(data stored in ACNUC7421 zone)

SWISSPROT: ISPH_ECODH

ID   ISPH_ECODH              Reviewed;         316 AA.
AC   B1XBF4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 66.
DE   RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate 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};
GN   OrderedLocusNames=ECDH10B_0030;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate
CC       into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate
CC       (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00191}.
CC   -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized
CC       ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-
CC       methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-
CC       sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}.
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized
CC       ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-
CC       methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-
CC       sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00191};
CC       Note=Binds 1 [3Fe-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-
CC       Rule:MF_00191}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000255|HAMAP-
CC       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; CP000948; ACB01234.1; -; Genomic_DNA.
DR   RefSeq; WP_001166395.1; NC_010473.1.
DR   ProteinModelPortal; B1XBF4; -.
DR   SMR; B1XBF4; -.
DR   EnsemblBacteria; ACB01234; ACB01234; ECDH10B_0030.
DR   KEGG; ecd:ECDH10B_0030; -.
DR   eggNOG; ENOG4105C48; Bacteria.
DR   eggNOG; COG0761; LUCA.
DR   HOGENOM; HOG000220192; -.
DR   KO; K03527; -.
DR   OMA; TKVHKEA; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
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; B1XBF4.
DR   SWISS-2DPAGE; B1XBF4.
KW   3Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    316       4-hydroxy-3-methylbut-2-enyl diphosphate
FT                                reductase.
FT                                /FTId=PRO_1000098946.
FT   REGION      225    227       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL        12     12       Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL        96     96       Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       197    197       Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      41     41       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      74     74       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING     124    124       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING     167    167       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING     269    269       Substrate. {ECO:0000255|HAMAP-
FT                                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
//

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