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Reviewed, UniProtKB/Swiss-Prot P28643 (FABG_CUPLA)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic
    EC=1.1.1.100
Alternative name(s):
    3-ketoacyl-acyl carrier protein reductase
Gene names
Name: CLKR27
OrganismCuphea lanceolata
Taxonomic identifier3930 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsMyrtalesLythraceaeCuphea

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. Plastid. Note: And non-photosynthetic plastids.

Sequence similarities

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

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
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 function3-oxoacyl-[acyl-carrier-protein] reductase activity

Inferred from electronic annotation. Source: EC

NAD or NADH binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6161Chloroplast By similarity
Chain62 – 3202593-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic
PRO_0000031981

Regions

Nucleotide binding82 – 10625NADP By similarity

Sites

Active site2271Proton acceptor By similarity
Binding site2141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P28643-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 06BAF0522B2B8C87

FASTA32033,103
        10         20         30         40         50         60 
MATATAAGCS GAVALKSLGG RRLCIPQQLS PVLAGFGSHA AKSFPILSTR SIATSGIRAQ 

        70         80         90        100        110        120 
VATAEKVSAG AGQSVESPVV IVTGASRGIG KAIALSLGKA GCKVLVNYAR SSKEAEEVSK 

       130        140        150        160        170        180 
EIEAFGGQAL TFGGDVSKEE DVEAMIKTAV DAWGTVDILV NNAGITRDGL LMRMKKSQWQ 

       190        200        210        220        230        240 
EVIDLNLTGV FLCTQAAAKI MMKKKKGRII NIASVVGLVG NAGQANYSAA KAGVIGFTKT 

       250        260        270        280        290        300 
VAREYASRNI NVNAVAPGFI SSDMTSKLGD DINKKILETI PLGRYGQPEE VAGLVEFLAI 

       310        320 
NPASSYVTGQ VFTIDGGMTM 

« Hide

References

[1]"Isolation and characterization of a cDNA from Cuphea lanceolata encoding a beta-ketoacyl-ACP reductase."
Klein B., Pawlowski K., Hoericke-Grandpierre C., Schell J., Toepfer R.
Mol. Gen. Genet. 233:122-128(1992) [PubMed: 1376402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

X64566 mRNA. Translation: CAA45866.1.
PIRS22450.

3D structure databases

HSSPHSSP built from PDB template 1EDO based on UniProtKB Q93X62.
SMRP28643. Positions 77-320.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.100. 66873.

Family and domain databases

InterProIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
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.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG_CUPLA
AccessionPrimary (citable) accession number: P28643
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 59 of the entry and version 1 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

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