ID   CHLP_TOBAC              Reviewed;         464 AA.
AC   Q9ZS34;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Geranylgeranyl diphosphate reductase, chloroplastic;
DE            EC=1.3.1.83;
DE   AltName: Full=Geranylgeranyl reductase;
DE   Flags: Precursor;
GN   Name=CHLP;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=10398704; DOI=10.1104/pp.120.3.695;
RA   Tanaka R., Oster U., Kruse E., Ruediger W., Grimm B.;
RT   "Reduced activity of geranylgeranyl reductase leads to loss of chlorophyll
RT   and tocopherol and to partially geranylgeranylated chlorophyll in
RT   transgenic tobacco plants expressing antisense RNA for geranylgeranyl
RT   reductase.";
RL   Plant Physiol. 120:695-704(1999).
CC   -!- FUNCTION: Catalyzes the reduction of geranylgeranyl diphosphate to
CC       phytyl diphosphate, providing phytol for both tocopherol and
CC       chlorophyll synthesis. {ECO:0000269|PubMed:10398704}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 NADP(+) + phytyl diphosphate = geranylgeranyl diphosphate +
CC         3 H(+) + 3 NADPH; Xref=Rhea:RHEA:26229, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57533, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:75434; EC=1.3.1.83;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Constant levels during the development of leaves.
CC       {ECO:0000269|PubMed:10398704}.
CC   -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. ChlP
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ007789; CAA07683.1; -; mRNA.
DR   RefSeq; NP_001312288.1; NM_001325359.1.
DR   AlphaFoldDB; Q9ZS34; -.
DR   SMR; Q9ZS34; -.
DR   STRING; 4097.Q9ZS34; -.
DR   PRIDE; Q9ZS34; -.
DR   GeneID; 107783257; -.
DR   KEGG; ag:CAA07683; -.
DR   KEGG; nta:107783257; -.
DR   OMA; GMCRREV; -.
DR   BioCyc; MetaCyc:MON-14870; -.
DR   BRENDA; 1.3.1.83; 3645.
DR   UniPathway; UPA00160; -.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0102067; F:geranylgeranyl diphosphate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045550; F:geranylgeranyl reductase activity; IBA:GO_Central.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0033385; P:geranylgeranyl diphosphate metabolic process; IMP:UniProtKB.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   GO; GO:0033521; P:phytyl diphosphate biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0010189; P:vitamin E biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR010253; BchP_ChlP_pln/prok.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR011777; Geranylgeranyl_Rdtase_fam.
DR   InterPro; IPR011774; Geranylgeranyl_Rdtase_pln/cyn.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02023; BchP-ChlP; 1.
DR   TIGRFAMs; TIGR02028; ChlP; 1.
DR   TIGRFAMs; TIGR02032; GG-red-SF; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase;
KW   Photosynthesis; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           55..464
FT                   /note="Geranylgeranyl diphosphate reductase, chloroplastic"
FT                   /id="PRO_0000386544"
SQ   SEQUENCE   464 AA;  51301 MW;  8F99F85EDDBFB765 CRC64;
     MASIALKTFT GLRQSSPENN SITLSKSLPF TQTHRRLRIN ASKSSPRVNG RNLRVAVVGG
     GPAGGAAAET LAKGGIETFL IERKMDNCKP CGGAIPLCMV GEFDLPLDII DRKVTKMKMI
     SPSNVAVDIG QTLKPHEYIG MVRREVLDAY LRDRAAEAGA SVLNGLFLKM DMPKAPNAPY
     VLHYTAYDSK TNGAGEKRTL EVDAVIGADG ANSRVAKSIN AGDYEYAIAF QERIKISDDK
     MKYYENLAEM YVGDDVSPDF YGWVFPKCDH VAVGTGTVTH KADIKKFQLA TRLRADSKIT
     GGKIIRVEAH PIPEHPRPRR LQDRVALVGD AAGYVTKCSG EGIYFAAKSG RMCAEAIVEG
     SEMGKRMVDE SDLRKYLEKW DKTYWPTYKV LDILQKVFYR SNPAREAFVE MCADEYVQKM
     TFDSYLYKKV APGNPIEDLK LAVNTIGSLV RANALRREMD KLSV