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Database: UniProt
Entry: A1HTW2_9FIRM
LinkDB: A1HTW2_9FIRM
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ID   A1HTW2_9FIRM            Unreviewed;       655 AA.
AC   A1HTW2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=TcarDRAFT_0216 {ECO:0000313|EMBL:EAX46538.1};
OS   Thermosinus carboxydivorans Nor1.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Thermosinus.
OX   NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX46538.1, ECO:0000313|Proteomes:UP000005139};
RN   [1] {ECO:0000313|EMBL:EAX46538.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX46538.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M., Hauser L.;
RT   "Annotation of the draft genome assembly of Thermosinus
RT   carboxydivorans Nor1.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAX46538.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX46538.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Thermosinus
RT   carboxydivorans Nor1.";
RL   Submitted (JAN-2007) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAX46538.1}.
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DR   EMBL; AAWL01000029; EAX46538.1; -; Genomic_DNA.
DR   RefSeq; WP_007290465.1; NZ_AAWL01000029.1.
DR   STRING; 401526.TcarDRAFT_0216; -.
DR   EnsemblBacteria; EAX46538; EAX46538; TcarDRAFT_0216.
DR   eggNOG; ENOG4105CAV; Bacteria.
DR   eggNOG; COG0539; LUCA.
DR   eggNOG; COG0761; LUCA.
DR   OrthoDB; 1235756at2; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000005139; 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:0003676; F:nucleic acid binding; IEA:InterPro.
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   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF02401; LYTB; 1.
DR   Pfam; PF00575; S1; 4.
DR   SMART; SM00316; S1; 4.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00216; ispH_lytB; 1.
DR   PROSITE; PS50126; S1; 4.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS01001097}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005139};
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:UP000005139}.
FT   DOMAIN      289    358       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      376    442       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      463    531       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      548    617       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      215    217       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   COILED      430    450       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    123    123       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   METAL        12     12       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL        93     93       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       187    187       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      39     39       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING      71     71       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     121    121       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     159    159       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     259    259       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
SQ   SEQUENCE   655 AA;  71627 MW;  0684C2215AA41675 CRC64;
     MKIILAEYRG FCYGVKRAIE TAYACIGQGP VYTLGPIIHN PQLVQRLSEQ GVVMANTLEQ
     IPAGRVIIRS HGVGPEVYDQ ARARSLEVVD ATCPHVRKAQ QAARQLAEKG YYVAVVGEPN
     HPEVKSIVAW AGERVTVVET PADAQNLPYH EQLGVVAQTT FASDQFNTIV DILKTKCREI
     EVSRTICTAT DQRQQAAIKL ARKVDVMVVV GGKNSANTSR LAELCRLQGC PTYHVETAQE
     LKIDWFTGVQ TVGITAGAST PDWIIEEVYS KMQEFDQLLD QDMKPLEPGV ILKGRVVGVR
     KDEVFVDIGH KGEGVIPLTE LAYPVPENAS DVVSEGDEID VYVLAPEGDD GPVKLSKVKA
     DNIVAWEKLQ AAAQANETVT GKVTAVVKGG LAVSLYGVRG FVPASQVAVQ HVADLTPYVG
     QTLELLPIEI DQAKQKIVLS RRKVLEQEQQ RRAEELFSRL AEGQIVTGTV SRIADFGVFV
     DLGGVDGLIH ISDLSWHRVK NPTEVVNIGD EVQVFVQKVD PKAKRISLSL KRVQRDPWYD
     VVEGLREGMT VAGKVTKLAK FGAFVEVKPG VEGLVHLSEL ADRRVASAQE VVEVGQTVTV
     KILGIDKENK RISLSIAQAQ QDAERADYQR FLSQESNTLG VTIGEKFGHL FGRKG
//
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