ID H9NA01_OPHAA Unreviewed; 346 AA.
AC H9NA01;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=acyl-[acyl-carrier-protein] 4-desaturase {ECO:0000256|ARBA:ARBA00012015};
DE EC=1.14.19.11 {ECO:0000256|ARBA:ARBA00012015};
DE Flags: Fragment;
GN Name=sad5 {ECO:0000313|EMBL:AFF19389.1};
OS Ophrys arachnitiformis subsp. archipelagi (Orchid) (Ophrys exaltata subsp.
OS archipelagi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Orchidoideae; Orchideae; Orchidinae; Ophrys.
OX NCBI_TaxID=884019 {ECO:0000313|EMBL:AFF19389.1};
RN [1] {ECO:0000313|EMBL:AFF19389.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22916031; DOI=10.1371/journal.pgen.1002889;
RA Xu S., Schluter P.M., Grossniklaus U., Schiestl F.P.;
RT "The genetic basis of pollinator adaptation in a sexually deceptive
RT orchid.";
RL PLoS Genet. 8:E1002889-E1002889(2012).
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:0000256|ARBA:ARBA00001006};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR000346-1};
CC Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000346-1};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000256|ARBA:ARBA00008749}.
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DR EMBL; JN412891; AFF19389.1; -; mRNA.
DR AlphaFoldDB; H9NA01; -.
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; 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 2: Evidence at transcript level;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Iron {ECO:0000256|PIRSR:PIRSR000346-1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000346-1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 209
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 209
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFF19389.1"
SQ SEQUENCE 346 AA; 39935 MW; ADEDA4CAAC5C5E1E CRC64;
HEVEGQVTHS MPPHKMEIFK SLENWAENNL LTLLKPVESS WQPHDFLPDP SLSDKFYEQT
EELRKRAKEI PDDYYVCLVG DMITEEALPT YQTVLNTFDG IRDETGASLS PWAIWTRGWT
AEENRHGDLL KQYLYLSGRV DMRQIEKTIQ YLIGCGMYIK TENSPFMGSI YTSFQERATF
ISHSNTARHA KRHGDLLLAQ ICGAIAADEK RHEGAYTRIV EKLFELDPDA AVIAFADMMR
KKIVMPAHLM FDGRDPALFD HFAAVAQRLG VYSATDYADI LEFLVGRWKV EGLAVGLSED
GKKARDFLCC LGQRYRKLEE RARGRREKQE RRSVRFSWVF NREVQV
//
