STAD_RICCO
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 03-AUG-2022, entry version 144.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 STRING; 3988.XP_002531889.1; -.
DR PRIDE; P22337; -.
DR GeneID; 8271760; -.
DR KEGG; rcu:8271760; -.
DR eggNOG; ENOG502QRJK; Eukaryota.
DR OrthoDB; 608188at2759; -.
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; -; 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 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
