ID   STAD2_OPHSP             Reviewed;         376 AA.
AC   E3PZS2;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   22-FEB-2023, entry version 39.
DE   RecName: Full=Palmitoyl-[acyl-carrier-protein] 4-desaturase 2, chloroplastic;
DE            EC=1.14.19.11 {ECO:0000269|PubMed:21436056};
DE   AltName: Full=Acyl-[acyl-carrier-protein] desaturase 2;
DE   AltName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 2;
DE            Short=Stearoyl-ACP desaturase 2;
DE            EC=1.14.19.2 {ECO:0000269|PubMed:21436056};
DE   Flags: Precursor;
GN   Name=SAD2;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   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 stearoyl-ACP to oleoyl-ACP by introduction of a cis
CC       double bond between carbons 9 and 10 of the acyl chain. Converts
CC       palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis
CC       double bond between carbons 4 and 5 of the acyl chain. Catalyzes the
CC       desaturation of saturated fatty acid 18:0 and 16:0 to generate 18:1
CC       (delta-9) and 16:1 (delta-4) intermediates, expected to give rise to 9-
CC       alkenes and 12-alkenes, respectively. {ECO:0000269|PubMed:21436056}.
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:0000269|PubMed:21436056};
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:0000269|PubMed:21436056};
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       {ECO:0000269|PubMed:21436056}.
CC   -!- MISCELLANEOUS: Flowers 9-alkenes and 12-alkenes function as attractants
CC       to the pollinator Andrena nigroaenea by mimicry of the bee's sex
CC       pheromones. {ECO:0000305|PubMed:21436056}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Unusual liaisons - Issue 145
CC       of December 2012;
CC       URL="https://web.expasy.org/spotlight/back_issues/145";
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DR   EMBL; FR688109; CBW95566.1; -; mRNA.
DR   AlphaFoldDB; E3PZS2; -.
DR   SMR; E3PZS2; -.
DR   UniPathway; UPA00199; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102786; F:stearoyl-[acp] desaturase activity; IDA:UniProtKB.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
DR   CDD; cd01050; Acyl_ACP_Desat; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
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.
PE   1: Evidence at protein 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..33
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..376
FT                   /note="Palmitoyl-[acyl-carrier-protein] 4-desaturase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000417064"
FT   BINDING         114
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
SQ   SEQUENCE   376 AA;  42359 MW;  1A262105E0B6CE52 CRC64;
     MELHLALRAS PLPAADPGRR PPPPRGNFAT NCTAAINSTH ISQEKFRSLD SWVEHNMLTF
     LKPVEKCWQP QDFLPDPSHL SAEELGDAVR EIHERAAEIP DEVWVCMVGN MVTEEALPTY
     QSLISSVLGG TVAGSTPWDR WIRGWSAEEN RHGDLLNKYL YLTGRLDMRQ VEKTIQYLIG
     SGMDVGVGNS ILCGFIYTCF QEKATFISHG NTARLAKHHG DTTLAKICGL VAADEKRHAV
     AYTNLMKKLF EVAPNESMLA FAHIMRAHVT MPASRMFDGR DPRLFTHFSA VTQKIGVYTV
     RDYGEMLDFF LKEWEISAVV DDLSPEGRQA QEYVCGLPEV MGKMAERADD RRKKLVNVGE
     PRYIPFSWIF NKQVCV
//