ID   DCVR_MAIZE              Reviewed;         401 AA.
AC   B6SZW0;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic;
DE            EC=1.3.1.75 {ECO:0000269|PubMed:23154534};
DE   Flags: Precursor;
GN   Name=DVR; Synonyms=PCB2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, 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. Can use (3,8-divinyl)-
CC       chlorophyllide a (DV-Chlidea) > (3,8-divinyl)-chlorophyll a (DV-Chla) >
CC       (3,8-divinyl)-protochlorophyllide a (DV-Pchlidea) > (3,8-divinyl)-
CC       magnesium-protoporphyrin IX monomethyl ester (DV-MPE) > (3,8-divinyl)-
CC       magnesium-protoporphyrin IX (DV-Mg-Proto) as substrates.
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:23154534};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
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DR   EMBL; EU958275; ACG30393.1; -; mRNA.
DR   RefSeq; NP_001148282.1; NM_001154810.1.
DR   AlphaFoldDB; B6SZW0; -.
DR   SMR; B6SZW0; -.
DR   STRING; 4577.GRMZM2G063048_P01; -.
DR   GeneID; 100281890; -.
DR   KEGG; zma:100281890; -.
DR   eggNOG; KOG1203; Eukaryota.
DR   OrthoDB; 707551at2759; -.
DR   BRENDA; 1.3.1.75; 6752.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; B6SZW0; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0051744; F:3,8-divinyl protochlorophyllide a 8-vinyl reductase activity; IEA:EnsemblPlants.
DR   GO; GO:0033728; F:divinyl chlorophyllide a 8-vinyl-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
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..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           55..401
FT                   /note="Divinyl chlorophyllide a 8-vinyl-reductase,
FT                   chloroplastic"
FT                   /id="PRO_0000422537"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  43230 MW;  A7A396B84228C5C0 CRC64;
     MATILLSSRL PTTGTATPSP TRPAPRFLSF PGTAIRRRGR GPLLASSAVS PPAPASAAQP
     YRALPASETT VLVTGATGYI GRYVVWELLR RGHRVLAVAR SRSGIRGRNS PDDVVADLAP
     AQVVFSDVTD PAALLADLAP HGPVHAAVCC LASRGGGVQD SWRVDYRATL HTLQAARGLG
     AAHFVLLSAI CVQKPLLEFQ RAKLKFEEEL AAEAARDPSF TYSVVRPTAF FKSLGGQVDI
     VKNGQPYVMF GDGKLCACKP ISEEDLAAFI ADCIYDQDKA NKVLPIGGPG KALTPLEQGE
     MLFRLLGREP KFIKVPIQIM DAVIWVLDGL AKLFPGLEDA AEFGKIGRYY ASESMLLLDP
     ETGEYSDEKT PSYGKDTLEQ FFQRVIREGM AGQELGEQTI F