ID A0A0F7KS99_9SPHN Unreviewed; 324 AA.
AC A0A0F7KS99;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ECO:0000313|EMBL:AKH42434.1};
GN ORFNames=FHS61_000204 {ECO:0000313|EMBL:MBB5731211.1}, WYH_01393
GN {ECO:0000313|EMBL:AKH42434.1};
OS Croceibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH42434.1, ECO:0000313|Proteomes:UP000034392};
RN [1] {ECO:0000313|EMBL:AKH42434.1, ECO:0000313|Proteomes:UP000034392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26DY36 {ECO:0000313|EMBL:AKH42434.1,
RC ECO:0000313|Proteomes:UP000034392};
RA Wu Y.-H., Cheng H., Wu X.-W.;
RT "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5731211.1, ECO:0000313|Proteomes:UP000556014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100738 {ECO:0000313|EMBL:MBB5731211.1,
RC ECO:0000313|Proteomes:UP000556014};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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}.
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DR EMBL; CP011452; AKH42434.1; -; Genomic_DNA.
DR EMBL; JACIJL010000001; MBB5731211.1; -; Genomic_DNA.
DR RefSeq; WP_046903251.1; NZ_JACIJL010000001.1.
DR AlphaFoldDB; A0A0F7KS99; -.
DR STRING; 1267766.WYH_01393; -.
DR KEGG; aay:WYH_01393; -.
DR PATRIC; fig|1267766.3.peg.1401; -.
DR OrthoDB; 9804068at2; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR Proteomes; UP000034392; Chromosome.
DR Proteomes; UP000556014; 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:AKH42434.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034392}.
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 239..241
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
SQ SEQUENCE 324 AA; 35296 MW; 7C849AA267F25C26 CRC64;
MNAPFQDTPA GQARDALTVL IAAPRGFCAG VDRAIEIVER AIAKYGAPVY VRHEIVHNRF
VVDDLKAKGA IFVEELDEVP DDMPVVFSAH GVPKSVPEEA QRRELTYVDA TCPLVSKVHR
QAERQVEAGR HIVFIGHKGH PEVIGTFGQV PEGQMTLVET VEDVADLDFT ADTPLAFLTQ
TTLSVDDTYK IVAALKDRFP QIVGPKAEDI CYATSNRQMA VKLIAPGSDL VLVIGAPNSS
NSLRLVEVAE RCGTSARLIQ RAMDIDPAWL EGVGTVGITA GASAPETLVR EVVDRLGEWR
DVEEHTLVTA EEKMVFKLPR QLTA
//
