STAD5_ORYSJ
ID STAD5_ORYSJ Reviewed; 390 AA.
AC Q40731; A0A0P0W9B6; Q0JDS9; Q7XNQ5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 5, chloroplastic;
DE Short=Stearoyl-ACP desaturase 5;
DE EC=1.14.19.2 {ECO:0000250|UniProtKB:P22337};
DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase 5;
DE Flags: Precursor;
GN OrderedLocusNames=Os04g0379900, LOC_Os04g31070;
GN ORFNames=OsJ_14516, OSJNBb0089B03.6;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Seed;
RX PubMed=7610181; DOI=10.1104/pp.108.2.845;
RA Akagi H., Baba T., Shimada H., Fujimura T.;
RT "Nucleotide sequence of a stearoyl-acyl carrier protein desaturase cDNA
RT from developing seeds of rice.";
RL Plant Physiol. 108:845-846(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP GENE FAMILY.
RX PubMed=19522564; DOI=10.1094/mpmi-22-7-0820;
RA Jiang C.J., Shimono M., Maeda S., Inoue H., Mori M., Hasegawa M.,
RA Sugano S., Takatsuji H.;
RT "Suppression of the rice fatty-acid desaturase gene OsSSI2 enhances
RT resistance to blast and leaf blight diseases in rice.";
RL Mol. Plant Microbe Interact. 22:820-829(2009).
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:0000250|UniProtKB:P22337}.
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:0000250|UniProtKB:P22337};
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
CC {ECO:0000250|UniProtKB:P22337}. Plastid {ECO:0000250|UniProtKB:P22337}.
CC Note=In green tissue, found in chloroplasts. In non-photosynthetic
CC tissue, found in plastids.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE03992.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D38753; BAA07631.1; -; mRNA.
DR EMBL; AL607000; CAE03992.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14508.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS88879.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE60868.1; -; Genomic_DNA.
DR EMBL; AK065340; BAG89478.1; -; mRNA.
DR PIR; T04097; T04097.
DR RefSeq; XP_015636259.1; XM_015780773.1.
DR AlphaFoldDB; Q40731; -.
DR SMR; Q40731; -.
DR STRING; 4530.OS04T0379900-01; -.
DR PaxDb; Q40731; -.
DR PRIDE; Q40731; -.
DR EnsemblPlants; Os04t0379900-01; Os04t0379900-01; Os04g0379900.
DR GeneID; 4335627; -.
DR Gramene; Os04t0379900-01; Os04t0379900-01; Os04g0379900.
DR KEGG; osa:4335627; -.
DR eggNOG; ENOG502QRJK; Eukaryota.
DR HOGENOM; CLU_034505_1_1_1; -.
DR InParanoid; Q40731; -.
DR OMA; LAPNQAM; -.
DR OrthoDB; 608188at2759; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q40731; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0102786; F:stearoyl-[acp] desaturase activity; IEA:UniProtKB-EC.
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; -; 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; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P22243"
FT CHAIN 32..390
FT /note="Stearoyl-[acyl-carrier-protein] 9-desaturase 5,
FT chloroplastic"
FT /id="PRO_0000007136"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT CONFLICT 12
FT /note="S -> Y (in Ref. 1; BAA07631)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..28
FT /note="PV -> KM (in Ref. 1; BAA07631)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="K -> N (in Ref. 1; BAA07631)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="P -> T (in Ref. 1; BAA07631)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="F -> L (in Ref. 1; BAA07631)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="A -> V (in Ref. 1; BAA07631)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="I -> M (in Ref. 1; BAA07631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 44341 MW; 02416A09813A48F0 CRC64;
MAFAASHTAS PSSCGGVAQR RSNGMSPVVA MASTINRVKT AKKPYTPPRE VHLQVKHSLP
PQKREIFDSL QPWAKENLLN LLKPVEKSWQ PQDFLPDPSS DGFYDEVKEL RERAKEIPDD
YFVCLVGDMV TEEALPTYQT MLNTLDGVRD ETGASPTTWA VWTRAWTAEE NRHGDLLNKY
MYLTGRVDMK QIEKTIQYLI GSGMDPGTEN NPYLGFLYTS FQERATFISH GNTARHAKEY
GDLKLAQICG TIAADEKRHE TAYTKIVEKL FEIDPDYTVL AFADMMRKKI SMPAHLMYDG
KDDNLFEHFS AVAQRLGVYT ARDYADILEF LVQRWKVADL TGLSGEGRRA QDFVCTLAPR
IRRLDERAQA RAKQAPVIPF SWVYDRKVQL
