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P27582 (FABG6_BRANA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
3-oxoacyl-[acyl-carrier-protein] reductase

EC=1.1.1.100
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
OrganismBrassica napus (Rape)
Taxonomic identifier3708 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Protein attributes

Sequence length201 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer Probable.

Subcellular location

Plastidchloroplast. Note: And non-photosynthetic plastids.

Tissue specificity

Embryo and leaf tissues.

Miscellaneous

Exhibits a marked preference for acyl-carrier protein derivatives over CoA derivatives as substrates.

Sequence similarities

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

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentChloroplast
Plastid
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect 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_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2012013-oxoacyl-[acyl-carrier-protein] reductase
PRO_0000054661

Sites

Active site1081Proton acceptor By similarity
Binding site951Substrate By similarity

Experimental info

Non-adjacent residues27 – 282
Non-adjacent residues34 – 352
Non-adjacent residues62 – 632

Sequences

Sequence LengthMass (Da)Tools
P27582 [UniParc].

Last modified February 1, 1994. Version 3.
Checksum: FD51B2E369D2D967

FASTA20121,047
        10         20         30         40         50         60 
ATAQEQPEGE APDKVESPVV XXXEAXIVLV NYAREADVDA MMKDAVDYWG QIDVIANNAG 

        70         80         90        100        110        120 
ITVIALNLTG VFLCSQAATK IMMKKRKGRI INIASVVGLI GNIGQANYAA AKAGVIGFSK 

       130        140        150        160        170        180 
TAAREGASRN INVNVVCPGF IASEMTAKLG EDMEKKILGT IPLGRYGQPE DVAGLVEFLA 

       190        200 
LSPAASYITG QTFTIDGGIA I 

« Hide

References

[1]"3-oxoacyl-[ACP] reductase from oilseed rape (Brassica napus)."
Sheldon P.S., Kekwick R.G.O., Smith C.G., Sidebottom C.M., Slabas A.R.
Biochim. Biophys. Acta 1120:151-159(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-62 AND 81-84.
Tissue: Seed.
[2]"Molecular cloning of higher-plant 3-oxoacyl-(acyl carrier protein) reductase. Sequence identities with the nodG-gene product of the nitrogen-fixing soil bacterium Rhizobium meliloti."
Slabas A.R., Chase D., Nishida I., Murata N., Sidebottom C.M., Safford R., Sheldon P.S., Kekwick R.G.O., Hardie D.G., Mackintosh R.W.
Biochem. J. 283:321-326(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-201, PARTIAL PROTEIN SEQUENCE.
Tissue: Seed.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64463 mRNA. Translation: CAA45793.1.
PIRS22417.

3D structure databases

ProteinModelPortalP27582.
SMRP27582. Positions 31-201.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG6_BRANA
AccessionPrimary (citable) accession number: P27582
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1994
Last modified: February 19, 2014
This is version 92 of the entry and version 3 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