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STAD2_OPHAA
ID   STAD2_OPHAA             Reviewed;         376 AA.
AC   E3PZS3;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Palmitoyl-[acyl-carrier-protein] 4-desaturase 2, chloroplastic;
DE            EC=1.14.19.11 {ECO:0000250|UniProtKB:E3PZS2};
DE   AltName: Full=Acyl-[acyl-carrier-protein] desaturase 2;
DE   AltName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 2;
DE            Short=Stearoyl-ACP desaturase 2;
DE            EC=1.14.19.2 {ECO:0000250|UniProtKB:E3PZS2};
DE   Flags: Precursor;
GN   Name=SAD2;
OS   Ophrys arachnitiformis subsp. archipelagi (Orchid) (Ophrys exaltata subsp.
OS   archipelagi).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Orchidoideae; Orchideae; Orchidinae; Ophrys.
OX   NCBI_TaxID=884019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Flower;
RX   PubMed=21436056; DOI=10.1073/pnas.1013313108;
RA   Schlueter P.M., Xu S., Gagliardini V., Whittle E., Shanklin J.,
RA   Grossniklaus U., Schiestl F.P.;
RT   "Stearoyl-acyl carrier protein desaturases are associated with floral
RT   isolation in sexually deceptive orchids.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:5696-5701(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. Converts
CC       palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis
CC       double bond between carbons 4 and 5 of the acyl chain. Catalyzes the
CC       desaturation of saturated fatty acid 18:0 and 16:0 to generate 18:1
CC       (delta-9) and 16:1 (delta-4) intermediates, expected to give rise to 9-
CC       alkenes and 12-alkenes, respectively. {ECO:0000250|UniProtKB:E3PZS2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-
CC         [ferredoxin] = (4Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:38043, Rhea:RHEA-COMP:9652, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:11488,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78483,
CC         ChEBI:CHEBI:85919; EC=1.14.19.11;
CC         Evidence={ECO:0000250|UniProtKB:E3PZS2};
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:E3PZS2};
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 stroma
CC       {ECO:0000250|UniProtKB:P22337}.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in the flower labellum.
CC       {ECO:0000269|PubMed:21436056}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; FR688110; CBW95567.1; -; mRNA.
DR   AlphaFoldDB; E3PZS3; -.
DR   SMR; E3PZS3; -.
DR   UniPathway; UPA00199; -.
DR   GO; GO:0009570; C:chloroplast stroma; 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; 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   2: Evidence at transcript level;
KW   Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..376
FT                   /note="Palmitoyl-[acyl-carrier-protein] 4-desaturase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000417066"
FT   BINDING         114
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
SQ   SEQUENCE   376 AA;  42465 MW;  64F9EEAB060AA385 CRC64;
     MELHLALRAS PLPAADPGRR PPPPRGNFAT NCTAAINSTH ISQEKFRSLD SWVEHNMLTF
     LKPVEKCWQP QDFLPDPSHL SAEELGDAVR EIHERAAEIP DEVWVCMVGN MVTEEALPTY
     QSLISSVLGG TVAGSTPWDR WIRGWSAEEN RHGDLLNKYL YLTGRLDMRQ VEKTIQYLIG
     SGMDVGVGNS ILCGFIYTCF QEKATFIPHG NTARLAKHHG DTTLAKICGL VAADEKRHAA
     AYTNLMRKLF EVDPNESMLA FAHVMQARVT MPASRMFDGR DPHLFTHFSD VSQKIGVYTV
     GDYSEMLDFF LKEWDISAIV DGLSPEGRRV QEYVCGLPEV MRKLAERADD RRKKLVNVGE
     PRYIPFSWIF NKQVRV
 
 
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