ID A0A0E0KPM2_ORYPU Unreviewed; 393 AA.
AC A0A0E0KPM2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Acyl-[acyl-carrier-protein] desaturase {ECO:0000256|RuleBase:RU000582};
DE EC=1.14.19.- {ECO:0000256|RuleBase:RU000582};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC04G07990.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC04G07990.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC04G07990.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
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 AlphaFoldDB; A0A0E0KPM2; -.
DR STRING; 4537.A0A0E0KPM2; -.
DR EnsemblPlants; OPUNC04G07990.1; OPUNC04G07990.1; OPUNC04G07990.
DR Gramene; OPUNC04G07990.1; OPUNC04G07990.1; OPUNC04G07990.
DR eggNOG; ENOG502QRJK; Eukaryota.
DR HOGENOM; CLU_034505_1_1_1; -.
DR OMA; GMPNFRR; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000026962; Chromosome 4.
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; 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:SF11; 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.
DR PROSITE; PS00574; FATTY_ACID_DESATUR_2; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135
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 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 226
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"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 262
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; 44571 MW; E429D5D0685A65A3 CRC64;
MAFAASHTAS PSGAPSSCGG AQRRSNGMSP VVAMASTINR VKTAKKPYTP PREVHLQVKH
SLPPQKREIF DSLQPWAKEN LLNLLKPVEK SWQPQDFLPD PSSDGFYDEV KELRERAKEI
PDDYFVCLVG DMVTEEALPT YQTMLNTLDG VRDETGASPT TWAVWTRAWT AEENRHGDLL
NKYMYLTGRV DMKQIEKTIQ YLIGSGMDPG TENNPYLGFL YTSFQERATF ISHGNTARHA
KEYGDLKLAQ ICGTIAADEK RHETAYTKIV EKLFEIDPDY TVLAFADMMR KKISMPAHLM
YDGKDDNLFE HFSSVAQRLG VYTARDYADI LEFLVQRWKV ADLTGLSGEG RRAQDFVCTL
APRIRRLDER AQARAKQAPV IPFSWVYDRK VQL
//
