Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9SLA8 (FABI_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

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. Ref.6

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Subcellular location

Plastidchloroplast 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:

KM=288 µM for crotonyl-CoA Ref.6

Sequence caution

The sequence AAG40070.1 differs from that shown. Reason: Frameshift at position 150.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7474Chloroplast Potential
Chain75 – 390316Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic
PRO_0000420278

Regions

Nucleotide binding165 – 1662NAD By similarity
Nucleotide binding212 – 2132NAD By similarity
Nucleotide binding312 – 3165NAD By similarity

Sites

Active site2641Proton acceptor By similarity
Active site2741Proton acceptor By similarity
Binding site1011NAD; via carbonyl oxygen By similarity
Binding site1081NAD By similarity
Binding site2621NAD; via carbonyl oxygen By similarity
Binding site2821NAD By similarity

Experimental info

Mutagenesis2261T → I: Loss of activity. Ref.2
Sequence conflict241I → V in CAA74175. Ref.1
Sequence conflict351N → Y in CAA74175. Ref.1
Sequence conflict59 – 602HS → NT in CAA74175. Ref.1
Sequence conflict2341A → V in CAA74175. Ref.1
Sequence conflict3761V → R in AAF37208. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9SLA8 [UniParc].

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

FASTA39041,214
        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' 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. expand/collapse author list , 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.
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. expand/collapse author list , 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.
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.
PIRH84473.
RefSeqNP_565331.1. NM_126612.2.
NP_849940.1. NM_179609.1.
UniGeneAt.23842.

3D structure databases

ProteinModelPortalQ9SLA8.
SMRQ9SLA8. Positions 87-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9SLA8. 1 interaction.
STRING3702.AT2G05990.2-P.

Proteomic databases

PRIDEQ9SLA8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G05990.1; AT2G05990.1; AT2G05990.
AT2G05990.2; AT2G05990.2; AT2G05990.
GeneID815152.
KEGGath:AT2G05990.

Organism-specific databases

TAIRAT2G05990.

Phylogenomic databases

InParanoidQ9SLA8.
KOK00208.
OMATGEIHHV.
PhylomeDBQ9SLA8.

Enzyme and pathway databases

BioCycARA:AT2G05990-MONOMER.
ARA:GQT-2200-MONOMER.
UniPathwayUPA00094.

Gene expression databases

GenevestigatorQ9SLA8.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Entry information

Entry nameFABI_ARATH
AccessionPrimary (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: May 14, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names