ID B8XJY3_SOYBN Unreviewed; 391 AA.
AC B8XJY3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Acyl-[acyl-carrier-protein] desaturase {ECO:0000256|RuleBase:RU000582};
DE EC=1.14.19.- {ECO:0000256|RuleBase:RU000582};
GN Name=SAD1 {ECO:0000313|EMBL:ACJ39209.1};
GN Synonyms=547808 {ECO:0000313|EnsemblPlants:KRH71270};
GN ORFNames=GLYMA_02G138100 {ECO:0000313|EMBL:KRH71270.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:ACJ39209.1};
RN [1] {ECO:0000313|EMBL:ACJ39209.1}
RP NUCLEOTIDE SEQUENCE.
RA Li W., Chang W., Han Y.;
RT "Some cold-related genes of soybean.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRH71270.1, ECO:0000313|EnsemblPlants:KRH71270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH71270};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH71270.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [3] {ECO:0000313|EnsemblPlants:KRH71270}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH71270};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KRH71270.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH71270.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000256|ARBA:ARBA00008749, ECO:0000256|RuleBase:RU000582}.
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DR EMBL; FJ393221; ACJ39209.1; -; mRNA.
DR EMBL; CM000835; KRH71270.1; -; Genomic_DNA.
DR RefSeq; NP_001238253.1; NM_001251324.1.
DR AlphaFoldDB; B8XJY3; -.
DR SMR; B8XJY3; -.
DR STRING; 3847.B8XJY3; -.
DR EnsemblPlants; KRH71270; KRH71270; GLYMA_02G138100.
DR GeneID; 547808; -.
DR Gramene; KRH71270; KRH71270; GLYMA_02G138100.
DR KEGG; gmx:547808; -.
DR HOGENOM; CLU_034505_1_1_1; -.
DR InParanoid; B8XJY3; -.
DR OMA; CPPRETH; -.
DR OrthoDB; 588486at2759; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000008827; Chromosome 2.
DR ExpressionAtlas; B8XJY3; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
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:UP000008827};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 171
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 171
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 260
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
SQ SEQUENCE 391 AA; 44888 MW; 9409EC3AB83E4D11 CRC64;
MALRLNPIPT QTFSLPQMAS LRSPRFRMAS TLRSGSKEVE NIKKPFTPPR EVHVQVTHSM
PPQKIEIFKS LEDWAEQNIL THLKPVEKCW QPQDFLPDPS SDGFEEQVKE LRERAKELPD
DYFVVLVGDM ITEEALPTYQ TMLNTLDGVR DETGASLTSW AIWTRAWTAE ENRHGDLLNK
YLYLSGRVDM KQIEKTIQYL IGSGMDPRTE NSPYLGFIYT SFQERATFIS HGNTARLAKE
HGDIKLAQIC GMIASDEKRH ETAYTKIVEK LFEVDPDGTV MAFADMMRKK IAMPAHLMYD
GRDDNLFDSY SSVAQRIGVY TAKDYADILE FLVGRWKVEQ LTGLSGEGRK AQEYICGLPP
RIRRLEERAQ ARVKESSTLK FSWIHDREVL L
//
