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Database: UniProt
Entry: A0A0D3AG00_BRAOL
LinkDB: A0A0D3AG00_BRAOL
Original site: A0A0D3AG00_BRAOL 
ID   A0A0D3AG00_BRAOL        Unreviewed;       393 AA.
AC   A0A0D3AG00;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=stearoyl-[acyl-carrier-protein] 9-desaturase {ECO:0000256|ARBA:ARBA00012617};
DE            EC=1.14.19.2 {ECO:0000256|ARBA:ARBA00012617};
GN   Name=106294068 {ECO:0000313|EnsemblPlants:Bo1g156250.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g156250.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo1g156250.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo1g156250.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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.
CC       {ECO:0000256|ARBA:ARBA00037304}.
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:0000256|ARBA:ARBA00000991};
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   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {ECO:0000256|ARBA:ARBA00008749}.
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DR   RefSeq; XP_013585166.1; XM_013729712.1.
DR   AlphaFoldDB; A0A0D3AG00; -.
DR   STRING; 109376.A0A0D3AG00; -.
DR   EnsemblPlants; Bo1g156250.1; Bo1g156250.1; Bo1g156250.
DR   GeneID; 106294068; -.
DR   Gramene; Bo1g156250.1; Bo1g156250.1; Bo1g156250.
DR   KEGG; boe:106294068; -.
DR   eggNOG; ENOG502QRJK; Eukaryota.
DR   HOGENOM; CLU_034505_1_1_1; -.
DR   OMA; GMPNFRR; -.
DR   OrthoDB; 588486at2759; -.
DR   Proteomes; UP000032141; Chromosome C1.
DR   GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102786; F:stearoyl-[acp] desaturase activity; IEA:UniProtKB-EC.
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:SF27; STEAROYL-[ACYL-CARRIER-PROTEIN] 9-DESATURASE 5, CHLOROPLASTIC; 1.
DR   Pfam; PF03405; FA_desaturase_2; 1.
DR   PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   BINDING         134
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         172
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         172
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         175
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         225
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         258
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         258
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         261
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
SQ   SEQUENCE   393 AA;  44644 MW;  3AA0EED678F63B23 CRC64;
     MVMALNQIVV SSSSYAYRPR QARGSRSSIA SSIRSATTEV TNGRKLYIPP REVHVQVKHS
     MPPQKLEIFK SLEGWADETL LTYLKPVEKS WQPTDFLPEA ESEGFYDQVK ELRERCKELP
     DEYFVVLVGD MITEEALPTY QTMLNTLDGV RDETGASPTP WAVWTRAWTA EENRHGDLLN
     KYLYLSGRVD MRQIEKTIQY LIGSGMDPKT ENNPYLGFIY TSFQERATFI SHGNTARHAK
     DLGDLKLAQI CGTIAADEKR HETAYTKIVE KLFEIDADGT ILGLADMMKK KISMPAHLMY
     DGQDDNLFEH FSTVAQRLGV YTAKDYADIL EFLVERWNVE TLSGLSSEGH KAQDFVCGLP
     ARIRKIEERA QGRAKEAAKN VPLSWIFGRE IRA
//
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