ID STAD3_OPHSP Reviewed; 398 AA.
AC E3PZR9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=Palmitoyl-[acyl-carrier-protein] 4-desaturase 3, chloroplastic;
DE EC=1.14.19.11;
DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase 3;
DE Flags: Precursor;
GN Name=SAD3;
OS Ophrys sphegodes (Early spider orchid) (Arachnites aranifera).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Orchidoideae; Orchideae; Orchidinae; Ophrys.
OX NCBI_TaxID=145953;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Flower;
RX PubMed=21436056; DOI=10.1073/pnas.1013313108;
RA Schlueter P.M., Xu S., Gagliardini V., Whittle E., Shanklin J.,
RA Grossniklaus U., Schiestl F.P.;
RT "Stearoyl-acyl carrier protein desaturases are associated with floral
RT isolation in sexually deceptive orchids.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5696-5701(2011).
CC -!- FUNCTION: Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by
CC introduction of a cis double bond between carbons 4 and 5 of the acyl
CC chain. {ECO:0000250|UniProtKB:Q4KN79}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (4Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:38043, Rhea:RHEA-COMP:9652, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:11488,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78483,
CC ChEBI:CHEBI:85919; EC=1.14.19.11;
CC Evidence={ECO:0000250|UniProtKB:Q4KN79};
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 stroma
CC {ECO:0000250|UniProtKB:P22337}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the flower labellum.
CC Low expression in leaves. {ECO:0000269|PubMed:21436056}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
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DR EMBL; FR688106; CBW95563.1; -; mRNA.
DR AlphaFoldDB; E3PZR9; -.
DR SMR; E3PZR9; -.
DR UniPathway; UPA00199; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
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; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Plastid; Transit peptide.
FT TRANSIT 1..29
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 30..398
FT /note="Palmitoyl-[acyl-carrier-protein] 4-desaturase 3,
FT chloroplastic"
FT /id="PRO_0000417065"
FT BINDING 139
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 177
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 177
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
SQ SEQUENCE 398 AA; 45413 MW; 59F0D542358CB1CE CRC64;
MALRSLFLPN AFPNASSFRG GSRRGAAPRA MPIVMKSNVE VGARNEIAKK PFTPPFEIHE
QITHSLPPEK IEIFKSLEGW ATDNILIHLR PVEKSWQPQD YLPDPSAESF HDQVKELRQR
SKEIPDDYFV ALVGDMITEE ALPTYQTMLN TLDGVRDETG ASLTSWAVWT RAWTAEENRH
GDLLNKYLYL TGRVDMRQIE KTIQYLIGSG MDPRTENNPY LGFIYTSFQE RATSISHGNT
ARHAKDYGDL SLAQVCGIIA SDEKRHEKAY TKIIEKLFEI DPDATVLAFA DMMKKKISMP
AHLMYDGRDD NLFKHFSSVA QRLGVYTAKD YADILEFLVE RWNVEELTGL SSEGRKAQDY
VCTLVPRIRK VDERAQGMAK KGGQTMRFSW IHDREVML
//
