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Database: UniProt
Entry: R7RS98_9CLOT
LinkDB: R7RS98_9CLOT
Original site: R7RS98_9CLOT 
ID   R7RS98_9CLOT            Unreviewed;       633 AA.
AC   R7RS98;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000256|HAMAP-Rule:MF_00191};
DE            Short=HMBPP reductase {ECO:0000256|HAMAP-Rule:MF_00191};
DE            EC=1.17.7.4 {ECO:0000256|HAMAP-Rule:MF_00191};
GN   Name=ispH {ECO:0000256|HAMAP-Rule:MF_00191};
GN   ORFNames=TCEL_00209 {ECO:0000313|EMBL:CDF58163.1};
OS   Thermobrachium celere DSM 8682.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Thermobrachium.
OX   NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58163.1, ECO:0000313|Proteomes:UP000014923};
RN   [1] {ECO:0000313|EMBL:CDF58163.1, ECO:0000313|Proteomes:UP000014923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58163.1,
RC   ECO:0000313|Proteomes:UP000014923};
RA   Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT   "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT   alkalithermophilic Caloramator celere.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl
CC       4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP)
CC       and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the
CC       DOXP/MEP pathway for isoprenoid precursor biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00191}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+)
CC         + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24488, Rhea:RHEA-
CC         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   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+)
CC         + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24825, Rhea:RHEA-
CC         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   -!- 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-Rule:MF_00191}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 6/6. {ECO:0000256|HAMAP-Rule:MF_00191}.
CC   -!- SIMILARITY: Belongs to the IspH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00191}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDF58163.1}.
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DR   EMBL; CAVN010000095; CDF58163.1; -; Genomic_DNA.
DR   RefSeq; WP_018661991.1; NZ_HF952018.1.
DR   AlphaFoldDB; R7RS98; -.
DR   eggNOG; COG0539; Bacteria.
DR   eggNOG; COG0761; Bacteria.
DR   HOGENOM; CLU_015805_3_1_9; -.
DR   OrthoDB; 9804077at2; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000014923; 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   CDD; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR   CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR   Gene3D; 3.40.50.11270; -; 1.
DR   Gene3D; 3.40.1010.20; 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain; 2.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR   HAMAP; MF_00191; IspH; 1.
DR   InterPro; IPR003451; LytB/IspH.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR035104; Ribosomal_protein_S1-like.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00216; ispH_lytB; 1.
DR   PANTHER; PTHR30426; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR30426:SF0; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR   Pfam; PF02401; LYTB; 1.
DR   Pfam; PF00575; S1; 3.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 4.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR   PROSITE; PS50126; S1; 3.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00191};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00191};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00191}; Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00191};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00191};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000313|EMBL:CDF58163.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014923}.
FT   DOMAIN          302..370
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          478..546
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          563..632
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   ACT_SITE        123
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         12
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         93
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         188
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         216..218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
SQ   SEQUENCE   633 AA;  71695 MW;  DDC3FB86909E6754 CRC64;
     MEILVAKSAG FCFGVKKAIE KAFNENGERV FTYGPIIHNK QVVEDLKNRG IEVVEDLENI
     KPKDKVIIRS HGIPKNEYKK LEEKGAIIVD ATCPYVKHIH KIVEQRYSEG YKIIIVGDEN
     HPEVKGINGW CDNTATIISD VNDIEKLNQN LGKVCLVAQT TFNQNKWYNL SSEIIKRAKE
     IIIYNTICSA TDERQNEAIE LSKQVDAMII IGGKNSSNSR KLYEICKENC KKAIFIEDES
     ELDLNDIKGL SKVGITAGAS TPDYTIKAVI DKLHSVDIEK IEDDAKNEEH ELDYEFKKLT
     VGEIVEGKVI HVTKDEVFFD IGYKSDGILP KELASNKEIN LKDVFKVGDV YDLEVVKLSD
     KEGNVVLSRI NIEKYDIIEE LEKAKNEDKI IKVKLLGEIK GGYECSYNNI KAFLPESHSG
     ITTKDDIKNI IGKEIEVNII DVKLQKNDTI ELIVSRKSIL KNKLQEEKRR FIDELSFGQV
     LNGRIKSFID SGIFVNVGPI DIFVPNSEVS WDRKVKPQKE FKINQEINVV VTKINKEENK
     VSGSIKRTMK EPWDEFILKY KEGDVVTGKV VAFTDYGAFV ELIEGVEGLI HISQITTRRI
     DKPTDFLKIG QVVKPKIVGI DYEKKRVSLS LIA
//
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