STAD_SOLCO
ID STAD_SOLCO Reviewed; 393 AA.
AC Q41319;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
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 Solanum commersonii (Commerson's wild potato) (Commerson's nightshade).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4109;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Trucci M., Grillo S., Costa A., Leone A.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:P22337}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:P22337}. Plastid {ECO:0000250|UniProtKB:P22337}.
CC Note=In green tissue, found in chloroplasts. In non-photosynthetic
CC tissue, found in plastids.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X78935; CAA55535.2; -; mRNA.
DR PIR; S44202; S44202.
DR AlphaFoldDB; Q41319; -.
DR SMR; Q41319; -.
DR PRIDE; Q41319; -.
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; 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.
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..30
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P22243"
FT CHAIN 31..393
FT /note="Stearoyl-[acyl-carrier-protein] 9-desaturase,
FT chloroplastic"
FT /id="PRO_0000007139"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
SQ SEQUENCE 393 AA; 44833 MW; 111E5F801E2B82DD CRC64;
MALNFNSPTF QSIKTTRRPC SPLRSPRVFM ASTLRPPSVE DGNVKKPFSP PREVHVQVTH
SMPPEKREIF DSLHGWADNN ILVHLKPVEK CWQASDFLPD PASEGFEDQV KELRERCKEI
PDDYFVVLVG DMITEEALPT YQTMLNTLDG VRDETGASLT PWAIWTRAWT AEENRHGDLL
NKYLYLSGRV DMRQIEKTIQ YLIGSGMDPR TENNPYLGFI YTSFQERATF ISHGNTARHA
KEHGDMKLAQ VCGIIAADEK RHETAYTKIV EKLFEVDPDG TVLAVADMMR KKISMPAHLM
YDGRDDNLFE HFSTVAQRLG VYTAKDYADI LEFLVGRWEI EKLTGLSGEG HKARDYVCGL
APRIRKLEER AQARAKQKAP VPFSWVFGKD IKL
