ID STAD3_ARATH Reviewed; 401 AA.
AC Q9LF05;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 24-JAN-2024, entry version 136.
DE RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 3, chloroplastic;
DE Short=Stearoyl-ACP desaturase 3;
DE EC=1.14.19.2 {ECO:0000269|PubMed:17072561, ECO:0000269|PubMed:27681170};
DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase 3;
DE Flags: Precursor;
GN Name=S-ACP-DES3; Synonyms=AAD3, SAD3; OrderedLocusNames=At5g16230;
GN ORFNames=T21H19_150;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=17072561; DOI=10.1007/s11103-006-9086-y;
RA Kachroo A., Shanklin J., Whittle E., Lapchyk L., Hildebrand D., Kachroo P.;
RT "The Arabidopsis stearoyl-acyl carrier protein-desaturase family and the
RT contribution of leaf isoforms to oleic acid synthesis.";
RL Plant Mol. Biol. 63:257-271(2007).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY MYB115 AND MYB118,
RP DEVELOPMENTAL STAGE, SITE FOR SUBSTRATE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=27681170; DOI=10.1105/tpc.16.00612;
RA Troncoso-Ponce M.A., Barthole G., Tremblais G., To A., Miquel M.,
RA Lepiniec L., Baud S.;
RT "Transcriptional activation of two palmitoyl-ACP delta9 desaturase genes by
RT MYB115 and MYB118 is critical for biosynthesis of omega-7 monounsaturated
RT fatty acid in the endosperm of Arabidopsis seeds.";
RL Plant Cell 28:2666-2682(2016).
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. Also able to
CC convert palmitoyl-ACP to palmitoleoyl-ACP at the C9 position. Exhibits
CC delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD) activity.
CC Involved in omega-7 monounsaturated fatty acid biosynthesis, especially
CC in the endosperm oil (PubMed:27681170). {ECO:0000269|PubMed:17072561,
CC ECO:0000269|PubMed:27681170}.
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:17072561, ECO:0000269|PubMed:27681170};
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 {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with a preference in leaves,
CC flowers and stems. {ECO:0000269|PubMed:17072561}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in maturing endosperm.
CC {ECO:0000269|PubMed:27681170}.
CC -!- INDUCTION: Activated by MYB115 and MYB118 in the endosperm.
CC {ECO:0000269|PubMed:27681170}.
CC -!- DISRUPTION PHENOTYPE: Reduced omega-7 fatty acids accumulation in the
CC endosperm. The endosperm oil of double mutant aad2-3 aad3-3 lacks
CC omega-7 fatty acids. {ECO:0000269|PubMed:27681170}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
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DR EMBL; AL391148; CAC01864.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92263.1; -; Genomic_DNA.
DR EMBL; BT029294; ABK32108.1; -; mRNA.
DR PIR; T51493; T51493.
DR RefSeq; NP_197127.1; NM_121628.4.
DR AlphaFoldDB; Q9LF05; -.
DR SMR; Q9LF05; -.
DR STRING; 3702.Q9LF05; -.
DR PaxDb; 3702-AT5G16230-1; -.
DR ProteomicsDB; 228342; -.
DR EnsemblPlants; AT5G16230.1; AT5G16230.1; AT5G16230.
DR GeneID; 831483; -.
DR Gramene; AT5G16230.1; AT5G16230.1; AT5G16230.
DR KEGG; ath:AT5G16230; -.
DR Araport; AT5G16230; -.
DR TAIR; AT5G16230; AAD3.
DR eggNOG; ENOG502QRJK; Eukaryota.
DR HOGENOM; CLU_034505_1_0_1; -.
DR InParanoid; Q9LF05; -.
DR OrthoDB; 652158at2759; -.
DR BRENDA; 1.14.19.2; 399.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9LF05; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF05; baseline and differential.
DR Genevisible; Q9LF05; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IDA:UniProtKB.
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:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0055089; P:fatty acid homeostasis; IMP:UniProtKB.
DR GO; GO:2000014; P:regulation of endosperm development; IMP:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:UniProtKB.
DR CDD; cd01050; Acyl_ACP_Desat; 1.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
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:SF18; STEAROYL-[ACYL-CARRIER-PROTEIN] 9-DESATURASE 3, CHLOROPLASTIC; 1.
DR Pfam; PF03405; FA_desaturase_2; 1.
DR PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..401
FT /note="Stearoyl-[acyl-carrier-protein] 9-desaturase 3,
FT chloroplastic"
FT /id="PRO_0000401421"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT SITE 216
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000305|PubMed:27681170"
SQ SEQUENCE 401 AA; 45860 MW; 8EE1D3EEF09BF65C CRC64;
MSMALLLTSP AMKQKPAVIT SPRRGSSPSR RLRVSCVTTN PARKKNETCN HFRPIKEVNN
QLTHTIPQEK LEIFKSMENW AEQKLLPYLK PVEDSWQPQD FLPAPENDDE FYDRVKEIRE
RTKEIPDDYF VVLVGDMITE EALPTYQTTL NTLDGVKDET GGSLSPWAVW IRAWTAEENR
HGDLLNKYLY LTGRVDMRHV EKTIQYLIGS GMDSKFENNP YNGFIYTSFQ ERATFISHGN
TARLATTYGD VTLAKICGTI AADEKRHETA YTKIVEKLFE IDPDGSVQAL ASMMKKRITM
PAHLMHDGRD NDLFDHYAAV AQRIGVYTAA DYAGILEFLL RRWKVESLGL GLSGEGRRAQ
EYLCTLPQRI KRLEERANDR VKLVSKPSVS FSWVFGRDVK L
//
