Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic precursor

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Q9SLA8 (FABI_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic
Short name=ENR
EC=1.3.1.9

Alternative name(s):
NADH-dependent enoyl-ACP reductase 1
Protein MOSAIC DEATH 1

Gene names

Name:	MOD1
Synonyms:	ENR-A, ENR1
Ordered Locus Names:	At2g05990
ORF Names:	T6P5.19

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.2 Ref.6
Catalytic activity	Acyl-[acyl-carrier-protein] + NAD⁺ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Enzyme regulation	Inhibited by the phytotoxin cyperin and the synthetic antimicrobial compound triclosan. Ref.6
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer By similarity.
Subcellular location	Plastid › chloroplast Potential.
Tissue specificity	Expressed in flowers and siliques and at lower levels in roots and leaves (at protein level). Ref.1 Ref.2
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. Ref.2
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=288 µM for crotonyl-CoA Ref.6
Sequence caution	The sequence AAG40070.1 differs from that shown. Reason: Frameshift at position 150.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from mutant phenotype Ref.2. Source: TAIR
Cellular_component	chloroplast envelope Inferred from direct assay PubMed 12938931. Source: TAIR chloroplast stroma Inferred from direct assay PubMed 16207701 PubMed 18633119 PubMed 20061580. Source: TAIR fatty acid synthase complex Traceable author statement Ref.2. Source: TAIR thylakoid Inferred from direct assay PubMed 11826309. Source: TAIR
Molecular_function	copper ion binding Inferred from direct assay PubMed 20018591. Source: TAIR enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from electronic annotation. Source: EC enoyl-[acyl-carrier-protein] reductase activity Inferred from mutant phenotype Ref.2. Source: TAIR nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 74

Chloroplast Potential

Chain

75 – 390

316

Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic

PRO_0000420278

Regions

Nucleotide binding

165 – 166

NAD By similarity

Nucleotide binding

212 – 213

NAD By similarity

Nucleotide binding

312 – 316

NAD By similarity

Sites

Active site

264

Proton acceptor By similarity

Active site

274

Proton acceptor By similarity

Binding site

101

NAD; via carbonyl oxygen By similarity

Binding site

108

NAD By similarity

Binding site

262

NAD; via carbonyl oxygen By similarity

Binding site

282

NAD By similarity

Experimental info

Mutagenesis

226

T → I: Loss of activity. Ref.2

Sequence conflict

I → V in CAA74175. Ref.1

Sequence conflict

N → Y in CAA74175. Ref.1

Sequence conflict

59 – 60

HS → NT in CAA74175. Ref.1

Sequence conflict

234

A → V in CAA74175. Ref.1

Sequence conflict

376

V → R in AAF37208. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9SLA8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 95E549A6E64BE5BC
Show »

FASTA

390

41,214

        10         20         30         40         50         60 
MAATAASSLQ IATRRPSMSS PSKILKAGTY IVGANPGNAS WDKLSCTRQL SNLGCLRNHS 

        70         80         90        100        110        120 
AVPTCKRPFS FSTRAMSESS ENKAPSGLPI DLRGKRAFIA GIADDNGYGW AIAKSLAAAG 

       130        140        150        160        170        180 
AEILVGTWVP ALNIFETSLR RGKFDQSRVL PDGSLMEIKK VYALDAVFDN PEDVPEDVKT 

       190        200        210        220        230        240 
NKRYAGSSNW TVQEAAECVK KDFGSIDILV HSLANGPEVS KPLLETSRKG YLAAISASSY 

       250        260        270        280        290        300 
SFVSLLRHFL PIMNPGGASI SLTYIASERI IPGYGGGMSS AKAALESDTR VLAYEAGRKS 

       310        320        330        340        350        360 
NIRVNTISAG PLGSRAAKAI GFIDTMIEYS YNNGPIQKTL TADEVGNAAA FLASPLASAI 

       370        380        390 
TGATIYVDNG LNAMGVALDS PVFKDLNSKN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequences surrounding the transcription initiation site of the Arabidopsis enoyl-acyl carrier protein reductase gene control seed expression in transgenic tobacco." de Boer G.J., Testerink C., Pielage G., Nijkamp H.J., Stuitje A.R. Plant Mol. Biol. 39:1197-1207(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: cv. Landsberg erecta.
[2]	"Deficiency in fatty acid synthase leads to premature cell death and dramatic alterations in plant morphology." Mou Z., He Y., Dai Y., Liu X., Li J. Plant Cell 12:405-418(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF THR-226. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." 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. Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"A pathogenic fungi diphenyl ether phytotoxin targets plant enoyl (acyl carrier protein) reductase." Dayan F.E., Ferreira D., Wang Y.H., Khan I.A., McInroy J.A., Pan Z. Plant Physiol. 147:1062-1071(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y13860 Genomic DNA. Translation: CAA74175.1. AF207593 mRNA. Translation: AAF37208.1. AC005970 Genomic DNA. Translation: AAC95176.1. CP002685 Genomic DNA. Translation: AEC05988.1. CP002685 Genomic DNA. Translation: AEC05989.1. AF324719 mRNA. Translation: AAG40070.1. Frameshift. AY056192 mRNA. Translation: AAL07041.1. AY113962 mRNA. Translation: AAM45010.1.
IPI	IPI00527352.
PIR	H84473.
RefSeq	NP_565331.1. NM_126612.2. NP_849940.1. NM_179609.1.
UniGene	At.23842.
3D structure databases
HSSP	HSSP built from PDB template 1ENP based on UniProtKB P80030.
ProteinModelPortal	Q9SLA8.
SMR	Q9SLA8. Positions 87-383.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SLA8. 1 interaction.
STRING	3702.AT2G05990.2-P.
Proteomic databases
PRIDE	Q9SLA8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G05990.1; AT2G05990.1; AT2G05990. AT2G05990.2; AT2G05990.2; AT2G05990.
GeneID	815152.
KEGG	ath:AT2G05990.
Organism-specific databases
TAIR	At2g05990.
Phylogenomic databases
InParanoid	Q9SLA8.
KO	K00208.
OMA	LVHCLAF.
PhylomeDB	Q9SLA8.
ProtClustDB	PLN02730.
Enzyme and pathway databases
UniPathway	UPA00094.
Gene expression databases
ArrayExpress	Q9SLA8.
Genevestigator	Q9SLA8.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
PRINTS	PR00081. GDHRDH.
PROSITE	PS00061. ADH_SHORT. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FABI_ARATH

Accession

Primary (citable) accession number: Q9SLA8
Secondary accession number(s): O04942, Q9FEF2, Q9M672

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents