位置:首页 > 蛋白库 > STAD2_ORYSI
STAD2_ORYSI
ID   STAD2_ORYSI             Reviewed;         396 AA.
AC   A2WYF4;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 2, chloroplastic;
DE            Short=Stearoyl-ACP desaturase 2;
DE            EC=1.14.19.2 {ECO:0000250|UniProtKB:P22337};
DE   AltName: Full=Acyl-[acyl-carrier-protein] desaturase 2;
DE   AltName: Full=SSI2 homolog;
DE            Short=OsSSI2;
DE   Flags: Precursor;
GN   Name=SSI2; ORFNames=OsI_04956;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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).
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. Required for
CC       the repression of the salicylic acid (SA) signaling pathway.
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {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; CM000126; EAY77000.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2WYF4; -.
DR   SMR; A2WYF4; -.
DR   STRING; 39946.A2WYF4; -.
DR   EnsemblPlants; BGIOSGA000237-TA; BGIOSGA000237-PA; BGIOSGA000237.
DR   Gramene; BGIOSGA000237-TA; BGIOSGA000237-PA; BGIOSGA000237.
DR   HOGENOM; CLU_034505_1_1_1; -.
DR   OMA; NRHSMLH; -.
DR   UniPathway; UPA00199; -.
DR   Proteomes; UP000007015; Chromosome 1.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW   Plant defense; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..396
FT                   /note="Stearoyl-[acyl-carrier-protein] 9-desaturase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000401429"
FT   BINDING         138
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         179
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         229
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         262
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         262
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
SQ   SEQUENCE   396 AA;  44875 MW;  2A3C588505FFF6DD CRC64;
     MALRPNDVTL RLTPPLAAAA RRNRRAAAGG VRVYAVASGA VSTKVENKKP FAPPREVHVQ
     VTHSMPPQKI EIFKSLDDWA RDNILSHLKP VEKCWQPQDF LPDPASDGFH DEVKELRERA
     KEIPDDYFVC LVGDMITEEA LPTYQTMLNT LDGVRDETGA SPTAWAVWTR AWTAEENRHG
     DLLNKYLYLT GRVDMRQIEK TIQYLIGSGM DPRTENNPYL GFIYTSFQER ATFISHGNTA
     RHAKDFGDLK LAQICGIIAS DEKRHETAYT KIVEKLFEID PDGTVLAFAD MMKKKISMPA
     HLMFDGEDDK LFEHFSMVAQ RLGVYTAKDY ADILEFLVSR WKISDLTGLS SEGNKAQDYL
     CTLAARIRRL DERAQSRAKK AGTLPFSWVY GREVQL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024