ID   A0A1I5KDG4_9RHOB        Unreviewed;       316 AA.
AC   A0A1I5KDG4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 7.
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   ORFNames=SAMN04488047_10137 {ECO:0000313|EMBL:SFO83028.1};
OS   Tranquillimonas alkanivorans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=441119 {ECO:0000313|EMBL:SFO83028.1, ECO:0000313|Proteomes:UP000199356};
RN   [1] {ECO:0000313|EMBL:SFO83028.1, ECO:0000313|Proteomes:UP000199356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19547 {ECO:0000313|EMBL:SFO83028.1,
RC   ECO:0000313|Proteomes:UP000199356};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOXA01000001; SFO83028.1; -; Genomic_DNA.
DR   BioCyc; GCF_900115595:BM162_RS00185-MONOMER; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000199356; Unassembled WGS sequence.
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;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS01001097};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199356};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199356}.
FT   REGION      228    230       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   ACT_SITE    131    131       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   METAL        17     17       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       101    101       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      46     46       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING      79     79       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     129    129       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   316 AA;  34137 MW;  D4C06A17C9EA8339 CRC64;
     MTKPPLTLYL AAPRGFCAGV DRAIKIVEMA LEKWGAPVYV RHEIVHNRYV VDGLREKGAV
     FVEELDECPD DRPVIFSAHG VPKAVPAEAA KREMVYVDAT CPLVSKVHIE AERHHENGLQ
     MIMIGHAGHP ETVGTMGQLP AGEVLLVETD EDVAGLDVRD PDKLAFITQT TLSVDDTAGI
     VAALQARFPN IVGPHKEDIC YATTNRQAAV KAMAPHADAM LVIGAPNSSN SKRLVEVGRG
     AGCGYAQLVQ RADDIDWRAL EGIGSIGITA GASAPEVLVN EVLDAFRDRF DVTVEQVETA
     QENVEFKVPR VLRVPA
//