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Database: UniProt
Entry: H8ZQ99_9ASPA
LinkDB: H8ZQ99_9ASPA
Original site: H8ZQ99_9ASPA 
ID   H8ZQ99_9ASPA            Unreviewed;       303 AA.
AC   H8ZQ99;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
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:AFD64595.1};
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:AFD64595.1};
RN   [1] {ECO:0000313|EMBL:AFD64595.1}
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; JN413017; AFD64595.1; -; mRNA.
DR   AlphaFoldDB; H8ZQ99; -.
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   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 2.
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; 2.
DR   PIRSF; PIRSF000346; Dlt9_acylACP_des; 2.
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   NON_TER         303
FT                   /evidence="ECO:0000313|EMBL:AFD64595.1"
SQ   SEQUENCE   303 AA;  34375 MW;  D42814C709FB2965 CRC64;
     MELHLALRAS PLPAADPGRR PPPPRGNFAT NCTAAINSTH ISQEKFRSLD SWVEHNMLTF
     LKPVEKCWQP QDFLPDPSHL SAEELGDAVR EIHERAAEIP DEVWVCMVGN MVTEEALPTY
     QSLISSVLGG TVAGSTPWDR WIRGWSAEEN RHGDLLNKYL YLTGRLDMRR VEKTIQYLIG
     SGMDVGVGNS ILCGFIYTCF QEKFDGRDPR LFTHFSAVTQ KIGVYTVGDY GEMLDFFLKE
     WDISAVVDGL SPEGRRAQEY VCGLPEVMRK LAERADDHRK KLVNVGEPRY IPFSWIFNKQ
     VRV
//
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