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ISPH_BACFN
ID   ISPH_BACFN              Reviewed;         290 AA.
AC   Q5L9K3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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}; OrderedLocusNames=BF3536;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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; CR626927; CAH09224.1; -; Genomic_DNA.
DR   RefSeq; WP_005797949.1; NC_003228.3.
DR   AlphaFoldDB; Q5L9K3; -.
DR   SMR; Q5L9K3; -.
DR   STRING; 272559.BF9343_3443; -.
DR   DNASU; 3286026; -.
DR   EnsemblBacteria; CAH09224; CAH09224; BF9343_3443.
DR   GeneID; 66331619; -.
DR   KEGG; bfs:BF9343_3443; -.
DR   eggNOG; COG0761; Bacteria.
DR   HOGENOM; CLU_027486_0_1_10; -.
DR   OMA; NDSICRQ; -.
DR   OrthoDB; 1235756at2; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000006731; 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   PANTHER; PTHR30426; PTHR30426; 1.
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..290
FT                   /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase"
FT                   /id="PRO_1000021088"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         13
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         97
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         198
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         226..228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
SQ   SEQUENCE   290 AA;  32869 MW;  F7BB95CC5E361E2D CRC64;
     MVKVEIDEGS GFCFGVVTAI HKAEEELAKG VTLYCLGDIV HNSREVERLK EMGLITINHE
     EFKQLHNAKV LLRAHGEPPE TYIIAKENNI EIIDATCPVV LRLQKRIKQE YMQEDLDEKQ
     IVIYGKNGHA EVLGLVGQTT GKAIVIEKLD EARRLDFSKS IRLYSQTTKS LDEFWEIVEY
     IKEHISPDVT FEYYDTICRQ VANRMPNLRK FAASHDLIFF VSGKKSSNGK MLFEECKKVN
     PNSHLIDSAD EIDDSLLPGV NSIGVCGATS TPKWLMEEIS EAIKAQIKRQ
 
 
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