DCVR_ARATH
ID DCVR_ARATH Reviewed; 417 AA.
AC Q1H537; Q8GZ86; Q8LE07;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic;
DE EC=1.3.1.75 {ECO:0000269|PubMed:15632054, ECO:0000269|PubMed:17991629};
DE AltName: Full=Protein PALE-GREEN AND CHLOROPHYLL B REDUCED 2;
DE Flags: Precursor;
GN Name=DVR; Synonyms=PCB2; OrderedLocusNames=At5g18660; ORFNames=T1A4.40;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF PRO-333.
RX PubMed=15632054; DOI=10.1105/tpc.104.027276;
RA Nagata N., Tanaka R., Satoh S., Tanaka A.;
RT "Identification of a vinyl reductase gene for chlorophyll synthesis in
RT Arabidopsis thaliana and implications for the evolution of Prochlorococcus
RT species.";
RL Plant Cell 17:233-240(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15695432; DOI=10.1093/pcp/pci053;
RA Nakanishi H., Nozue H., Suzuki K., Kaneko Y., Taguchi G., Hayashida N.;
RT "Characterization of the Arabidopsis thaliana mutant pcb2 which accumulates
RT divinyl chlorophylls.";
RL Plant Cell Physiol. 46:467-473(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17991629; DOI=10.1093/pcp/pcm153;
RA Nagata N., Tanaka R., Tanaka A.;
RT "The major route for chlorophyll synthesis includes [3,8-divinyl]-
RT chlorophyllide a reduction in Arabidopsis thaliana.";
RL Plant Cell Physiol. 48:1803-1808(2007).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23154534; DOI=10.1104/pp.112.208421;
RA Wang P., Wan C., Xu Z., Wang P., Wang W., Sun C., Ma X., Xiao Y., Zhu J.,
RA Gao X., Deng X.;
RT "One divinyl reductase reduces the 8-vinyl groups in various intermediates
RT of chlorophyll biosynthesis in a given higher plant species, but the
RT isozyme differs between species.";
RL Plant Physiol. 161:521-534(2013).
CC -!- FUNCTION: Catalyzes the conversion of divinyl chlorophyllide to
CC monovinyl chlorophyllide. Reduces the 8-vinyl group of the tetrapyrrole
CC to an ethyl group using NADPH as the reductant. The best substrate is
CC (3,8-divinyl)-chlorophyllide a (DV-Chlidea). Very low activity with
CC (3,8-divinyl)-protochlorophyllide a (DV-Pchlidea) and (3,8-divinyl)-
CC magnesium-protoporphyrin IX monomethyl ester (DV-MPE). No activity with
CC (3,8-divinyl)-chlorophyllide b (DV-Chlideb), (3,8-divinyl)-magnesium-
CC protoporphyrin IX (DV-Mg-Proto) and either (3,8-divinyl)-chlorophyll a
CC (DV-Chla) or b (DV-Chlb). {ECO:0000269|PubMed:15632054,
CC ECO:0000269|PubMed:15695432, ECO:0000269|PubMed:17991629,
CC ECO:0000269|PubMed:23154534}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + protochlorophyllide a = 3,8-divinyl
CC protochlorophyllide a + H(+) + NADPH; Xref=Rhea:RHEA:48884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58632, ChEBI:CHEBI:83350; EC=1.3.1.75;
CC Evidence={ECO:0000269|PubMed:15632054, ECO:0000269|PubMed:17991629};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:17991629,
CC ECO:0000269|PubMed:23154534};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:17991629, ECO:0000269|PubMed:23154534};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15695432}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, stems and flower buds.
CC Detected in roots. {ECO:0000269|PubMed:15695432}.
CC -!- DISRUPTION PHENOTYPE: Pale-green leaves with a reduced amount of
CC chlorophylls a and b, and an accumulation of divinyl chlorophylls.
CC Severe reduction of grana stacks in chloroplasts.
CC {ECO:0000269|PubMed:15695432}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC051627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92595.1; -; Genomic_DNA.
DR EMBL; AK117151; BAC41829.1; -; mRNA.
DR EMBL; BT025627; ABF59045.1; -; mRNA.
DR EMBL; AY085692; AAM62911.1; -; mRNA.
DR RefSeq; NP_197367.1; NM_121871.3.
DR AlphaFoldDB; Q1H537; -.
DR SMR; Q1H537; -.
DR BioGRID; 17260; 1.
DR IntAct; Q1H537; 1.
DR STRING; 3702.AT5G18660.1; -.
DR iPTMnet; Q1H537; -.
DR PaxDb; Q1H537; -.
DR PRIDE; Q1H537; -.
DR ProteomicsDB; 224661; -.
DR EnsemblPlants; AT5G18660.1; AT5G18660.1; AT5G18660.
DR GeneID; 831984; -.
DR Gramene; AT5G18660.1; AT5G18660.1; AT5G18660.
DR KEGG; ath:AT5G18660; -.
DR Araport; AT5G18660; -.
DR TAIR; locus:2180019; AT5G18660.
DR eggNOG; KOG1203; Eukaryota.
DR HOGENOM; CLU_043999_1_0_1; -.
DR InParanoid; Q1H537; -.
DR OMA; FARIGKY; -.
DR OrthoDB; 707551at2759; -.
DR PhylomeDB; Q1H537; -.
DR BioCyc; MetaCyc:MON-11752; -.
DR BRENDA; 1.3.1.75; 399.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q1H537; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1H537; baseline and differential.
DR Genevisible; Q1H537; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0051744; F:3,8-divinyl protochlorophyllide a 8-vinyl reductase activity; IDA:TAIR.
DR GO; GO:0033728; F:divinyl chlorophyllide a 8-vinyl-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
DR InterPro; IPR044201; DVR-like.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR47378; PTHR47378; 1.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..417
FT /note="Divinyl chlorophyllide a 8-vinyl-reductase,
FT chloroplastic"
FT /id="PRO_0000422534"
FT MUTAGEN 333
FT /note="P->L: Decreased catalytic activity, accumulation of
FT divinyl chlorophylls and pale green mutant."
FT /evidence="ECO:0000269|PubMed:15632054"
FT CONFLICT 380
FT /note="G -> E (in Ref. 7; AAM62911)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="E -> G (in Ref. 5; BAC41829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 45893 MW; 77F250E113087981 CRC64;
MSLCSSFNVF ASYSPKPKTI FKDSKFISQF QVKSSPLAST FHTNESSTSL KYKRARLKPI
SSLDSGISEI ATSPSFRNKS PKDINVLVVG STGYIGRFVV KEMIKRGFNV IAVAREKSGI
RGKNDKEETL KQLQGANVCF SDVTELDVLE KSIENLGFGV DVVVSCLASR NGGIKDSWKI
DYEATKNSLV AGKKFGAKHF VLLSAICVQK PLLEFQRAKL KFEAELMDLA EQQDSSFTYS
IVRPTAFFKS LGGQVEIVKD GKPYVMFGDG KLCACKPISE QDLAAFIADC VLEENKINQV
LPIGGPGKAL TPLEQGEILF KILGREPKFL KVPIEIMDFV IGVLDSIAKI FPSVGEAAEF
GKIGRYYAAE SMLILDPETG EYSEEKTPSY GKDTLEDFFA KVIREGMAGQ ELGEQFF
