STAD_CORSA
ID STAD_CORSA Reviewed; 385 AA.
AC P32063;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Palmitoyl-[acyl-carrier-protein] 4-desaturase, chloroplastic;
DE EC=1.14.19.11 {ECO:0000269|PubMed:12232129};
DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase;
DE Flags: Precursor;
OS Coriandrum sativum (Coriander) (Chinese parsley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Coriandreae; Coriandrum.
OX NCBI_TaxID=4047;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Endosperm;
RX PubMed=1454797; DOI=10.1073/pnas.89.23.11184;
RA Cahoon E.B., Shanklin J., Ohlrogge J.B.;
RT "Expression of a coriander desaturase results in petroselinic acid
RT production in transgenic tobacco.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11184-11188(1992).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12232129; DOI=10.1104/pp.104.3.827;
RA Cahoon E.B., Ohlrogge J.B.;
RT "Metabolic evidence for the involvement of a Delta4-palmitoyl-acyl carrier
RT protein desaturase in petroselinic acid synthesis in coriander endosperm
RT and transgenic tobacco cells.";
RL Plant Physiol. 104:827-837(1994).
CC -!- FUNCTION: Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by
CC introduction of a cis double bond between carbons 4 and 5 of the acyl
CC chain. {ECO:0000269|PubMed:12232129, ECO:0000269|PubMed:1454797}.
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:0000269|PubMed:12232129};
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P22337}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid. Note=In green
CC tissue, found in chloroplasts. In non-photosynthetic tissue, found in
CC plastids.
CC -!- TISSUE SPECIFICITY: Found only in tissues which synthesize petroselinic
CC acid, such as developing seeds.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
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DR EMBL; M93115; AAC63059.1; -; mRNA.
DR PIR; A47245; A47245.
DR AlphaFoldDB; P32063; -.
DR SMR; P32063; -.
DR BioCyc; MetaCyc:MON-12587; -.
DR BRENDA; 1.14.19.11; 1619.
DR GO; GO:0009507; C:chloroplast; 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; -; 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; PTHR31155; 1.
DR Pfam; PF03405; FA_desaturase_2; 1.
DR PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00574; FATTY_ACID_DESATUR_2; 1.
PE 1: Evidence at protein 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..36
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P22243"
FT CHAIN 37..385
FT /note="Palmitoyl-[acyl-carrier-protein] 4-desaturase,
FT chloroplastic"
FT /id="PRO_0000007143"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 250
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 250
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
SQ SEQUENCE 385 AA; 43805 MW; AF7E9BFB6946EF03 CRC64;
MAMKLNALMT LQCPKRNMFT RIAPPQAGRV RSKVSMASTL HASPLVFDKL KAGRPEVDEL
FNSLEGWARD NILVHLKSVE NSWQPQDYLP DPTSDAFEDQ VKEMRERAKD IPDEYFVVLV
GDMITEEALP TYMSMLNRCD GIKDDTGAQP TSWATWTRAW TAEENRHGDL LNKYLYLSGR
VDMRMIEKTI QYLIGSGMDT KTENCPYMGF IYTSFQERAT FISHANTAKL AQHYGDKNLA
QVCGNIASDE KRHATAYTKI VEKLAEIDPD TTVIAFSDMM RKKIQMPAHA MYDGSDDMLF
KHFTAVAQQI GVYSAWDYCD IIDFLVDKWN VAKMTGLSGE GRKAQEYVCS LAAKIRRVEE
KVQGKEKKAV LPVAFSWIFN RQIII
