CHLP_ARATH
ID CHLP_ARATH Reviewed; 467 AA.
AC Q9CA67; B9DHM2; O49594; Q56YY5; Q8H170;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Geranylgeranyl diphosphate reductase, chloroplastic;
DE EC=1.3.1.83;
DE AltName: Full=Geranylgeranyl reductase;
DE Flags: Precursor;
GN Name=CHLP; OrderedLocusNames=At1g74470; ORFNames=F1M20.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9492312; DOI=10.1046/j.1432-1327.1998.2510413.x;
RA Keller Y., Bouvier F., d'Harlingue A., Camara B.;
RT "Metabolic compartmentation of plastid prenyllipid biosynthesis -- evidence
RT for the involvement of a multifunctional geranylgeranyl reductase.";
RL Eur. J. Biochem. 251:413-417(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-467.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-467.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST
RP MEMBRANE COMPLEX.
RX PubMed=22212719; DOI=10.1016/j.febslet.2011.12.029;
RA Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.;
RT "FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is
RT physically linked to the final steps of the Mg(++)-branch of this
RT pathway.";
RL FEBS Lett. 586:211-216(2012).
CC -!- FUNCTION: Catalyzes the reduction of geranylgeranyl diphosphate to
CC phytyl diphosphate, providing phytol for both tocopherol and
CC chlorophyll synthesis. {ECO:0000269|PubMed:9492312}.
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 -!- SUBUNIT: Part of the FLU-containing chloroplast membrane complex
CC composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1.
CC {ECO:0000269|PubMed:22212719}.
CC -!- INTERACTION:
CC Q9CA67; Q39016: CPK11; NbExp=5; IntAct=EBI-2298544, EBI-979321;
CC Q9CA67; Q9SYX1: LIL3.1; NbExp=2; IntAct=EBI-2298544, EBI-11361535;
CC Q9CA67; Q6NKS4: LIL3.2; NbExp=2; IntAct=EBI-2298544, EBI-11361548;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:22212719}.
CC -!- DEVELOPMENTAL STAGE: Expressed during deetiolation and during
CC chloroplast to chromoplast transformation.
CC {ECO:0000269|PubMed:9492312}.
CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. ChlP
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA74372.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y14044; CAA74372.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC011765; AAG52372.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35597.1; -; Genomic_DNA.
DR EMBL; AY050893; AAK92830.1; -; mRNA.
DR EMBL; AY052328; AAK96521.1; -; mRNA.
DR EMBL; AY059860; AAL24342.1; -; mRNA.
DR EMBL; AY075688; AAL77695.1; -; mRNA.
DR EMBL; AY091297; AAM14236.1; -; mRNA.
DR EMBL; AY102144; AAM26711.1; -; mRNA.
DR EMBL; BT000734; AAN31876.1; -; mRNA.
DR EMBL; BT002571; AAO00931.1; -; mRNA.
DR EMBL; BT000656; AAN31803.1; -; mRNA.
DR EMBL; AK221185; BAD95270.1; -; mRNA.
DR EMBL; AK317575; BAH20239.1; -; mRNA.
DR PIR; F96773; F96773.
DR RefSeq; NP_177587.1; NM_106107.3.
DR AlphaFoldDB; Q9CA67; -.
DR SMR; Q9CA67; -.
DR BioGRID; 29007; 3.
DR DIP; DIP-53238N; -.
DR IntAct; Q9CA67; 7.
DR MINT; Q9CA67; -.
DR STRING; 3702.AT1G74470.1; -.
DR PaxDb; Q9CA67; -.
DR PRIDE; Q9CA67; -.
DR ProteomicsDB; 246880; -.
DR EnsemblPlants; AT1G74470.1; AT1G74470.1; AT1G74470.
DR GeneID; 843788; -.
DR Gramene; AT1G74470.1; AT1G74470.1; AT1G74470.
DR KEGG; ath:AT1G74470; -.
DR Araport; AT1G74470; -.
DR TAIR; locus:2019165; AT1G74470.
DR eggNOG; ENOG502QQWY; Eukaryota.
DR HOGENOM; CLU_024648_3_1_1; -.
DR InParanoid; Q9CA67; -.
DR OMA; TLHYTEY; -.
DR OrthoDB; 894979at2759; -.
DR PhylomeDB; Q9CA67; -.
DR BioCyc; ARA:AT1G74470-MON; -.
DR BioCyc; MetaCyc:AT1G74470-MON; -.
DR BRENDA; 1.3.1.83; 399.
DR UniPathway; UPA00160; -.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q9CA67; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA67; baseline and differential.
DR Genevisible; Q9CA67; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR010253; BchP_ChlP_pln/prok.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR011777; Geranylgeranyl_Rdtase_fam.
DR InterPro; IPR011774; Geranylgeranyl_Rdtase_pln/cyn.
DR Pfam; PF07992; Pyr_redox_2; 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 1: Evidence at protein level;
KW Chlorophyll biosynthesis; Chloroplast; Membrane; NADP; Oxidoreductase;
KW Photosynthesis; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..467
FT /note="Geranylgeranyl diphosphate reductase, chloroplastic"
FT /id="PRO_0000386542"
FT CONFLICT 194
FT /note="T -> A (in Ref. 4; AAN31803)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="K -> E (in Ref. 6; BAH20239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 51838 MW; A535388BE7758EBE CRC64;
MATTVTLKSF TGLRQSSTEQ TNFVSHVPSS LSLPQRRTSL RVTAARATPK LSNRKLRVAV
IGGGPAGGAA AETLAQGGIE TILIERKMDN CKPCGGAIPL CMVGEFNLPL DIIDRRVTKM
KMISPSNIAV DIGRTLKEHE YIGMVRREVL DAYLRERAEK SGATVINGLF LKMDHPENWD
SPYTLHYTEY DGKTGATGTK KTMEVDAVIG ADGANSRVAK SIDAGDYDYA IAFQERIRIP
DEKMTYYEDL AEMYVGDDVS PDFYGWVFPK CDHVAVGTGT VTHKGDIKKF QLATRNRAKD
KILGGKIIRV EAHPIPEHPR PRRLSKRVAL VGDAAGYVTK CSGEGIYFAA KSGRMCAEAI
VEGSQNGKKM IDEGDLRKYL EKWDKTYLPT YRVLDVLQKV FYRSNPAREA FVEMCNDEYV
QKMTFDSYLY KRVAPGSPLE DIKLAVNTIG SLVRANALRR EIEKLSV
