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4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) (EC 1.17.7.4)

 ISPH_EHRRW              Reviewed;         328 AA.
Q5HB13; Q5FEL8;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
20-JUN-2018, entry version 81.
RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000255|HAMAP-Rule:MF_00191};
Short=HMBPP reductase {ECO:0000255|HAMAP-Rule:MF_00191};
EC=1.17.7.4 {ECO:0000255|HAMAP-Rule:MF_00191};
Name=ispH {ECO:0000255|HAMAP-Rule:MF_00191};
OrderedLocusNames=Erum5180, ERWE_CDS_05430;
Ehrlichia ruminantium (strain Welgevonden).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Anaplasmataceae; Ehrlichia.
NCBI_TaxID=254945;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Welgevonden;
PubMed=15637156; DOI=10.1073/pnas.0406633102;
Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R.,
Allsopp M.T., Allsopp B.A.;
"The genome of the heartwater agent Ehrlichia ruminantium contains
multiple tandem repeats of actively variable copy number.";
Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Welgevonden;
PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006;
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J.,
Martinez D.;
"Comparative genomic analysis of three strains of Ehrlichia
ruminantium reveals an active process of genome size plasticity.";
J. Bacteriol. 188:2533-2542(2006).
-!- FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-
butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl
diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in
the terminal step of the DOXP/MEP pathway for isoprenoid precursor
biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00191}.
-!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized
ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-
methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-
sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}.
-!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized
ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-
methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-
sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000255|HAMAP-Rule:MF_00191};
Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
Rule:MF_00191};
-!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-
methylbutenyl diphosphate: step 1/1. {ECO:0000255|HAMAP-
Rule:MF_00191}.
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000255|HAMAP-
Rule:MF_00191}.
-!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP-
Rule:MF_00191}.
-!- SEQUENCE CAUTION:
Sequence=CAI27037.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; CR767821; CAH58247.1; -; Genomic_DNA.
EMBL; CR925678; CAI27037.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_011155198.1; NC_006832.1.
SMR; Q5HB13; -.
STRING; 254945.ERWE_CDS_05430; -.
EnsemblBacteria; CAH58247; CAH58247; Erum5180.
EnsemblBacteria; CAI27037; CAI27037; ERWE_CDS_05430.
GeneID; 33058245; -.
KEGG; eru:Erum5180; -.
KEGG; erw:ERWE_CDS_05430; -.
eggNOG; ENOG4105C48; Bacteria.
eggNOG; COG0761; LUCA.
HOGENOM; HOG000220192; -.
KO; K03527; -.
OrthoDB; POG091H038O; -.
BioCyc; ERUM254945:ERUM_RS02825-MONOMER; -.
UniPathway; UPA00056; UER00097.
UniPathway; UPA00059; UER00105.
Proteomes; UP000001021; Chromosome.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
CDD; cd13944; lytB_ispH; 1.
HAMAP; MF_00191; IspH; 1.
InterPro; IPR003451; LytB/IspH.
PANTHER; PTHR30426; PTHR30426; 1.
Pfam; PF02401; LYTB; 1.
TIGRFAMs; TIGR00216; ispH_lytB; 1.
3: Inferred from homology;
4Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis;
Metal-binding; Oxidoreductase.
CHAIN 1 328 4-hydroxy-3-methylbut-2-enyl diphosphate
reductase.
/FTId=PRO_0000128816.
REGION 236 238 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00191}.
ACT_SITE 140 140 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_00191}.
METAL 24 24 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_00191}.
METAL 110 110 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_00191}.
METAL 208 208 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_00191}.
BINDING 55 55 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00191}.
BINDING 88 88 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00191}.
BINDING 138 138 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00191}.
BINDING 178 178 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00191}.
BINDING 279 279 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00191}.
SEQUENCE 328 AA; 37020 MW; F28E64D0D13BE2DC CRC64;
MHNAIYTDLQ KEVEVILARP RGFCAGVSRA IEIVKLAIEY YKDTKTIYVL HEIVHNKYIV
ETLKTMGVIF IDKVDQAQDG SVLIYSAHGV SKSIKQLAEL RDLEVIDATC PLVNKVHKEV
QLYDKSGYQV ILIGHKGHRE VEGTVGQIST PVIIVQNLND IDKIEIFDPD KLAYVTQTTL
SVDDTKVIID KLKKKFPNIK GPDLKDICYA TQNRQTTTKR LAELVDIVFI LGSKNSSNSN
RLKELAGIQT QAFLIDSYKE IDLNLLNDIT KIGITAGASA PDILVQQVID FLKQHMKVKL
SDLEIVQESV TFNVPRQLRQ YKEQYNPI


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