ID A0A074MWT9_ERYLO Unreviewed; 318 AA.
AC A0A074MWT9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic {ECO:0000256|ARBA:ARBA00024089};
DE EC=1.3.1.75 {ECO:0000256|ARBA:ARBA00024059};
GN ORFNames=EH31_08190 {ECO:0000313|EMBL:KEO90062.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO90062.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO90062.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO90062.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023990};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005173}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEO90062.1}.
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DR EMBL; JMIW01000003; KEO90062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074MWT9; -.
DR STRING; 1044.EH31_08190; -.
DR eggNOG; COG0702; Bacteria.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000027647; Unassembled WGS sequence.
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 CDD; cd05243; SDR_a5; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR044201; DVR-like.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR47378; DIVINYL CHLOROPHYLLIDE A 8-VINYL-REDUCTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47378:SF1; DIVINYL CHLOROPHYLLIDE A 8-VINYL-REDUCTASE, CHLOROPLASTIC; 1.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000027647};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 17..205
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF13460"
SQ SEQUENCE 318 AA; 34195 MW; 6423D5F403DE58D0 CRC64;
MSITTTTIAR KSIAVAGASG TIGRAVVREC VSRGYDVTAL VRSEAAAQLP ELEGAQVTTV
DVSDPDALAR VFKEAVPDTV ISCIASRSGS PKDAKAIDLD ANLNLLLGAQ AARTQHFILL
SAICVQRPRL AFQRAKLAFE AALTDAPIEH TIVRPTAFFK SLSGQVERVR EGKPFFLFGD
GELTACKPIS DADLARFIVA QADDPKAYGA TLPIGGPGPA ITLKRQGEIL FEAAGREPRF
RRVPVGLFSL FGGVFSLGAW ASDWLAEKAE YARIAEYYAT QSMLVWDDER RAYDADATPE
FGSDTLADHY ARLLGKTN
//