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Reviewed, UniProtKB/Swiss-Prot P80030 (FABI_BRANA)

Last modified February 9, 2010. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeBrassica

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)

Catalytic activity

Acyl-[acyl-carrier-protein] + NAD+ = 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.

Subcellular location

Plastidchloroplast.

Tissue specificity

Seeds and leaves.

Sequence similarities

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

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   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-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

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

Inferred from electronic annotation. Source: 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 binding95 – 12127NAD By similarity

Sites

Active site2711Proton acceptor By similarity

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
P80030-1 [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: 1912503] [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: 1912504] [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: 8535786] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 74-382.
[4]"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: 10610777] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 84-380.
+Additional computationally mapped references.

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[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.1.9. 393.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PTHR19410:SF12. Enoyl-ACP_rdct. 1 hit.
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

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 9, 2010
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents