STAD_CUCSA
ID STAD_CUCSA Reviewed; 396 AA.
AC P32061;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Acyl-[acyl-carrier-protein] desaturase, chloroplastic;
DE EC=1.14.19.-;
DE Flags: Precursor;
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling cotyledon;
RX PubMed=16668411; DOI=10.1104/pp.97.1.467;
RA Shanklin J., Mullins C., Somerville C.R.;
RT "Sequence of a complementary DNA from Cucumis sativus L. encoding the
RT stearoyl-acyl-carrier protein desaturase.";
RL Plant Physiol. 97:467-468(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2006187; DOI=10.1073/pnas.88.6.2510;
RA Shanklin J., Somerville C.R.;
RT "Stearoyl-acyl-carrier-protein desaturase from higher plants is
RT structurally unrelated to the animal and fungal homologs.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2510-2514(1991).
CC -!- FUNCTION: Introduces a cis double bond in the acyl chain of an acyl-
CC [acyl-carrier protein]. {ECO:0000305}.
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. Plastid. Note=In green
CC tissue, found in chloroplasts. In non-photosynthetic tissue, found in
CC plastids.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
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DR EMBL; M59858; AAA33130.1; -; mRNA.
DR PIR; B39170; B39170.
DR RefSeq; NP_001267709.1; NM_001280780.1.
DR AlphaFoldDB; P32061; -.
DR SMR; P32061; -.
DR STRING; 3659.XP_004142937.1; -.
DR PRIDE; P32061; -.
DR GeneID; 101220831; -.
DR KEGG; csv:101220831; -.
DR eggNOG; ENOG502QRJK; Eukaryota.
DR UniPathway; UPA00199; -.
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 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..33
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P22243"
FT CHAIN 34..396
FT /note="Acyl-[acyl-carrier-protein] desaturase,
FT chloroplastic"
FT /id="PRO_0000007130"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
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 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 262
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="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT CONFLICT 114
FT /note="R -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="E -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45583 MW; 2E19E894C106D4C8 CRC64;
MALKFHPLTS QSPKLPSFRM PQLASLRSPK FVMASTLRST SREVETLKKP FMPPREVHLQ
VTHSMPPQKM EIFKSLEDWA EENLLVHLKP VERCWQPQDF LPDSAFEGFH EQVRELRERA
KELPDEYFVV LVGDMITEEA LPTYQTMLNT LDGVRDETGA SPTPWAIWTR AWTAEENRHG
DLLNKYLYLS GRVDMRQVEK TIQYLIGSGM DPRTENNPYL GFIYTSFQER ATFISHGNTA
RLAKEHGDIK LAQICGTITA DEKRHETAYT KIVEKLFEID PEGTVIAFEE MMRKKVSMPA
HLMYDGRDDN LFHHFSAVAQ RLGVYTAKDY ADILEFLVGR WKVESLTGLS GEGQKAQDYV
CALPARIRKL EERAQGRAKE GPTIPFSWIF DRQVKL
