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Database: UniProt
Entry: H8ZQ97_9ASPA
LinkDB: H8ZQ97_9ASPA
Original site: H8ZQ97_9ASPA 
ID   H8ZQ97_9ASPA            Unreviewed;       376 AA.
AC   H8ZQ97;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=sad2 {ECO:0000313|EMBL:AFD64593.1};
OS   Ophrys garganica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Orchidoideae; Orchideae; Orchidinae; Ophrys.
OX   NCBI_TaxID=145943 {ECO:0000313|EMBL:AFD64593.1};
RN   [1] {ECO:0000313|EMBL:AFD64593.1}
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; JN413008; AFD64587.1; -; mRNA.
DR   EMBL; JN413014; AFD64593.1; -; mRNA.
DR   AlphaFoldDB; H8ZQ97; -.
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         114
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   NON_TER         376
FT                   /evidence="ECO:0000313|EMBL:AFD64593.1"
SQ   SEQUENCE   376 AA;  42445 MW;  D15493293BCA5D1A CRC64;
     MELHLALRAS PLPAADPGRR PPPPRGNFAT NCTAAINSTH ISQEKFRSLD SWVEHNMLTF
     LKPVEKCWQP QDFLPDPSHL SAEELGDAVR EIHERAAEIP DEVWVCMVGN MVTEEALPTY
     QSLISSILGG TVAGSTPWDR WIRGWSAEEN RHGDLLNKYL YLTGRLDMRQ VEKTIQYLIG
     SGMDVGVGNS ILCGFIYTCF QEKATFISHG NTARLAKHHG DTTLAKICGL VAADEKRHAV
     AYTNLMKKLF EVAPNESMLA FAHIMRAHVT MPASRMFDGR DPRLFTHFSA VTQKIGVYTV
     RDYGEMLDFF LKEWDISAVV DGLSPEGRRA QEYVCGLPEV MRKLAERADD HRKKLVNVGE
     PRYIPFSWIF NKQVRV
//
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