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Database: UniProt
Entry: B2A4N7_NATTJ
LinkDB: B2A4N7_NATTJ
Original site: B2A4N7_NATTJ 
ID   B2A4N7_NATTJ            Unreviewed;       705 AA.
AC   B2A4N7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   05-JUN-2019, entry version 85.
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=Nther_1638 {ECO:0000313|EMBL:ACB85212.1};
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB85212.1, ECO:0000313|Proteomes:UP000001683};
RN   [1] {ECO:0000313|EMBL:ACB85212.1, ECO:0000313|Proteomes:UP000001683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC   {ECO:0000313|Proteomes:UP000001683};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-
RT   WN-LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB85212.1, ECO:0000313|Proteomes:UP000001683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC   {ECO:0000313|Proteomes:UP000001683};
RX   PubMed=21642468; DOI=10.1128/JB.05157-11;
RA   Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA   Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA   Kyrpides N., Wiegel J.;
RT   "Complete genome sequence of the anaerobic, halophilic
RT   alkalithermophile Natranaerobius thermophilus JW/NM-WN-LF.";
RL   J. Bacteriol. 193:4023-4024(2011).
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; CP001034; ACB85212.1; -; Genomic_DNA.
DR   STRING; 457570.Nther_1638; -.
DR   EnsemblBacteria; ACB85212; ACB85212; Nther_1638.
DR   KEGG; nth:Nther_1638; -.
DR   eggNOG; ENOG4105CAV; Bacteria.
DR   eggNOG; COG0539; LUCA.
DR   eggNOG; COG0761; LUCA.
DR   HOGENOM; HOG000057927; -.
DR   KO; K02945; -.
DR   KO; K03527; -.
DR   OMA; ATCPFVQ; -.
DR   BioCyc; NTHE457570:GHRL-1655-MONOMER; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000001683; 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: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:UP000001683};
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:UP000001683}.
FT   DOMAIN      326    395       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      413    479       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      500    568       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      585    654       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      230    232       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   REGION      291    320       Disordered. {ECO:0000256|MobiDB-lite:
FT                                B2A4N7}.
FT   REGION      655    685       Disordered. {ECO:0000256|MobiDB-lite:
FT                                B2A4N7}.
FT   COILED      403    423       {ECO:0000256|SAM:Coils}.
FT   COILED      467    487       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    138    138       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       108    108       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       202    202       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      44     44       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING      85     85       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     174    174       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     274    274       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
SQ   SEQUENCE   705 AA;  78862 MW;  789D45C3AC93267A CRC64;
     MEILVAKGAG FCSGVNRALD KTIQAVQTDT SRDIQVFTLG PIVHNKEVIQ NLTEKGIGII
     ENLTQLQSKK CLSEETNNYV VIRSHGVGPE TFKMLNNLSN TDVIDATCPF VRKVQQKASK
     LYQDGYQIFI VGDPNHPEVK GIKEWTDNNA IVIEKPEQVN DIEISNKTAV VAQTTLREEK
     FNEIVEKILD RNPNTIVHNT ICDATQKRQT ATKELAGQVD VMIVVGGYNS SNTKKLKELA
     VKEGVPTYHI ETAKELKTDW FLGCKKIGVT AGASTPDWTI KEVVGKMREF EEQNENLNTN
     SDESTQESQD ELMKATEDSA DKLDRGQVVK GKVVKVTEDE AMIDVGYKFE GSVPVNEMPI
     KEGESLEDLL SEGDEIDVKV VKVDDEEGQL ILSKKWADKD KQWEQLEQLM ENDEEIKAQV
     TEEVKGGLVV DLGQLQGFIP ASHVDIHYVP DLSKYVGEEL RLKPIELDRS RNKIVLSQKN
     ILEQEQEEKK NKTMETITEG DIVDGTVKRL TDFGAFIDIG GIDGLCHISQ ISHSRIDHPE
     SELETGENVK VKVLSLDPEN ERISLSIKEA QPDPFETFMK QYKSGDIVQG KVVRTVNFGA
     FIEITPGVEG LCHISQLSDD HVAKTQDVVN EGDQVTVKIL SIDDQQKKVS LSIKEAQGKS
     KKEQEQEEFA KYQDSQEEEE GVKLGDMFGD VLEEIKEDDK DDKSK
//
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