl-CoA {ECO:0000269|PubMed:18467464};
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in flowers and siliques and at lower
levels in roots and leaves (at protein level).
{ECO:0000269|PubMed:10380806, ECO:0000269|PubMed:10715326}.
-!- DISRUPTION PHENOTYPE: Premature cell death in several organs,
chlorotic and curly leaves, semidwarfism, distorted siliques,
premature senescence of primary inflorescences, reduced fertility
and decrease in total lipid content.
{ECO:0000269|PubMed:10715326}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. FabI subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG40070.1; Type=Frameshift; Positions=150; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Y13860; CAA74175.1; -; Genomic_DNA.
EMBL; AF207593; AAF37208.1; -; mRNA.
EMBL; AC005970; AAC95176.1; -; Genomic_DNA.
EMBL; CP002685; AEC05988.1; -; Genomic_DNA.
EMBL; CP002685; AEC05989.1; -; Genomic_DNA.
EMBL; AF324719; AAG40070.1; ALT_FRAME; mRNA.
EMBL; AY056192; AAL07041.1; -; mRNA.
EMBL; AY113962; AAM45010.1; -; mRNA.
PIR; H84473; H84473.
RefSeq; NP_565331.1; NM_126612.3.
RefSeq; NP_849940.1; NM_179609.1.
UniGene; At.23842; -.
ProteinModelPortal; Q9SLA8; -.
SMR; Q9SLA8; -.
BioGrid; 551; 1.
IntAct; Q9SLA8; 1.
STRING; 3702.AT2G05990.1; -.
iPTMnet; Q9SLA8; -.
PaxDb; Q9SLA8; -.
PRIDE; Q9SLA8; -.
ProMEX; Q9SLA8; -.
EnsemblPlants; AT2G05990.1; AT2G05990.1; AT2G05990.
EnsemblPlants; AT2G05990.2; AT2G05990.2; AT2G05990.
GeneID; 815152; -.
Gramene; AT2G05990.1; AT2G05990.1; AT2G05990.
Gramene; AT2G05990.2; AT2G05990.2; AT2G05990.
KEGG; ath:AT2G05990; -.
Araport; AT2G05990; -.
TAIR; locus:2064681; AT2G05990.
eggNOG; ENOG410IQSQ; Eukaryota.
eggNOG; COG0623; LUCA.
InParanoid; Q9SLA8; -.
KO; K00208; -.
OMA; SVATAMH; -.
OrthoDB; EOG09360GOD; -.
PhylomeDB; Q9SLA8; -.
BioCyc; ARA:AT2G05990-MONOMER; -.
UniPathway; UPA00094; -.
PRO; PR:Q9SLA8; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9SLA8; baseline and differential.
Genevisible; Q9SLA8; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005835; C:fatty acid synthase complex; TAS:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IMP:TAIR.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NAD;
Oxidoreductase; Plastid; Reference proteome; Transit peptide.
TRANSIT 1 74 Chloroplast. {ECO:0000255}.
CHAIN 75 390 Enoyl-[acyl-carrier-protein] reductase
[NADH], chloroplastic.
/FTId=PRO_0000420278.
NP_BIND 165 166 NAD. {ECO:0000250}.
NP_BIND 212 213 NAD. {ECO:0000250}.
NP_BIND 312 316 NAD. {ECO:0000250}.
ACT_SITE 264 264 Proton acceptor. {ECO:0000250}.
ACT_SITE 274 274 Proton acceptor. {ECO:0000250}.
BINDING 101 101 NAD; via carbonyl oxygen. {ECO:0000250}.
BINDING 108 108 NAD. {ECO:0000250}.
BINDING 262 262 NAD; via carbonyl oxygen. {ECO:0000250}.
BINDING 282 282 NAD. {ECO:0000250}.
MUTAGEN 226 226 T->I: Loss of activity.
{ECO:0000269|PubMed:10715326}.
CONFLICT 24 24 I -> V (in Ref. 1; CAA74175).
{ECO:0000305}.
CONFLICT 35 35 N -> Y (in Ref. 1; CAA74175).
{ECO:0000305}.
CONFLICT 59 60 HS -> NT (in Ref. 1; CAA74175).
{ECO:0000305}.
CONFLICT 234 234 A -> V (in Ref. 1; CAA74175).
{ECO:0000305}.
CONFLICT 376 376 V -> R (in Ref. 1; AAF37208).
{ECO:0000305}.
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


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