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Protein

Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.2 Publications

Catalytic activityi

Stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = oleoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O.2 Publications

Cofactori

Fe2+3 PublicationsNote: Binds 2 Fe2+ ions per subunit.3 Publications

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi138Iron 13 Publications1
Metal bindingi176Iron 13 Publications1
Metal bindingi176Iron 23 Publications1
Metal bindingi179Iron 1; via pros nitrogen3 Publications1
Metal bindingi229Iron 23 Publications1
Metal bindingi262Iron 13 Publications1
Metal bindingi262Iron 23 Publications1
Metal bindingi265Iron 2; via pros nitrogen3 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.19.2. 1204.
SABIO-RKP22337.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic (EC:1.14.19.22 Publications)
Short name:
Stearoyl-ACP desaturase
Alternative name(s):
Acyl-[acyl-carrier-protein] desaturase
Delta(9) stearoyl-acyl carrier protein desaturase
OrganismiRicinus communis (Castor bean)
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi232T → D or E: Decreases desaturase activity and increases oxidase activity. 1 Publication1
Mutagenesisi313D → K or R: Decreases Delta(9) desaturase activity and increases Delta(4) desaturase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 33ChloroplastAdd BLAST33
ChainiPRO_000000713734 – 396Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplasticAdd BLAST363

Proteomic databases

PRIDEiP22337.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

DIPiDIP-60379N.

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni67 – 69Combined sources3
Helixi70 – 75Combined sources6
Helixi77 – 83Combined sources7
Helixi85 – 87Combined sources3
Helixi91 – 93Combined sources3
Helixi97 – 100Combined sources4
Helixi109 – 121Combined sources13
Helixi125 – 139Combined sources15
Helixi141 – 148Combined sources8
Turni152 – 154Combined sources3
Beta strandi157 – 160Combined sources4
Helixi164 – 190Combined sources27
Beta strandi191 – 193Combined sources3
Helixi195 – 208Combined sources14
Helixi218 – 245Combined sources28
Helixi249 – 279Combined sources31
Helixi281 – 294Combined sources14
Turni299 – 302Combined sources4
Helixi311 – 322Combined sources12
Helixi327 – 341Combined sources15
Helixi343 – 345Combined sources3
Helixi351 – 372Combined sources22
Helixi376 – 379Combined sources4
Beta strandi383 – 385Combined sources3
Helixi387 – 389Combined sources3
Beta strandi393 – 395Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4V0JX-ray2.80A/B/C/D/E/F66-396[»]
ProteinModelPortaliP22337.
SMRiP22337.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22337.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK03921.

Family and domain databases

CDDicd01050. Acyl_ACP_Desat. 1 hit.
Gene3Di1.10.620.20. 1 hit.
InterProiIPR005803. FADS-2_CS.
IPR005067. Fatty_acid_desaturase-2.
IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
[Graphical view]
PANTHERiPTHR31155. PTHR31155. 1 hit.
PfamiPF03405. FA_desaturase_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000346. Dlt9_acylACP_des. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00574. FATTY_ACID_DESATUR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKLNPFLS QTQKLPSFAL PPMASTRSPK FYMASTLKSG SKEVENLKKP
60 70 80 90 100
FMPPREVHVQ VTHSMPPQKI EIFKSLDNWA EENILVHLKP VEKCWQPQDF
110 120 130 140 150
LPDPASDGFD EQVRELRERA KEIPDDYFVV LVGDMITEEA LPTYQTMLNT
160 170 180 190 200
LDGVRDETGA SPTSWAIWTR AWTAEENRHG DLLNKYLYLS GRVDMRQIEK
210 220 230 240 250
TIQYLIGSGM DPRTENSPYL GFIYTSFQER ATFISHGNTA RQAKEHGDIK
260 270 280 290 300
LAQICGTIAA DEKRHETAYT KIVEKLFEID PDGTVLAFAD MMRKKISMPA
310 320 330 340 350
HLMYDGRDDN LFDHFSAVAQ RLGVYTAKDY ADILEFLVGR WKVDKLTGLS
360 370 380 390
AEGQKAQDYV CRLPPRIRRL EERAQGRAKE APTMPFSWIF DRQVKL
Length:396
Mass (Da):45,371
Last modified:August 1, 1991 - v1
Checksum:iE50D4725996392AF
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59857 mRNA. Translation: AAA74692.1. Different initiation.
X56508 mRNA. Translation: CAA39859.1.
PIRiS16463. OHCSAD.
RefSeqiNP_001310659.1. NM_001323730.1.

Genome annotation databases

GeneIDi8271760.
KEGGircu:8271760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59857 mRNA. Translation: AAA74692.1. Different initiation.
X56508 mRNA. Translation: CAA39859.1.
PIRiS16463. OHCSAD.
RefSeqiNP_001310659.1. NM_001323730.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4V0JX-ray2.80A/B/C/D/E/F66-396[»]
ProteinModelPortaliP22337.
SMRiP22337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60379N.

Proteomic databases

PRIDEiP22337.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8271760.
KEGGircu:8271760.

Phylogenomic databases

KOiK03921.

Enzyme and pathway databases

UniPathwayiUPA00199.
BRENDAi1.14.19.2. 1204.
SABIO-RKP22337.

Miscellaneous databases

EvolutionaryTraceiP22337.

Family and domain databases

CDDicd01050. Acyl_ACP_Desat. 1 hit.
Gene3Di1.10.620.20. 1 hit.
InterProiIPR005803. FADS-2_CS.
IPR005067. Fatty_acid_desaturase-2.
IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
[Graphical view]
PANTHERiPTHR31155. PTHR31155. 1 hit.
PfamiPF03405. FA_desaturase_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000346. Dlt9_acylACP_des. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00574. FATTY_ACID_DESATUR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTAD_RICCO
AccessioniPrimary (citable) accession number: P22337
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 30, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.