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Database: UniProt
Entry: A0A066RMY0_9GAMM
LinkDB: A0A066RMY0_9GAMM
Original site: A0A066RMY0_9GAMM 
ID   A0A066RMY0_9GAMM        Unreviewed;       316 AA.
AC   A0A066RMY0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:KDM90491.1};
GN   ORFNames=EA58_17350 {ECO:0000313|EMBL:KDM90491.1};
OS   Photobacterium galatheae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=1654360 {ECO:0000313|EMBL:KDM90491.1, ECO:0000313|Proteomes:UP000027192};
RN   [1] {ECO:0000313|EMBL:KDM90491.1, ECO:0000313|Proteomes:UP000027192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2753 {ECO:0000313|EMBL:KDM90491.1,
RC   ECO:0000313|Proteomes:UP000027192};
RA   Machado H.R., Gram L.;
RT   "Draft genome sequence of Photobacterium halotolerans S2753: a solonamide,
RT   ngercheumicin and holomycin producer.";
RL   Submitted (APR-2014) 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:KDM90491.1}.
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DR   EMBL; JMIB01000032; KDM90491.1; -; Genomic_DNA.
DR   RefSeq; WP_036755277.1; NZ_JMIB01000032.1.
DR   AlphaFoldDB; A0A066RMY0; -.
DR   STRING; 1654360.EA58_17350; -.
DR   OrthoDB; 9804068at2; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000027192; 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:KDM90491.1}.
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         12
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         96
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         199
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         227..229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
SQ   SEQUENCE   316 AA;  34604 MW;  DE53284F38F6D939 CRC64;
     MKILLANPRG FCAGVDRAIS IVERALELYQ PPIYVRHEVV HNRFVVEGLK QRGAIFVEEL
     TEVPDDNIVI FSAHGVSQAV RNEAKARKLT VFDATCPLVT KVHMEVARAS RRNMEVVLIG
     HAGHPEVEGT MGQYASETGG MYLVETPADV DKLTTVVKDP GNLHYVSQTT LSVDETADVI
     DRLREVFPDI QGPRKDDICY ATQNRQDAVR EMAASVDVMI VVGSKNSSNS NRLRELAEKL
     GTPSFLTDCA EDVDANWFTG TQSVGVTAGA SAPEALVNQI IARIQALAGG EVEELSGREE
     NMFFEVPREL QVKNVG
//
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