(data stored in ACNUC1104 zone)

SWISSPROT: ISPH_STRCO

ID   ISPH_STRCO              Reviewed;         338 AA.
AC   Q9FBM1; Q9ADE9;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   16-JAN-2019, entry version 103.
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}; Synonyms=lytB;
GN   OrderedLocusNames=SCO5058; ORFNames=SCBAC20F6.01, SCK7.31;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-
CC       butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl
CC       diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in
CC       the terminal step of the DOXP/MEP pathway for isoprenoid precursor
CC       biosynthesis. {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
CC         H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24488,
CC         Rhea:RHEA-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
CC         H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24825,
CC         Rhea:RHEA-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-
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   -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00191}.
DR   EMBL; AL939122; CAD55221.1; -; Genomic_DNA.
DR   RefSeq; NP_733653.1; NC_003888.3.
DR   RefSeq; WP_003973920.1; NC_003888.3.
DR   SMR; Q9FBM1; -.
DR   STRING; 100226.SCO5058; -.
DR   PRIDE; Q9FBM1; -.
DR   EnsemblBacteria; CAD55221; CAD55221; CAD55221.
DR   GeneID; 1100499; -.
DR   KEGG; sco:SCO5058; -.
DR   PATRIC; fig|100226.15.peg.5137; -.
DR   eggNOG; ENOG4105C48; Bacteria.
DR   eggNOG; COG0761; LUCA.
DR   HOGENOM; HOG000220192; -.
DR   InParanoid; Q9FBM1; -.
DR   KO; K03527; -.
DR   OMA; HNKYVVD; -.
DR   PhylomeDB; Q9FBM1; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000001973; 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;
DR   PRODOM; Q9FBM1.
DR   SWISS-2DPAGE; Q9FBM1.
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN         1    338       4-hydroxy-3-methylbut-2-enyl diphosphate
FT                                reductase.
FT                                /FTId=PRO_0000128875.
FT   REGION      231    233       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   ACT_SITE    135    135       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL        21     21       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       105    105       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       203    203       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      50     50       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      83     83       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING     133    133       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING     173    173       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING     276    276       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00191}.
SQ   SEQUENCE   338 AA;  36609 MW;  07EDFF4D2D938E98 CRC64;
     MGAMTASPGR RVLLAAPRGY CAGVDRAVIA VEKALEQYGA PVYVRHEIVH NKYVVQTLEK
     KGAIFVERTE EVPEGNIVMF SAHGVAPVVH EEAERGKLAT IDATCPLVTK VHKEAVRFAN
     DDYDILLIGH EGHEEVIGTS GEAPDHIQLV DGPEDVAKVE VRDPSKVVWL SQTTLSVDET
     METVDALKDK FPQLISPPSD DICYATQNRQ LAVKQMGAEA ELVIVVGSRN SSNSKRLVEV
     AKQAGSRAAY LVDFADEIDE TWLDGVTTVG VTSGASVPDV LVEQVLEWLS RRGFEDVEIV
     KAAEESIIFS LPKELRRDLR EEAASLVAER GGSGTAGA
//

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