(data stored in SCRATCH3701 zone)

SWISSPROT: ISPH_ECOBW

ID   ISPH_ECOBW              Reviewed;         316 AA.
AC   C4ZPV5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 63.
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=BWG_0027;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00191}.
CC   -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00191}.
DR   EMBL; CP001396; ACR61738.1; -; Genomic_DNA.
DR   RefSeq; WP_001166395.1; NC_012759.1.
DR   SMR; C4ZPV5; -.
DR   EnsemblBacteria; ACR61738; ACR61738; BWG_0027.
DR   KEGG; ebw:BWG_0027; -.
DR   HOGENOM; HOG000220192; -.
DR   KO; K03527; -.
DR   OMA; HNKYVVD; -.
DR   BioCyc; ECOL595496:BWG_RS00140-MONOMER; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
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;
DR   PRODOM; C4ZPV5.
DR   SWISS-2DPAGE; C4ZPV5.
KW   4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..316
FT                   /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase"
FT                   /id="PRO_1000204001"
FT   REGION          225..227
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   METAL           12
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   METAL           96
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   METAL           197
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         41
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         74
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         124
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         167
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         269
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
SQ   SEQUENCE   316 AA;  34775 MW;  0E7B378BD49AB771 CRC64;
     MQILLANPRG FCAGVDRAIS IVENALAIYG APIYVRHEVV HNRYVVDSLR ERGAIFIEQI
     SEVPDGAILI FSAHGVSQAV RNEAKSRDLT VFDATCPLVT KVHMEVARAS RRGEESILIG
     HAGHPEVEGT MGQYSNPEGG MYLVESPDDV WKLTVKNEEK LSFMTQTTLS VDDTSDVIDA
     LRKRFPKIVG PRKDDICYAT TNRQEAVRAL AEQAEVVLVV GSKNSSNSNR LAELAQRMGK
     RAFLIDDAKD IQEEWVKEVK CVGVTAGASA PDILVQNVVA RLQQLGGGEA IPLEGREENI
     VFEVPKELRV DIREVD
//

If you have problems or comments...

PBIL Back to PBIL home page