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Database: UniProt
Entry: R7MNE6_9FIRM
LinkDB: R7MNE6_9FIRM
Original site: R7MNE6_9FIRM 
ID   R7MNE6_9FIRM            Unreviewed;       655 AA.
AC   R7MNE6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   16-JAN-2019, entry version 37.
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=BN739_01306 {ECO:0000313|EMBL:CDF01483.1};
OS   Ruminococcus sp. CAG:624.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus; environmental samples.
OX   NCBI_TaxID=1262965 {ECO:0000313|EMBL:CDF01483.1, ECO:0000313|Proteomes:UP000017977};
RN   [1] {ECO:0000313|EMBL:CDF01483.1, ECO:0000313|Proteomes:UP000017977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:624 {ECO:0000313|Proteomes:UP000017977};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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:CDF01483.1}.
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DR   EMBL; CBKC010000237; CDF01483.1; -; Genomic_DNA.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000017977; 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   InterPro; IPR002792; TRAM_dom.
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.
DR   PROSITE; PS50926; TRAM; 1.
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:UP000017977};
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:UP000017977}.
FT   DOMAIN      308    377       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      395    461       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      482    550       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      524    588       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   DOMAIN      567    636       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      224    226       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   COILED      535    555       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    126    126       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   METAL        13     13       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL        96     96       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       196    196       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      41     41       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING      74     74       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     124    124       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     168    168       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     267    267       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
SQ   SEQUENCE   655 AA;  72159 MW;  1FA423171590F281 CRC64;
     MKKITVAKSA GFCFGVDRAV KMVYNELEKK QHVATLGPII HNTDVVSDMQ RKGARIIETV
     SELKDNELVV IRSHGVGRDV YEQIAEKGNP MLDATCPFVA RIHKIVSEKA AEGYFILIAG
     DASHPEVQGI VGHCGENCMV FKDKTELQDF FEKKYTNLQK GVAIVAQTTY NIVVWDECLK
     IIPKDDPDIV IFDTICNATE ARQSDAEKLS READLMIVVG GKHSSNTVKL YDVCSKNCKT
     YHIENGDELL DLNLPSAEHI GITAGASTPA YIIKEVQTTM TDIQNNNLEE DINFEEMIDQ
     SFKKIHTGEK VKAYVEAVNK SEVIVSLGTK HTGYVALDDL TDDPTKTPAD IVKVGDEIEL
     IVIKVNDQEG TVALSKRKID EQAGFEKIMK AKEEGTVLEG TIQHVVKGGV TVSCFGVRVF
     IPASQTGLPR GAELDQLLKK KVQFMILEVT ENRRRAVGSI KAVLNAKKEE AKAKFWATAK
     VGDVFKGTVK SLTSFGAFVD LGGIDGMVHI SELSWKRIKH PSEVVSVGDT LEVYIKDLNQ
     EENRISLGYK KAEDNPWEIF KANYKVGDVV KATIVSITSF GAFAQIIDGV DGLIHISQIA
     DKKVENVKDI LSVGQEVDVK IIDIDTEAKR ISISIRALLE NSDEAAEEET SEDAE
//
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