ID C0P3R9_MAIZE Unreviewed; 391 AA.
AC C0P3R9;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 22-FEB-2023, entry version 81.
DE RecName: Full=Acyl-[acyl-carrier-protein] desaturase {ECO:0000256|RuleBase:RU000582};
DE EC=1.14.19.- {ECO:0000256|RuleBase:RU000582};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACN27635.1};
RN [1] {ECO:0000313|EMBL:ACN27635.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACN27635.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
CC -!- FUNCTION: Introduction of a cis double bond between carbons of the acyl
CC chain. {ECO:0000256|RuleBase:RU000582}.
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|RuleBase:RU000582};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|RuleBase:RU000582};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU000582}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000256|ARBA:ARBA00008749, ECO:0000256|RuleBase:RU000582}.
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DR EMBL; BT062938; ACN27635.1; -; mRNA.
DR EMBL; BT063807; ACN28504.1; -; mRNA.
DR EMBL; BT067612; ACN34509.1; -; mRNA.
DR RefSeq; NP_001140670.1; NM_001147198.1.
DR AlphaFoldDB; C0P3R9; -.
DR GeneID; 100272745; -.
DR KEGG; zma:100272745; -.
DR OrthoDB; 588486at2759; -.
DR UniPathway; UPA00199; -.
DR ExpressionAtlas; C0P3R9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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; 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:SF8; ACYL-[ACYL-CARRIER-PROTEIN] DESATURASE 3, CHLOROPLASTIC; 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 {ECO:0000256|RuleBase:RU000582};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU000582};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Iron {ECO:0000256|PIRSR:PIRSR000346-1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU000582};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000346-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000582}; Plastid {ECO:0000256|RuleBase:RU000582};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
SQ SEQUENCE 391 AA; 44417 MW; 690D550FDD985F1D CRC64;
MAVAAFPSCG AFAPPCLVST RRAFSSVVAM ASAAPVRAPS RKPFAPPREV HRPVAHSLPP
QKREIFESLE SWAADNILVL LKPVERSWQP QDYLPDAASE SFDDEVRELR ERAREIPDDY
FVCFVGDMVT EEALPTYQTM LNTLDGGVRD ETGASSTSWA VWTRAWAAEE NRHGDLMNKY
LFLTGRVDMR QIEKTVQYLI ASGMDPKTET NPYMGFVYTS FQERATFISH GNTARHARRY
GDTKLAQICG TIAADEKRHE SAYERIVEKL FEVDPDYTVR AFADTMRKKV AMPAHLMYDG
QDDGLFARFS AVAQRIGVYT ARDYVDILEF LVRRWGVQEL TGLSGEGRRA QEFVCELGPR
FRRLEERAHD NKAKDPEFAP FSWIHGRQVQ L
//
