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P22337

- STAD_RICCO

UniProt

P22337 - STAD_RICCO

Protein

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

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons Delta9 and Delta(10) of the acyl chain.

    Catalytic activityi

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

    Cofactori

    Binds 2 iron ions per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi138 – 1381Iron 13 Publications
    Metal bindingi176 – 1761Iron 13 Publications
    Metal bindingi176 – 1761Iron 23 Publications
    Metal bindingi179 – 1791Iron 1; via pros nitrogen3 Publications
    Metal bindingi229 – 2291Iron 23 Publications
    Metal bindingi262 – 2621Iron 13 Publications
    Metal bindingi262 – 2621Iron 23 Publications
    Metal bindingi265 – 2651Iron 2; via pros nitrogen3 Publications

    GO - Molecular functioni

    1. acyl-[acyl-carrier-protein] desaturase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Iron, Metal-binding, NADP

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    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
    OrganismiRicinus communis (Castor bean)
    Taxonomic identifieri3988 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

    Subcellular locationi

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

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi232 – 2321T → D or E: Decreases desaturase activity and increases oxidase activity. 1 Publication
    Mutagenesisi313 – 3131D → K or R: Decreases Delta(9) desaturase activity and increases Delta(4) desaturase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333ChloroplastAdd
    BLAST
    Chaini34 – 396363Acyl-[acyl-carrier-protein] desaturase, chloroplasticPRO_0000007137Add
    BLAST

    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

    1
    396
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni67 – 693
    Helixi70 – 756
    Helixi77 – 837
    Helixi85 – 873
    Helixi91 – 933
    Helixi97 – 1004
    Helixi109 – 12113
    Helixi125 – 13915
    Helixi141 – 1488
    Turni152 – 1543
    Beta strandi157 – 1604
    Helixi164 – 19027
    Beta strandi191 – 1933
    Helixi195 – 20814
    Helixi218 – 24528
    Helixi249 – 27931
    Helixi281 – 29414
    Turni299 – 3024
    Helixi311 – 32212
    Helixi327 – 34115
    Helixi343 – 3453
    Helixi351 – 37222
    Helixi376 – 3794
    Beta strandi383 – 3853
    Helixi387 – 3893
    Beta strandi393 – 3953

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP22337.
    SMRiP22337. Positions 51-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22337.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the fatty acid desaturase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KOiK03921.

    Family and domain databases

    Gene3Di1.10.620.20. 1 hit.
    InterProiIPR005067. Fatty_acid_desaturase-2.
    IPR009078. Ferritin-like_SF.
    IPR012348. RNR-rel.
    IPR005803. Stearoyl-ACP_desaturase_CS.
    [Graphical view]
    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

    MALKLNPFLS QTQKLPSFAL PPMASTRSPK FYMASTLKSG SKEVENLKKP    50
    FMPPREVHVQ VTHSMPPQKI EIFKSLDNWA EENILVHLKP VEKCWQPQDF 100
    LPDPASDGFD EQVRELRERA KEIPDDYFVV LVGDMITEEA LPTYQTMLNT 150
    LDGVRDETGA SPTSWAIWTR AWTAEENRHG DLLNKYLYLS GRVDMRQIEK 200
    TIQYLIGSGM DPRTENSPYL GFIYTSFQER ATFISHGNTA RQAKEHGDIK 250
    LAQICGTIAA DEKRHETAYT KIVEKLFEID PDGTVLAFAD MMRKKISMPA 300
    HLMYDGRDDN LFDHFSAVAQ RLGVYTAKDY ADILEFLVGR WKVDKLTGLS 350
    AEGQKAQDYV CRLPPRIRRL EERAQGRAKE APTMPFSWIF DRQVKL 396
    Length:396
    Mass (Da):45,371
    Last modified:August 1, 1991 - v1
    Checksum:iE50D4725996392AF
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59857 mRNA. Translation: AAA74692.1. Different initiation.
    X56508 mRNA. Translation: CAA39859.1.
    PIRiS16463. OHCSAD.
    RefSeqiXP_002531889.1. XM_002531843.1.

    Genome annotation databases

    GeneIDi8271760.
    KEGGircu:RCOM_1238330.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59857 mRNA. Translation: AAA74692.1 . Different initiation.
    X56508 mRNA. Translation: CAA39859.1 .
    PIRi S16463. OHCSAD.
    RefSeqi XP_002531889.1. XM_002531843.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P22337.
    SMRi P22337. Positions 51-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60379N.

    Proteomic databases

    PRIDEi P22337.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8271760.
    KEGGi rcu:RCOM_1238330.

    Phylogenomic databases

    KOi K03921.

    Enzyme and pathway databases

    UniPathwayi UPA00199 .
    BRENDAi 1.14.19.2. 1204.
    SABIO-RK P22337.

    Miscellaneous databases

    EvolutionaryTracei P22337.

    Family and domain databases

    Gene3Di 1.10.620.20. 1 hit.
    InterProi IPR005067. Fatty_acid_desaturase-2.
    IPR009078. Ferritin-like_SF.
    IPR012348. RNR-rel.
    IPR005803. Stearoyl-ACP_desaturase_CS.
    [Graphical view ]
    Pfami PF03405. FA_desaturase_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000346. Dlt9_acylACP_des. 1 hit.
    SUPFAMi SSF47240. SSF47240. 1 hit.
    PROSITEi PS00574. FATTY_ACID_DESATUR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 113 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

    External Data

    Dasty 3