STAD_SIMCH
ID STAD_SIMCH Reviewed; 398 AA.
AC Q01753;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic;
DE Short=Stearoyl-ACP desaturase;
DE EC=1.14.19.2 {ECO:0000250|UniProtKB:P22337};
DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase;
DE Flags: Precursor;
OS Simmondsia chinensis (Jojoba) (Buxus chinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Simmondsiaceae; Simmondsia.
OX NCBI_TaxID=3999;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16668880; DOI=10.1104/pp.99.1.362;
RA Sato A., Becker C.K., Knauf V.C.;
RT "Nucleotide sequence of a complementary DNA clone encoding stearoyl-acyl
RT carrier protein desaturase from Simmondsia chinensis.";
RL Plant Physiol. 99:362-363(1992).
CC -!- FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis
CC double bond between carbons 9 and 10 of the acyl chain.
CC {ECO:0000250|UniProtKB:P22337}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:11776, Rhea:RHEA-COMP:9656, Rhea:RHEA-
CC COMP:9924, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78495,
CC ChEBI:CHEBI:78783; EC=1.14.19.2;
CC Evidence={ECO:0000250|UniProtKB:P22337};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P22337};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid. Note=In green
CC tissue, found in chloroplasts. In non-photosynthetic tissue, found in
CC plastids.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
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DR EMBL; M83199; AAA33932.1; -; mRNA.
DR AlphaFoldDB; Q01753; -.
DR SMR; Q01753; -.
DR UniPathway; UPA00199; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102786; F:stearoyl-[acp] desaturase activity; IEA:UniProtKB-EC.
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; -; 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; PTHR31155; 1.
DR Pfam; PF03405; FA_desaturase_2; 1.
DR PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00574; FATTY_ACID_DESATUR_2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Plastid; Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P22243"
FT CHAIN 35..398
FT /note="Stearoyl-[acyl-carrier-protein] 9-desaturase,
FT chloroplastic"
FT /id="PRO_0000007138"
FT REGION 46..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
SQ SEQUENCE 398 AA; 45131 MW; F3E000BB044427D8 CRC64;
MALKLHHTAF NPSMAVTSSG LPRSYHLRSH RVFMASSTIG ITSKEIPNAK KPHMPPREAH
VQKTHSMPPQ KIEIFKSLEG WAEENVLVHL KPVEKCWQPQ DFLPDPASEG FMDQVKELRE
RTKEIPDEYL VVLVGDMITE EALPTYQTML NTLDGVRDET GASLTSWAIW TRAWTAEENR
HGDLLNKYLY LTGRVDMKQI EKTIQYLIGS GMDPRSENNP YLGFIYTSFQ ERATFISHGN
TARLAKDHGD FQLAQVCGII AADEKRHETA YTKIVEKLFE IDPDGAVLAL ADMMRKKVSM
PAHLMYDGKD DNLFENYSAV AQQIGVYTAK DYADILEHLV NRWKVENLMG LSGEGHKAQD
FVCGLAPRIR KLGERAQSLS KPVSLVPFSW IFNKELKV
