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P22337 (STAD_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 110. 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:
Acyl-[acyl-carrier-protein] desaturase, chloroplastic

EC=1.14.19.2
Alternative name(s):
Delta(9) stearoyl-acyl carrier protein desaturase
Stearoyl-ACP desaturase
OrganismRicinus communis (Castor bean)
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons Delta9 and Delta10 of the acyl chain.

Catalytic activity

Stearoyl-[acyl-carrier-protein] + reduced acceptor + O2 = oleoyl-[acyl-carrier-protein] + acceptor + 2 H2O. Ref.5 Ref.6

Cofactor

Binds 2 iron ions per subunit.

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Homodimer.

Subcellular location

Plastidchloroplast. Plastid. Note: In green tissue, found in chloroplasts. In non-photosynthetic tissue, found in plastids.

Tissue specificity

Higher levels in developing seeds than in leaf and root tissues.

Sequence similarities

Belongs to the fatty acid desaturase family.

Sequence caution

The sequence AAA74692.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandIron
Metal-binding
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacyl-[acyl-carrier-protein] desaturase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Chloroplast
Chain34 – 396363Acyl-[acyl-carrier-protein] desaturase, chloroplastic
PRO_0000007137

Sites

Metal binding1381Iron 1
Metal binding1761Iron 1
Metal binding1761Iron 2
Metal binding1791Iron 1; via pros nitrogen
Metal binding2291Iron 2
Metal binding2621Iron 1
Metal binding2621Iron 2
Metal binding2651Iron 2; via pros nitrogen

Experimental info

Mutagenesis2321T → D or E: Decreases desaturase activity and increases oxidase activity. Ref.5
Mutagenesis3131D → K or R: Decreases Delta(9) desaturase activity and increases Delta(4) desaturase activity. Ref.6

Secondary structure

................................................... 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22337 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: E50D4725996392AF

FASTA39645,371
        10         20         30         40         50         60 
MALKLNPFLS QTQKLPSFAL PPMASTRSPK FYMASTLKSG SKEVENLKKP FMPPREVHVQ 

        70         80         90        100        110        120 
VTHSMPPQKI EIFKSLDNWA EENILVHLKP VEKCWQPQDF LPDPASDGFD EQVRELRERA 

       130        140        150        160        170        180 
KEIPDDYFVV LVGDMITEEA LPTYQTMLNT LDGVRDETGA SPTSWAIWTR AWTAEENRHG 

       190        200        210        220        230        240 
DLLNKYLYLS GRVDMRQIEK TIQYLIGSGM DPRTENSPYL GFIYTSFQER ATFISHGNTA 

       250        260        270        280        290        300 
RQAKEHGDIK LAQICGTIAA DEKRHETAYT KIVEKLFEID PDGTVLAFAD MMRKKISMPA 

       310        320        330        340        350        360 
HLMYDGRDDN LFDHFSAVAQ RLGVYTAKDY ADILEFLVGR WKVDKLTGLS AEGQKAQDYV 

       370        380        390 
CRLPPRIRRL EERAQGRAKE APTMPFSWIF DRQVKL 

« Hide

References

[1]"Stearoyl-acyl-carrier-protein desaturase from higher plants is structurally unrelated to the animal and fungal homologs."
Shanklin J., Somerville C.R.
Proc. Natl. Acad. Sci. U.S.A. 88:2510-2514(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of a complementary DNA clone encoding stearoyl-acyl carrier protein desaturase from castor bean, Ricinus communis."
Knutzon D.S., Scherer D.E., Schreckengost W.E.
Plant Physiol. 96:344-345(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endosperm.
[3]"Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins."
Lindqvist Y., Huang W., Schneider G., Shanklin J.
EMBO J. 15:4081-4092(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 52-396 IN COMPLEX WITH IRON.
[4]"Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediates."
Moche M., Shanklin J., Ghoshal A., Lindqvist Y.
J. Biol. Chem. 278:25072-25080(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 34-396 IN COMPLEX WITH IRON.
[5]"A single mutation in the castor Delta9-18:0-desaturase changes reaction partitioning from desaturation to oxidase chemistry."
Guy J.E., Abreu I.A., Moche M., Lindqvist Y., Whittle E., Shanklin J.
Proc. Natl. Acad. Sci. U.S.A. 103:17220-17224(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 34-396 IN COMPLEX WITH IRON, MUTAGENESIS OF THR-232, CATALYTIC ACTIVITY.
[6]"Remote control of regioselectivity in acyl-acyl carrier protein-desaturases."
Guy J.E., Whittle E., Moche M., Lengqvist J., Lindqvist Y., Shanklin J.
Proc. Natl. Acad. Sci. U.S.A. 108:16594-16599(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 34-396, MUTAGENESIS OF ASP-313, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59857 mRNA. Translation: AAA74692.1. Different initiation.
X56508 mRNA. Translation: CAA39859.1.
PIROHCSAD. S16463.
RefSeqXP_002531889.1. XM_002531843.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFRX-ray2.40A/B/C/D/E/F52-396[»]
1OQ4X-ray2.40A/B/C/D/E/F34-396[»]
1OQ7X-ray3.20A/B/C/D/E/F34-396[»]
1OQ9X-ray2.40A34-396[»]
1OQBX-ray2.80A/B/C/D/E/F34-396[»]
2J2FX-ray2.65A/B/C/D/E/F34-396[»]
2XZ0X-ray3.00A/B/C34-396[»]
2XZ1X-ray3.35A/B34-396[»]
ProteinModelPortalP22337.
SMRP22337. Positions 51-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60379N.

Proteomic databases

PRIDEP22337.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8271760.
KEGGrcu:RCOM_1238330.

Phylogenomic databases

KOK03921.
ProtClustDBPLN00179.

Enzyme and pathway databases

BRENDA1.14.19.2. 1204.
SABIO-RKP22337.
UniPathwayUPA00199.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR005067. Fatty_acid_desaturase-2.
IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR005803. Stearoyl-ACP_desaturase_CS.
[Graphical view]
PfamPF03405. FA_desaturase_2. 1 hit.
[Graphical view]
PIRSFPIRSF000346. Dlt9_acylACP_des. 1 hit.
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00574. FATTY_ACID_DESATUR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22337.

Entry information

Entry nameSTAD_RICCO
AccessionPrimary (citable) accession number: P22337
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: February 19, 2014
This is version 110 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways