STAD_ELAGV
ID STAD_ELAGV Reviewed; 393 AA.
AC O24428;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 105.
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 Elaeis guineensis var. tenera (Oil palm).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Arecaceae; Arecoideae; Cocoseae;
OC Elaeidinae; Elaeis.
OX NCBI_TaxID=51953;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mesocarp;
RA Shah F.H., Rashid O.;
RT "Nucleotide sequence of a cDNA clone encoding stearoyl-acyl-carrier-protein
RT from Elaeis guineensis var tenera.";
RL (er) Plant Gene Register PGR96-110(1996).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAB41041.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U68756; AAB41041.1; ALT_INIT; mRNA.
DR AlphaFoldDB; O24428; -.
DR SMR; O24428; -.
DR PRIDE; O24428; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000504607; Genome assembly.
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; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P22243"
FT CHAIN 32..393
FT /note="Stearoyl-[acyl-carrier-protein] 9-desaturase,
FT chloroplastic"
FT /id="PRO_0000007131"
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; 44857 MW; C6A8788B80D8A0CC CRC64;
MASMVAFRPE AFLCFSPPKT TRSTRSPRIS MASTVGPSTK VEIPKKPFMP PREVHVQVTH
SMPPQKIEIF KSLEDWAENN ILVHLKPVEK CWQPQDFLPD PSSEGFHEEV KELRERSKEI
PDGYYVCLVG DMITEEALPT YQTMLNTLDG VRDETGASLT SWAVWTRAWT AEENRHGDLL
NKYLYLSGRV DMKQIEKTIQ YLIGSGMDPR TENSPYLGFI YTSFQERATF ISHGNTARHA
KEHGDVKLAQ ICGTIASDEK RHETAYTKIV EKLFEIDPDG TVLSFADMMK KKISMPAHLM
YDGQDDNLFE HFSAVAQRLG VDTAKDYADI LEFLINRWKV GELTGFSGEG KRAQDFVCTL
APRIRRIEER AQERAKQAPR IPCSWIYGRE VQL
