(data stored in SCRATCH zone)

SWISSPROT: Q47SQ8_THEFY

ID   Q47SQ8_THEFY            Unreviewed;       333 AA.
AC   Q47SQ8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 106.
DE   RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS01001099};
DE            Short=HMBPP reductase {ECO:0000256|HAMAP-Rule:MF_00191};
DE            EC=1.17.7.4 {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS01001099};
GN   Name=ispH {ECO:0000256|HAMAP-Rule:MF_00191};
GN   OrderedLocusNames=Tfu_0471 {ECO:0000313|EMBL:AAZ54509.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54509.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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:0000256|HAMAP-Rule:MF_00191,
CC       ECO:0000256|SAAS:SAAS01001098}.
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:0000256|HAMAP-Rule:MF_00191,
CC         ECO:0000256|SAAS:SAAS01125179};
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:0000256|HAMAP-Rule:MF_00191,
CC         ECO:0000256|SAAS:SAAS01125177};
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-
CC       Rule:MF_00191, ECO:0000256|SAAS:SAAS01001092}.
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:0000256|HAMAP-
CC       Rule:MF_00191, ECO:0000256|SAAS:SAAS01001076}.
CC   -!- SIMILARITY: Belongs to the IspH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00191, ECO:0000256|SAAS:SAAS01001094}.
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DR   EMBL; CP000088; AAZ54509.1; -; Genomic_DNA.
DR   RefSeq; WP_011290918.1; NC_007333.1.
DR   STRING; 269800.Tfu_0471; -.
DR   EnsemblBacteria; AAZ54509; AAZ54509; Tfu_0471.
DR   KEGG; tfu:Tfu_0471; -.
DR   eggNOG; ENOG4105C48; Bacteria.
DR   eggNOG; COG0761; LUCA.
DR   HOGENOM; HOG000220192; -.
DR   KO; K03527; -.
DR   OMA; HNKYVVD; -.
DR   OrthoDB; 1311145at2; -.
DR   BioCyc; TFUS269800:G1G4Q-478-MONOMER; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000000434; 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; Q47SQ8.
DR   SWISS-2DPAGE; Q47SQ8.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS01001097};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00772206};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS00772258};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS01001084};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS00772260};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS01001093, ECO:0000313|EMBL:AAZ54509.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   REGION      228    230       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   ACT_SITE    132    132       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   METAL        18     18       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       102    102       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       200    200       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      47     47       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING      80     80       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     130    130       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     273    273       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
SQ   SEQUENCE   333 AA;  36708 MW;  DA176D6437169696 CRC64;
     MTATNRRRVL LAKPRGYCAG VDRAIHTVEK ALEQYGPPIY VRKQIVHNTH VVRTLEERGV
     IFVEETSEVP EGATVVFSAH GVSPQVHKEA AERKLRTIDA ACPLVTKVHK EAQRFAAEDL
     DIILIGHEGH EEVEGTSGHA PEHIQIVDSP EEVANIKVRD PNRVAWLSQT TLSVDETNAT
     VQALRERFPN LIDPPSDDIC YATSNRQAAV KAIAPQCDLF IVVGSSNSSN SVRLVEVARD
     AGARASYLVD NATYLKEEWL EGVTTIGVSS GASVPEILVR ELLERLATYG FTDVEEVETE
     REKITFALPR ELRTRRSKND KSLVGKPLPV SPA
//

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