ISPH_GLOC7
ID ISPH_GLOC7 Reviewed; 402 AA.
AC B7KEG3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000255|HAMAP-Rule:MF_00191};
DE Short=HMBPP reductase {ECO:0000255|HAMAP-Rule:MF_00191};
DE EC=1.17.7.4 {ECO:0000255|HAMAP-Rule:MF_00191};
GN Name=ispH {ECO:0000255|HAMAP-Rule:MF_00191};
GN OrderedLocusNames=PCC7424_4926;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
CC -!- FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl
CC 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP)
CC and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the
CC DOXP/MEP pathway for isoprenoid precursor biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00191}.
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:0000255|HAMAP-Rule:MF_00191};
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:0000255|HAMAP-Rule:MF_00191};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00191};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00191};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-
CC methylbutenyl diphosphate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00191}.
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:0000255|HAMAP-Rule:MF_00191}.
CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP-
CC Rule:MF_00191}.
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DR EMBL; CP001291; ACK73281.1; -; Genomic_DNA.
DR RefSeq; WP_015956862.1; NC_011729.1.
DR AlphaFoldDB; B7KEG3; -.
DR SMR; B7KEG3; -.
DR STRING; 65393.PCC7424_4926; -.
DR EnsemblBacteria; ACK73281; ACK73281; PCC7424_4926.
DR KEGG; cyc:PCC7424_4926; -.
DR eggNOG; COG0761; Bacteria.
DR HOGENOM; CLU_027486_4_0_3; -.
DR OMA; HNKYVVD; -.
DR OrthoDB; 1235756at2; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR Proteomes; UP000002384; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..402
FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase"
FT /id="PRO_1000118602"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 288
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 317..319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
SQ SEQUENCE 402 AA; 45676 MW; D5617890D0206CFD CRC64;
MDTKAFKRSL QQSENYHRKG FGQEDEAMGV MNSEYQSSLI QEIRNNNYRL TQGDVTIRLA
EAFGFCWGVE RAVAMSYETR QHFPNQRIWL TNEVIHNPSV NQRLRDMKVE FIPVIEDQKD
FSVVERDDVV ILPAFGASVT EMQLLNDKGC TIVDTTCPWV AKVWNSVEKH KKRNYTSIIH
GKYKHEETVA TSSFAGTYLV VLNMEQAKYV CNYILNGGDK QEFLAKFKKA YSEGFDPDTD
LERVGIANQT TMLKSETEEI GKLFEHTMLK KYGPLDLNNH FMSFNTICDA TQERQDAMLD
LVKEKLDLMV VIGGFNSSNT THLQEISIHH GIVSYHIDSA ARIDLNNHIE HKPLGKDLEV
KENWLPDGKI VVGVTSGAST PDIVVEQVLQ KIFAIKSAVA MV
