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Database: UniProt
Entry: G8UPY4_TANFA
LinkDB: G8UPY4_TANFA
Original site: G8UPY4_TANFA 
ID   G8UPY4_TANFA            Unreviewed;       288 AA.
AC   G8UPY4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 65.
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:AEW21173.1};
GN   OrderedLocusNames=BFO_0949 {ECO:0000313|EMBL:AEW21173.1};
OS   Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS   5666 / FDC 338) (Bacteroides forsythus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Tannerella.
OX   NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW21173.1, ECO:0000313|Proteomes:UP000005436};
RN   [1] {ECO:0000313|Proteomes:UP000005436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC   {ECO:0000313|Proteomes:UP000005436};
RA   Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA   Shetty J., Torralba M., Gill S., Nelson K.;
RT   "Complete sequence of Tannerella forsythia ATCC 43037.";
RL   Submitted (DEC-2011) 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; CP003191; AEW21173.1; -; Genomic_DNA.
DR   RefSeq; WP_014224374.1; NC_016610.1.
DR   AlphaFoldDB; G8UPY4; -.
DR   STRING; 203275.BFO_0949; -.
DR   GeneID; 34758232; -.
DR   KEGG; tfo:BFO_0949; -.
DR   PATRIC; fig|203275.8.peg.850; -.
DR   eggNOG; COG0761; Bacteria.
DR   HOGENOM; CLU_027486_0_1_10; -.
DR   OMA; DSICRQV; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000005436; 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   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:AEW21173.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005436}.
FT   ACT_SITE        131
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         41
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         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         198
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         226..228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
SQ   SEQUENCE   288 AA;  32176 MW;  961D2DBF65466DD8 CRC64;
     MVEVTIDRGS GFCFGVVKAI QSAERELKQT DELYSLGDLV HNSLEMERLK ALGLHTIGHA
     DLAHLRNRTV LLRAHGEPPS TYALAQKNQI KIIDATCPVV LQLQKRIHRC YQETKEYGTQ
     LVIYGKKGHA EVNGLVGQTE GTAIVIEKLD DIEKLDFHRD IILFSQTTKP LDGFGKVVEG
     IRARISSDVT FQYFDTICRQ VANRLPNIRD FALQHDCIYF VAGKKSSNGQ MLFEQCLQAN
     PHSVFITSAA DIAEPLPEDI RSVGICGATS TPKWLMEEVA ERVKMLNP
//
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