ID D3D4Z7_9ACTN Unreviewed; 319 AA.
AC D3D4Z7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000256|HAMAP-Rule:MF_00191};
DE Short=HMBPP reductase {ECO:0000256|HAMAP-Rule:MF_00191};
DE EC=1.17.7.4 {ECO:0000256|HAMAP-Rule:MF_00191};
GN Name=ispH {ECO:0000256|HAMAP-Rule:MF_00191};
GN ORFNames=FrEUN1fDRAFT_4869 {ECO:0000313|EMBL:EFC81988.1};
OS Parafrankia sp. EUN1f.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC81988.1, ECO:0000313|Proteomes:UP000004777};
RN [1] {ECO:0000313|EMBL:EFC81988.1, ECO:0000313|Proteomes:UP000004777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUN1f {ECO:0000313|EMBL:EFC81988.1,
RC ECO:0000313|Proteomes:UP000004777};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA Fernandez M., Tisa L.;
RT "The draft genome of Frankia sp. EUN1f.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00191};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00191};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00191}.
CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000256|HAMAP-
CC Rule:MF_00191}.
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:EFC81988.1}.
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; ADGX01000087; EFC81988.1; -; Genomic_DNA.
DR RefSeq; WP_006542731.1; NZ_ADGX01000087.1.
DR AlphaFoldDB; D3D4Z7; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR Proteomes; UP000004777; Unassembled WGS sequence.
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 Gene3D; 3.40.50.11270; -; 1.
DR Gene3D; 3.40.1010.20; 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain; 2.
DR HAMAP; MF_00191; IspH; 1.
DR InterPro; IPR003451; LytB/IspH.
DR NCBIfam; TIGR00216; ispH_lytB; 1.
DR PANTHER; PTHR30426; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR30426:SF0; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF02401; LYTB; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00191};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00191};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00191}; Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00191};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00191};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191,
KW ECO:0000313|EMBL:EFC81988.1}.
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 97
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 223..225
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
SQ SEQUENCE 319 AA; 34478 MW; 4558712A89D99A97 CRC64;
MGRVLLAKPR GYCAGVDRAV QTVEKALDLY GSPVYVRKQI VHNAHVVKTL EAKGAIFVEE
TDEVPVGATV VFSAHGVAPT VHEEASSRQL RTIDATCPLV TKVHSEARRF AKEDLDILLI
GHEGHEEVVG TTGQAPDRIH LVDGPEDAAA VKVRDPKRVA FLSQTTLSVD ETMTTVNALR
ERFPHLQGPP NSDICYATQN RQVAVKEIAE KVDLLIVVGS PNSSNSVRLV EVALDAGAPK
SFLVDDSTEV DESWLDGVET VGVTSGASVP EELVTGVMAW LAERGFNDVE EVTSADEHLL
FALPPELRRD IRAKERAAG
//
