STAD2_OPHSP
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 03-AUG-2022, entry version 37.
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; -; 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 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
