STAD_SOLTU
ID STAD_SOLTU Reviewed; 393 AA.
AC P46253;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16652995; DOI=10.1104/pp.100.1.533;
RA Taylor M.A., Smith S.B., Davies H.V., Burch L.R.;
RT "The primary structure of a cDNA clone of the stearoyl-acyl carrier protein
RT desaturase gene from potato (Solanum tuberosum L.).";
RL Plant Physiol. 100:533-534(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. {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}.
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DR EMBL; M91238; AAA33839.1; -; mRNA.
DR PIR; T07653; T07653.
DR RefSeq; NP_001275198.1; NM_001288269.1.
DR AlphaFoldDB; P46253; -.
DR SMR; P46253; -.
DR STRING; 4113.PGSC0003DMT400041874; -.
DR GeneID; 102577562; -.
DR KEGG; sot:102577562; -.
DR eggNOG; ENOG502QRJK; Eukaryota.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P46253; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IBA:GO_Central.
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 GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
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; Reference proteome; 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_0000007140"
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 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; 44538 MW; 3FBCC282D57CA7FF CRC64;
MALNINGVSL KSHKMLPFPC SSARSERVFM ASTIHRPSVE VGSVKKAFTP PREVHVQVTH
SMPPEKIEVF DSLRDWAAQN LLVHLKPVEK CWQPTDFLPD PASEGFDEQV KELRERCKEI
PDDYFVVLIG DMITEEALPT YQTMINTLDG VRDETGATVT PWAIWTRAWT AEENRHGDLL
NKYLYLSGRV DMKQIEKTIQ YLIGSGMDPR TENNPYLGFV YTSLRKGVTF VSHGNTARLA
KEHGDMKLAQ ICGSIAADEK RHETAYTKIV EKLLEVDPDG AVLAIGDMMR KNISMPAHLM
YDGRDDNLFE HFSAVAQRLG VYTAKDYADI LEFHVGRWEV EKLTGLSSEG RRAQDYVCGL
APRIRKLEER AQARAKHAKS VPFSWIFGKE IKL
