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

P80030 (FABI_BRANA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 109. 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

EC=1.3.1.9
Alternative name(s):
NADH-dependent enoyl-ACP reductase
OrganismBrassica napus (Rape)
Taxonomic identifier3708 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Protein attributes

Sequence length385 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 By similarity.

Catalytic activity

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

Enzyme regulation

Inactivated by phenylglyoxal by binding covalently to two arginine residues.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer. Ref.3

Subcellular location

Plastidchloroplast Potential.

Tissue specificity

Seeds and leaves.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7373Chloroplast Ref.1 Ref.2
Chain74 – 385312Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic
PRO_0000031984

Regions

Nucleotide binding162 – 1632NAD
Nucleotide binding209 – 2102NAD
Nucleotide binding309 – 3135NAD

Sites

Active site2611Proton acceptor By similarity
Active site2711Proton acceptor By similarity
Binding site981NAD; via carbonyl oxygen
Binding site1051NAD
Binding site2591NAD; via carbonyl oxygen
Binding site2791NAD

Natural variations

Natural variant3331I → V.

Experimental info

Sequence conflict1041G → A AA sequence Ref.2
Sequence conflict1091V → I AA sequence Ref.2
Sequence conflict280 – 2812AA → N AA sequence Ref.2

Secondary structure

......................................................... 385
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80030 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: C435BCE32A8D059B

FASTA38540,479
        10         20         30         40         50         60 
MAATAAASSL QMATTRPSIS AASSKARTYV VGANPRNAYK IACTPHLSNL GCLRNDSALP 

        70         80         90        100        110        120 
ASKKSFSFST KAMSESSESK ASSGLPIDLR GKRAFIAGIA DDNGYGWAVA KSLAAAGAEI 

       130        140        150        160        170        180 
LVGTWVPALN IFETSLRRGK FDQSRVLPDG SLMEIKKVYP LDAVFDNPED VPEDVKANKR 

       190        200        210        220        230        240 
YAGSSNWTVQ EAAECVRQDF GSIDILVHSL ANGPEVSKPL LETSRKGYLA AISASSYSFV 

       250        260        270        280        290        300 
SLLSHFLPIM NPGGASISLT YIASERIIPG YGGGMSSAKA ALESDTRVLA FEAGRKQNIR 

       310        320        330        340        350        360 
VNTISAGPLG SRAAKAIGFI DTMIEYSYNN APIQKTLTAD EVGNAAAFLV SPLASAITGA 

       370        380 
TIYVDNGLNS MGVALDSPVF KDLNK 

« Hide

References

[1]"cDNA cloning and expression of Brassica napus enoyl-acyl carrier protein reductase in Escherichia coli."
Kater M.M., Koningstein G.M., Nijkamp H.J., Stuitje A.R.
Plant Mol. Biol. 17:895-909(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74-86.
Strain: cv. Rafal.
[2]"Amino acid sequence analysis of rape seed (Brassica napus) NADH-enoyl ACP reductase."
Slabas A.R., Cottingham I., Austin A., Fawcett T., Sidebottom C.M.
Plant Mol. Biol. 17:911-914(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 74-122; 146-174; 181-193; 250-295; 301-311; 316-346 AND 371-385.
Tissue: Seed.
[3]"Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase."
Rafferty J.B., Simon J.W., Baldock C., Artymiuk P.J., Baker P.J., Stuitje A.R., Slabas A.R., Rice D.W.
Structure 3:927-938(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 74-383 IN COMPLEX WITH NAD, SUBUNIT.
[4]"Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition."
Roujeinikova A., Sedelnikova S., de Boer G.J., Stuitje A.R., Slabas A.R., Rafferty J.B., Rice D.W.
J. Biol. Chem. 274:30811-30817(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 85-380 IN COMPLEX WITH NAD.
[5]"Crystallographic analysis of triclosan bound to enoyl reductase."
Roujeinikova A., Levy C.W., Rowsell S., Sedelnikova S., Baker P.J., Minshull C.A., Mistry A., Colls J.G., Camble R., Stuitje A.R., Slabas A.R., Rafferty J.B., Pauptit R.A., Viner R., Rice D.W.
J. Mol. Biol. 294:527-535(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 84-380 IN COMPLEX WITH NAD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S60064 mRNA. Translation: AAB20114.2.
PIRS17761.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWUX-ray2.50A/B85-380[»]
1D7OX-ray1.90A84-380[»]
1ENOX-ray1.90A74-383[»]
1ENPX-ray2.60A74-383[»]
ProteinModelPortalP80030.
SMRP80030. Positions 84-380.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP80030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

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

Other

EvolutionaryTraceP80030.

Entry information

Entry nameFABI_BRANA
AccessionPrimary (citable) accession number: P80030
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1994
Last modified: February 19, 2014
This is version 109 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways