ID   STAD_RICCO              Reviewed;         396 AA.
AC   P22337;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic;
DE            Short=Stearoyl-ACP desaturase;
DE            EC=1.14.19.2 {ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:21930947};
DE   AltName: Full=Acyl-[acyl-carrier-protein] desaturase;
DE   AltName: Full=Delta(9) stearoyl-acyl carrier protein desaturase;
DE   Flags: Precursor;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Endosperm;
RX   PubMed=16668180; DOI=10.1104/pp.96.1.344;
RA   Knutzon D.S., Scherer D.E., Schreckengost W.E.;
RT   "Nucleotide sequence of a complementary DNA clone encoding stearoyl-acyl
RT   carrier protein desaturase from castor bean, Ricinus communis.";
RL   Plant Physiol. 96:344-345(1991).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 52-396 IN COMPLEX WITH IRON, AND
RP   COFACTOR.
RX   PubMed=8861937; DOI=10.1002/j.1460-2075.1996.tb00783.x;
RA   Lindqvist Y., Huang W., Schneider G., Shanklin J.;
RT   "Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from
RT   castor seed and its relationship to other di-iron proteins.";
RL   EMBO J. 15:4081-4092(1996).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 34-396 IN COMPLEX WITH IRON, AND
RP   COFACTOR.
RX   PubMed=12704186; DOI=10.1074/jbc.m301662200;
RA   Moche M., Shanklin J., Ghoshal A., Lindqvist Y.;
RT   "Azide and acetate complexes plus two iron-depleted crystal structures of
RT   the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase.
RT   Implications for oxygen activation and catalytic intermediates.";
RL   J. Biol. Chem. 278:25072-25080(2003).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 34-396 IN COMPLEX WITH IRON,
RP   MUTAGENESIS OF THR-232, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=17088542; DOI=10.1073/pnas.0607165103;
RA   Guy J.E., Abreu I.A., Moche M., Lindqvist Y., Whittle E., Shanklin J.;
RT   "A single mutation in the castor Delta9-18:0-desaturase changes reaction
RT   partitioning from desaturation to oxidase chemistry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17220-17224(2006).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 34-396, MUTAGENESIS OF ASP-313,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21930947; DOI=10.1073/pnas.1110221108;
RA   Guy J.E., Whittle E., Moche M., Lengqvist J., Lindqvist Y., Shanklin J.;
RT   "Remote control of regioselectivity in acyl-acyl carrier protein-
RT   desaturases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:16594-16599(2011).
CC   -!- FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis
CC       double bond between carbons 9 and 10 of the acyl chain.
CC       {ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:21930947}.
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:0000269|PubMed:17088542, ECO:0000269|PubMed:21930947};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542,
CC         ECO:0000269|PubMed:8861937};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000269|PubMed:12704186,
CC       ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12704186,
CC       ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937}.
CC   -!- INTERACTION:
CC       P22337; P07854: ACL1.1; Xeno; NbExp=2; IntAct=EBI-15944981, EBI-15944962;
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: Higher levels in developing seeds than in leaf and
CC       root tissues.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA74692.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M59857; AAA74692.1; ALT_INIT; mRNA.
DR   EMBL; X56508; CAA39859.1; -; mRNA.
DR   PIR; S16463; OHCSAD.
DR   RefSeq; NP_001310659.1; NM_001323730.1.
DR   PDB; 1AFR; X-ray; 2.40 A; A/B/C/D/E/F=52-396.
DR   PDB; 1OQ4; X-ray; 2.40 A; A/B/C/D/E/F=34-396.
DR   PDB; 1OQ7; X-ray; 3.20 A; A/B/C/D/E/F=34-396.
DR   PDB; 1OQ9; X-ray; 2.40 A; A=34-396.
DR   PDB; 1OQB; X-ray; 2.80 A; A/B/C/D/E/F=34-396.
DR   PDB; 2J2F; X-ray; 2.65 A; A/B/C/D/E/F=34-396.
