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ZDS_CAPAN
ID   ZDS_CAPAN               Reviewed;         588 AA.
AC   Q9SMJ3;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Zeta-carotene desaturase, chloroplastic/chromoplastic;
DE            EC=1.3.5.6;
DE   AltName: Full=9,9'-di-cis-zeta-carotene desaturase;
DE   AltName: Full=Carotene 7,8-desaturase;
DE   Flags: Precursor;
GN   Name=ZDS;
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Lamuyo; TISSUE=Fruit;
RX   PubMed=7556669; DOI=10.1016/0014-5793(95)00978-i;
RA   Albrecht M., Klein A., Hugueney P., Sandmann G., Kuntz M.;
RT   "Molecular cloning and functional expression in E. coli of a novel plant
RT   enzyme mediating zeta-carotene desaturation.";
RL   FEBS Lett. 372:199-202(1995).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=10491195; DOI=10.1046/j.1432-1327.1999.00746.x;
RA   Breitenbach J., Kuntz M., Takaichi S., Sandmann G.;
RT   "Catalytic properties of an expressed and purified higher plant type zeta-
RT   carotene desaturase from Capsicum annuum.";
RL   Eur. J. Biochem. 265:376-383(1999).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15503129; DOI=10.1007/s00425-004-1395-2;
RA   Breitenbach J., Sandmann G.;
RT   "zeta-Carotene cis isomers as products and substrates in the plant poly-cis
RT   carotenoid biosynthetic pathway to lycopene.";
RL   Planta 220:785-793(2005).
CC   -!- FUNCTION: Catalyzes the conversion of zeta-carotene to lycopene via the
CC       intermediary of neurosporene. It carries out two consecutive
CC       desaturations (introduction of double bonds) at positions C-7 and C-7'.
CC       Shows stereoselectivity toward trans C15-C15'zeta-carotene double bond.
CC       The zeta-carotene produced by the phytoene desaturase PDS has a C15-
CC       C15' double bond in the cis configuration and it requires isomerization
CC       before being recognized as substrate by ZDS. No activity with all-
CC       trans-zeta-carotene. The main product is 7,9,7',9'-tetra-cis-lycopene
CC       (pro-lycopene). {ECO:0000269|PubMed:10491195,
CC       ECO:0000269|PubMed:15503129}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9,9'-di-cis-zeta-carotene + 2 a quinone = 7,7',9,9'-tetra-cis-
CC         lycopene + 2 a quinol; Xref=Rhea:RHEA:30955, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:48716, ChEBI:CHEBI:62466, ChEBI:CHEBI:132124; EC=1.3.5.6;
CC         Evidence={ECO:0000269|PubMed:10491195, ECO:0000269|PubMed:15503129};
CC   -!- COFACTOR:
CC       Name=decylplastoquinone; Xref=ChEBI:CHEBI:72953;
CC         Evidence={ECO:0000269|PubMed:10491195};
CC       Name=6-decylubiquinone; Xref=ChEBI:CHEBI:52020;
CC         Evidence={ECO:0000269|PubMed:10491195};
CC       Note=Lipophilic quinones such as decyl-plastoquinone or decyl-
CC       ubiquinone. {ECO:0000269|PubMed:10491195};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.4 uM for zeta-carotene {ECO:0000269|PubMed:10491195};
CC         KM=9.0 uM for neurosporene {ECO:0000269|PubMed:10491195};
CC         Vmax=0.665 nmol/h/mg enzyme with zeta-carotene as substrate
CC         {ECO:0000269|PubMed:10491195};
CC         Vmax=0.0542 nmol/h/mg enzyme with neurosporene as substrate
CC         {ECO:0000269|PubMed:10491195};
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC   -!- SUBUNIT: Monomer and dimer. {ECO:0000269|PubMed:10491195}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, chromoplast.
CC   -!- SIMILARITY: Belongs to the zeta carotene desaturase family.
CC       {ECO:0000305}.
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DR   EMBL; X89897; CAA61985.1; -; mRNA.
DR   PIR; S66625; S66625.
DR   RefSeq; NP_001311497.1; NM_001324568.1.
DR   AlphaFoldDB; Q9SMJ3; -.
DR   SMR; Q9SMJ3; -.
DR   ChEMBL; CHEMBL2268004; -.
DR   GeneID; 107839468; -.
DR   KEGG; ag:CAA61985; -.
DR   KEGG; cann:107839468; -.
DR   SABIO-RK; Q9SMJ3; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000189700; Genome assembly.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0052887; F:7,9,9'-tricis-neurosporene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052886; F:9,9'-dicis-carotene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016719; F:carotene 7,8-desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR014103; Zeta_caro_desat.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02732; zeta_caro_desat; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Chloroplast; Chromoplast; Oxidoreductase; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast and chromoplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..588
FT                   /note="Zeta-carotene desaturase,
FT                   chloroplastic/chromoplastic"
FT                   /id="PRO_0000041606"
SQ   SEQUENCE   588 AA;  64684 MW;  55F5668FAEE7EA91 CRC64;
     MATCSAYLCC PATSASLKKR VFPDGSAGFL FFGGRRLSNR LVTPKSVIRA DLNSMVSDMS
     TNAPKGLFPP EPEHYRGPKL KVAIIGAGLA GMSTAVELLD QGHEVDIYES RTFIGGKVGS
     FVDKRGNHIE MGLHVFFGCY NNLFRLMKKV GAEKNLLVKE HTHTFVNKGG EIGELDFRFP
     VGAPLHGINA FLSTNQLKTY DKARNAVALA LSPVVRALVD PDGALQQIRD LDSVSFSDWF
     MSKGGTRASI QRMWDPVAYA LGFIDCDNIS ARCMLTIFAL FATKTEASLL RMLKGSPDVY
     LSGPIKKYII DKGGRFHLRW GCREVLYETS SDGSMYVSGL AMSKATQKKI VKADAYVAAC
     VVPGIKRLVP QKWRELEFFG NIYKLIGVPV VTVQLRYNGW VTELQDLERS RQSKRATGLD
     NLLYTPDADF SCFADLALAS PEDYYIEGQG SLLQCVLTPG DPYMPLPNEE IIRRVSKQVL
     ALFPSSQGLE VTWSSVVKIG QSLYREGPGK DPFRPDQKTP VENFFLAGSY TKQDYIDSME
     GATLSGRQAS AYICDAGEQL LALRKKIAAA ELNEISKGVS LSDELSLV
 
 
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