ID   CHLP_SYNY3              Reviewed;         407 AA.
AC   Q55087; P74245;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Geranylgeranyl diphosphate reductase;
DE            EC=1.3.1.83;
DE   AltName: Full=Geranylgeranyl reductase;
GN   Name=chlP; OrderedLocusNames=sll1091;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8766814; DOI=10.1016/0014-5793(96)00549-2;
RA   Addlesee H.A., Gibson L.C.D., Jensen P.E., Hunter C.N.;
RT   "Cloning, sequencing and functional assignment of the chlorophyll
RT   biosynthesis gene, chlP, of Synechocystis sp. PCC 6803.";
RL   FEBS Lett. 389:126-130(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Catalyzes the stepwise hydrogenation of geranylgeraniol to
CC       phytol during chlorophyll A (ChlA) biosynthesis.
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   -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. ChlP
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA18339.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X97972; CAA66615.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18339.1; ALT_INIT; Genomic_DNA.
DR   PIR; S69286; S69286.
DR   AlphaFoldDB; Q55087; -.
DR   SMR; Q55087; -.
DR   STRING; 1148.1653425; -.
DR   PaxDb; Q55087; -.
DR   EnsemblBacteria; BAA18339; BAA18339; BAA18339.
DR   KEGG; syn:sll1091; -.
DR   eggNOG; COG0644; Bacteria.
DR   InParanoid; Q55087; -.
DR   OMA; GMCRREV; -.
DR   PhylomeDB; Q55087; -.
DR   BRENDA; 1.3.1.111; 382.
DR   BRENDA; 1.3.1.83; 382.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000001425; Chromosome.
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; IEA:InterPro.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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; 2.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02023; BchP-ChlP; 1.
DR   TIGRFAMs; TIGR02028; ChlP; 1.
DR   TIGRFAMs; TIGR02032; GG-red-SF; 1.
PE   3: Inferred from homology;
KW   Chlorophyll biosynthesis; NADP; Oxidoreductase; Photosynthesis;
KW   Reference proteome.
FT   CHAIN           1..407
FT                   /note="Geranylgeranyl diphosphate reductase"
FT                   /id="PRO_0000219664"
SQ   SEQUENCE   407 AA;  44883 MW;  1D46FA7AE1C43CC5 CRC64;
     MVLRVAVVGG GPAGSSAAEI LVKAGIETYL FERKLDNAKP CGGAIPLCMV DEFDLPPEII
     DRRVRKMKMI SPSNIEVNIG QTLKDDEYIG MCRREVLDGF LRERAEKLGT KVINGTVYKL
     DIPSKDSDPY TLHYADHSVG GTTGEMKILK VDVVIGADGA NSRIAKAIDA GDYNYAIAFQ
     ERIRLPEDKM AYYDELAEMY VGDDVSPDFY AWVFPKYDHV AVGTGTMKVN KARIKDLQAG
     IRTRAAKKLE GGEIIKVEAH PIPEHPRPRR VVGRVALVGD AAGTVTKSSG EGIYFAAKSA
     RMCAETIVAT SNNGQRVPTE ADLKQYIKQW DKRYGATYLV LDILQRVFYR TDATREAFVE
     MCSDIDVQKL TFDSYLYKTV VPANPLVQMK ITAKTIGSLL RGNALAP