DR   PDB; 2XZ0; X-ray; 3.00 A; A/B/C=34-396.
DR   PDB; 2XZ1; X-ray; 3.35 A; A/B=34-396.
DR   PDB; 4V0J; X-ray; 2.80 A; A/B/C/D/E/F=66-396.
DR   PDBsum; 1AFR; -.
DR   PDBsum; 1OQ4; -.
DR   PDBsum; 1OQ7; -.
DR   PDBsum; 1OQ9; -.
DR   PDBsum; 1OQB; -.
DR   PDBsum; 2J2F; -.
DR   PDBsum; 2XZ0; -.
DR   PDBsum; 2XZ1; -.
DR   PDBsum; 4V0J; -.
DR   AlphaFoldDB; P22337; -.
DR   SMR; P22337; -.
DR   DIP; DIP-60379N; -.
DR   IntAct; P22337; 1.
DR   GeneID; 8271760; -.
DR   KEGG; rcu:8271760; -.
DR   eggNOG; ENOG502QRJK; Eukaryota.
DR   OrthoDB; 588486at2759; -.
DR   BRENDA; 1.14.19.2; 1204.
DR   SABIO-RK; P22337; -.
DR   UniPathway; UPA00199; -.
DR   EvolutionaryTrace; P22337; -.
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:SF9; STEAROYL-[ACYL-CARRIER-PROTEIN] 9-DESATURASE 7, 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   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Chloroplast"
FT   CHAIN           34..396
FT                   /note="Stearoyl-[acyl-carrier-protein] 9-desaturase,
FT                   chloroplastic"
FT                   /id="PRO_0000007137"
FT   BINDING         138
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12704186,
FT                   ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12704186,
FT                   ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12704186,
FT                   ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937"
FT   BINDING         179
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12704186,
FT                   ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937"
FT   BINDING         229
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12704186,
FT                   ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937"
FT   BINDING         262
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12704186,
FT                   ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937"
FT   BINDING         262
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12704186,
FT                   ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12704186,
FT                   ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937"
FT   MUTAGEN         232
FT                   /note="T->D,E: Decreases desaturase activity and increases
FT                   oxidase activity."
FT                   /evidence="ECO:0000269|PubMed:17088542"
FT   MUTAGEN         313
FT                   /note="D->K,R: Decreases Delta(9) desaturase activity and
FT                   increases Delta(4) desaturase activity."
FT                   /evidence="ECO:0000269|PubMed:21930947"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           70..75
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           77..83
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           109..121
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           125..139
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           141..148
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           164..190
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:1OQ4"
FT   HELIX           195..208
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           218..245
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           249..279
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           281..294
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   TURN            299..302
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           311..322
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           327..341
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           343..345
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           351..372
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           376..379
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   STRAND          383..385
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   HELIX           387..389
FT                   /evidence="ECO:0007829|PDB:1AFR"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:1AFR"
SQ   SEQUENCE   396 AA;  45371 MW;  E50D4725996392AF CRC64;
     MALKLNPFLS QTQKLPSFAL PPMASTRSPK FYMASTLKSG SKEVENLKKP FMPPREVHVQ
     VTHSMPPQKI EIFKSLDNWA EENILVHLKP VEKCWQPQDF LPDPASDGFD EQVRELRERA
     KEIPDDYFVV LVGDMITEEA LPTYQTMLNT LDGVRDETGA SPTSWAIWTR AWTAEENRHG
     DLLNKYLYLS GRVDMRQIEK TIQYLIGSGM DPRTENSPYL GFIYTSFQER ATFISHGNTA
     RQAKEHGDIK LAQICGTIAA DEKRHETAYT KIVEKLFEID PDGTVLAFAD MMRKKISMPA
     HLMYDGRDDN LFDHFSAVAQ RLGVYTAKDY ADILEFLVGR WKVDKLTGLS AEGQKAQDYV
     CRLPPRIRRL EERAQGRAKE APTMPFSWIF DRQVKL
//