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Database: UniProt
Entry: Q43140_SESIN
LinkDB: Q43140_SESIN
Original site: Q43140_SESIN 
ID   Q43140_SESIN            Unreviewed;       396 AA.
AC   Q43140;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   22-FEB-2023, entry version 99.
DE   RecName: Full=Acyl-[acyl-carrier-protein] desaturase {ECO:0000256|ARBA:ARBA00030374, ECO:0000256|RuleBase:RU000582};
DE            EC=1.14.19.- {ECO:0000256|RuleBase:RU000582};
OS   Sesamum indicum (Oriental sesame) (Sesamum orientale).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
OX   NCBI_TaxID=4182 {ECO:0000313|EMBL:BAA07681.1};
RN   [1] {ECO:0000313|EMBL:BAA07681.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4294 {ECO:0000313|EMBL:BAA07681.1};
RX   PubMed=8665096;
RA   Yukawa Y., Takaiwa F., Shoji K., Masuda K., Yamada K.;
RT   "Structure and expression of two seed-specific cDNA clones encoding
RT   stearoyl-acyl carrier protein desaturase from sesame, Sesamum indicum L.";
RL   Plant Cell Physiol. 37:201-205(1996).
CC   -!- FUNCTION: Introduction of a cis double bond between carbons of the acyl
CC       chain. {ECO:0000256|RuleBase:RU000582}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000346-1};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000346-1};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|RuleBase:RU000582};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|RuleBase:RU000582};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU000582}.
CC   -!- SUBCELLULAR LOCATION: Plastid {ECO:0000256|ARBA:ARBA00004474}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {ECO:0000256|ARBA:ARBA00008749, ECO:0000256|RuleBase:RU000582}.
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DR   EMBL; D42086; BAA07681.1; -; mRNA.
DR   AlphaFoldDB; Q43140; -.
DR   SMR; Q43140; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01050; Acyl_ACP_Desat; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR005803; FADS-2_CS.
DR   InterPro; IPR005067; Fatty_acid_desaturase-2.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   PANTHER; PTHR31155; ACYL- ACYL-CARRIER-PROTEIN DESATURASE-RELATED; 1.
DR   PANTHER; PTHR31155:SF9; STEAROYL-[ACYL-CARRIER-PROTEIN] 9-DESATURASE 7, CHLOROPLASTIC; 1.
DR   Pfam; PF03405; FA_desaturase_2; 1.
DR   PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00574; FATTY_ACID_DESATUR_2; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast {ECO:0000256|RuleBase:RU000582};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW   ECO:0000256|RuleBase:RU000582};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Iron {ECO:0000256|PIRSR:PIRSR000346-1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU000582};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000346-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000582}; Plastid {ECO:0000256|RuleBase:RU000582};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   BINDING         138
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         179
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         229
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         262
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         262
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
SQ   SEQUENCE   396 AA;  45168 MW;  A23475AB676A0940 CRC64;
     MALKLNAINF QSPKCPSFAL PPVASVRSPK FFMASTLRSG SKEVETVKRP FNPPREVHVQ
     VTHSMPPQKI EIFKALEDWA DNNILVHLKP VEKCWQPQDF LPDPSSDGFD DQVKELRERA
     KEIPDDYFVV LVGDMITEEA LPTYQTMLNT LDGVRDETGA SPTSWAIWTR AWTAEENRHG
     DLLNKYLYLS GRVDMRQIEK TIQYLIGSGM DPRTENSPYL GFIYTSFQER ATFISHGNTA
     RLAREHGDLK LAQICGTIAA DEKRHETAYT KIVEKLFEID PNDTVLAFAD MMRKKISMPA
     HLMYDGRDDN LFDHFSSVAQ RLGVYTAKDY ADILEHLVAR WKVANLTGLS ADGRKAQDYV
     CGLPPRIRRL EERAQGRAKQ APKIPFSWIH DREVQL
//
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