ID STADS_BRANA Reviewed; 399 AA. AC Q01771; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 22-FEB-2023, entry version 113. DE RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase, seed specific, chloroplastic; DE Short=Stearoyl-ACP desaturase; DE EC=1.14.19.2; DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase; DE Flags: Precursor; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Jet neuf; TISSUE=Embryo; RX PubMed=1515603; DOI=10.1007/bf00029157; RA Slocombe S.P., Cummins I., Jarvis R.P., Murphy D.J.; RT "Nucleotide sequence and temporal regulation of a seed-specific Brassica RT napus cDNA encoding a stearoyl-acyl carrier protein (ACP) desaturase."; RL Plant Mol. Biol. 20:151-155(1992). CC -!- FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis CC double bond between carbons Delta(9) and Delta(10) of the acyl chain. 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:0000250|UniProtKB:P22337}; 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 {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Developing seeds. CC -!- DEVELOPMENTAL STAGE: Induced by 25 days after anthesis (dAA), peaking CC at 45 dAA but decreasing considerably thereafter. CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X63364; CAA44964.1; -; mRNA. DR PIR; S24995; S24995. DR AlphaFoldDB; Q01771; -. DR SMR; Q01771; -. DR UniPathway; UPA00199; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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; IPR005803; FADS-2_CS. 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:SF37; ACYL-[ACYL-CARRIER-PROTEIN] DESATURASE; 1. DR Pfam; PF03405; FA_desaturase_2; 1. DR PIRSF; PIRSF000346; Dlt9_acylACP_des; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00574; FATTY_ACID_DESATUR_2; 1. PE 2: Evidence at transcript 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..34 FT /note="Chloroplast" FT /evidence="ECO:0000250|UniProtKB:P22243" FT CHAIN 35..399 FT /note="Stearoyl-[acyl-carrier-protein] 9-desaturase, seed FT specific, chloroplastic" FT /id="PRO_0000007128" FT BINDING 141 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P22337" FT BINDING 179 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P22337" FT BINDING 179 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P22337" FT BINDING 182 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P22337" FT BINDING 232 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P22337" FT BINDING 265 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P22337" FT BINDING 265 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P22337" FT BINDING 268 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P22337" SQ SEQUENCE 399 AA; 45359 MW; 8537254C13D9AF80 CRC64; MALKFNPLVS QPYKLASSAR PPVSTFRSPK FLCLASSSSP ALSSKEVESL KKPFTPPREV HLQVLHSMPP QKIEIFKSME DRAEQNLLPH LKDVEKSWQP QDFLPDPASD GFEDQVKELR ERARELPDDY FVVLVGDMIT EEALPTYQTM LNTLDGVRDE TGASPTSWAV WTRAWTAEEN RHGDLLNKYL YLSGRVDMRQ IEKTIQYLIG SGMDPRTENN PYLGFIYTSF QERATFVSHG NTARQAKEHG DLKLAQICGT IAADEKRHET AYTKIVEKLL EIDPDGTVVA FADMMRKKIS MPAHLMYDGR DDNLFDNFSS VAQRLGVYTA KDYADILEFL AGRWRIESLT GLSGEGNKAQ EYLCGLTPRI RRLDERAQAR AKKGPKIPFS WIHDREVQL //