ISPH_BOTBR
ID ISPH_BOTBR Reviewed; 502 AA.
AC A0A2Z5WA18;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic {ECO:0000305};
DE Short=BbHDR {ECO:0000303|PubMed:29725892};
DE EC=1.17.7.4 {ECO:0000305|PubMed:29725892};
DE Flags: Precursor;
GN Name=HDR {ECO:0000303|PubMed:29725892};
GN Synonyms=IspH {ECO:0000312|EMBL:BBB76028.1},
GN LytB {ECO:0000312|EMBL:BBB76028.1};
OS Botryococcus braunii (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Botryococcus.
OX NCBI_TaxID=38881;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Race B;
RX PubMed=29725892; DOI=10.1007/s10265-018-1039-4;
RA Uchida H., Sumimoto K., Oki T., Nishii I., Mizohata E., Matsunaga S.,
RA Okada S.;
RT "Isolation and characterization of 4-hydroxy-3-methylbut-2-enyl diphosphate
RT reductase gene from Botryococcus braunii, race B.";
RL J. Plant Res. 131:839-848(2018).
CC -!- FUNCTION: Enzyme of the plastid non-mevalonate pathway for isoprenoid
CC biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-
CC diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl
CC diphosphate (DMAPP). {ECO:0000305|PubMed:29725892}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+)
CC + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24825, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57623, ChEBI:CHEBI:128753; EC=1.17.7.4;
CC Evidence={ECO:0000305|PubMed:29725892};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-
CC [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+)
CC + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24488, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:128753, ChEBI:CHEBI:128769; EC=1.17.7.4;
CC Evidence={ECO:0000305|PubMed:29725892};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P62623};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P62623};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-
CC methylbutenyl diphosphate: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 6/6. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P62623}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q94B35}.
CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000305}.
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DR EMBL; LC090196; BBB76027.1; -; mRNA.
DR EMBL; LC105995; BBB76028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5WA18; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR CDD; cd13944; lytB_ispH; 1.
DR HAMAP; MF_00191; IspH; 1.
DR InterPro; IPR003451; LytB/IspH.
DR Pfam; PF02401; LYTB; 1.
DR TIGRFAMs; TIGR00216; ispH_lytB; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Isoprene biosynthesis;
KW Metal-binding; Oxidoreductase; Plastid; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..502
FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase,
FT chloroplastic"
FT /id="PRO_0000446507"
FT ACT_SITE 262
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 140
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 363
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 398..400
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
SQ SEQUENCE 502 AA; 55640 MW; D7934165075C374D CRC64;
MQVLPQTRVQ GVPSGRNLSC SKAVGGTPLR ALTRDVVRPA RSVNVHVVAD GESADDVLLR
SSSVAVAEKP KVSGRAFRRS LKDTGRYVAK PINDKDSLDL MEEHGVGYSS VGLVAQMRAN
NNEWRFKDIR VKLASAYGYC WGVERAVQMA YEAKKKYPDR QIHLTNEIIH NPTVNERMTE
MDINIIEQKE NGSKDFSKVS RQDVVILPAF GASVQELSLL KDLEVQIVDT TCPWVSKVWT
AVDNQARKAH TSVIHGKYSH EETIATASFA ETYLIVRDIE EANYVCNYIL NGGNKEEFLT
KFKNAISKGF DPDRDLARVG LANQTTMLRD ETMAIGKLLE KTMIQKHGPA AIKEHFMVMD
TICDATQERQ DAVYQLVGQQ DNPAEKLDLI LVVGGFNSSN TSHLQEIPEL KNIPSFWVNE
AACIDPVNKK ITHRTAHGTM LDTQNWLPDG PVTIGVTSGA STPDRAVEEV LEAVFKTRDA
SFGGIAPNYD LGTAPVVRHE EH
