Acyl-[acyl-carrier-protein] desaturase, chloroplastic precursor

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P22337 (STAD_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended 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
Organism	Ricinus communis (Castor bean) [Complete proteome]
Taxonomic identifier	3988 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast. 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 process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Iron Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acyl-[acyl-carrier-protein] desaturase activity Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 33

Chloroplast

Chain

34 – 396

363

Acyl-[acyl-carrier-protein] desaturase, chloroplastic

PRO_0000007137

Sites

Metal binding

138

Iron 1

Metal binding

176

Iron 1

Metal binding

176

Iron 2

Metal binding

179

Iron 1; via pros nitrogen

Metal binding

229

Iron 2

Metal binding

262

Iron 1

Metal binding

262

Iron 2

Metal binding

265

Iron 2; via pros nitrogen

Experimental info

Mutagenesis

232

T → D or E: Decreases desaturase activity and increases oxidase activity. Ref.5

Mutagenesis

313

D → 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

Length

Mass (Da)

Tools

P22337 [UniParc].

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

396

45,371

        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.

PIR

OHCSAD. S16463.

RefSeq

XP_002531889.1. XM_002531843.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AFR	X-ray	2.40	A/B/C/D/E/F	52-396	[»]
1OQ4	X-ray	2.40	A/B/C/D/E/F	34-396	[»]
1OQ7	X-ray	3.20	A/B/C/D/E/F	34-396	[»]
1OQ9	X-ray	2.40	A	34-396	[»]
1OQB	X-ray	2.80	A/B/C/D/E/F	34-396	[»]
2J2F	X-ray	2.65	A/B/C/D/E/F	34-396	[»]
2XZ0	X-ray	3.00	A/B/C	34-396	[»]
2XZ1	X-ray	3.35	A/B	34-396	[»]

ProteinModelPortal

P22337.

SMR

P22337. Positions 51-396.

ModBase

Search...

Proteomic databases

PRIDE

P22337.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

8271760.

KEGG

rcu:RCOM_1238330.

Phylogenomic databases

K03921.

ProtClustDB

PLN00179.

Enzyme and pathway databases

BRENDA

1.14.19.2. 1204.

SABIO-RK

P22337.

UniPathway

UPA00199.

Family and domain databases

Gene3D

1.10.620.20. 1 hit.

InterPro

IPR005067. Fatty_acid_desaturase-2.
IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR005803. Stearoyl-ACP_desaturase_CS.
[Graphical view]

Pfam

PF03405. FA_desaturase_2. 1 hit.
[Graphical view]

PIRSF

PIRSF000346. Dlt9_acylACP_des. 1 hit.

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

PROSITE

PS00574. FATTY_ACID_DESATUR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22337.

Entry information

Entry name

STAD_RICCO

Accession

Primary (citable) accession number: P22337

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents