ID A0A1T4LI71_9FIRM Unreviewed; 728 AA.
AC A0A1T4LI71;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN02745118_01153 {ECO:0000313|EMBL:SJZ54433.1};
OS Selenihalanaerobacter shriftii.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Selenihalanaerobacter.
OX NCBI_TaxID=142842 {ECO:0000313|EMBL:SJZ54433.1, ECO:0000313|Proteomes:UP000190625};
RN [1] {ECO:0000313|Proteomes:UP000190625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-73 {ECO:0000313|Proteomes:UP000190625};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUWM01000008; SJZ54433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4LI71; -.
DR STRING; 142842.SAMN02745118_01153; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR Proteomes; UP000190625; 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 CDD; cd05688; S1_RPS1_repeat_ec3; 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; 4.
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; 4.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 4.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS50126; S1; 4.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00191};
KW Coiled coil {ECO:0000256|SAM:Coils};
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}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191};
KW Reference proteome {ECO:0000313|Proteomes:UP000190625}.
FT DOMAIN 356..425
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 443..508
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 529..597
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 614..683
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 685..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 312..343
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 501..528
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 692..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 228
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 256..258
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191"
SQ SEQUENCE 728 AA; 80737 MW; 29B2305DA4647495 CRC64;
MTKKYKGFFL IFIIFQVRMG IISLENVLVF VGLEGGLGLE IILADHAGFC FGVTRAMDLT
MDAGKNDDNE IYTLGPLIHN PQAVNKLEGL GIRIVDEVDE VNEGTIIIRS HGVPPNTLNE
AKDKDLEVLD ATCPFVKKAQ KSAARLQEAG YQVIISGDKQ HPEVVAILGS TNGQAIVIEE
EEDFEKLPKK IKKAGIIAQT TQSIDNLKTV VNRLMDITEE LKVYNTICTT TNERQTSAAD
LAVEVDIMIV IGGYNSANTN RLAEVCWEVG TTTYHIETAD DLSRDWFHNI KRIGVTAGAS
TPNWIIKEVV SRMEDIKQEE NVNEEVEEVN EEEVEEVNEE EVEEVDYEGV KALEKGEALD
GTVEQVTDDG VYVNIGAKSE GLIPLNELSS SHFESPSDVV AEGDEIKVEV LNPEDEEGNI
LLSKKRIDYE EAWGSVQQAY ESGEIIEAEV TKEVKGGLVV DIGLRGFIPA SHVAIEYIED
LSQYIGETLP LRIIEVERDN NNVVLSRKEV LAEELEEKKE EIFSSLEEGD VISGTITKLV
DFGAFVDIGG VEGLLHISEM SWGRIDHPSD VLEEGEEIEV KVLGVNPEEE RISLGLKQIL
PDPWDQFIDN HNEGEVVSGK ITKTVDFGAF MEIEPGVEGL IHISQLSRRH VATVEEVVTA
GDEVEAKIIN IEPQERRVGL SMKELEEEDD NDNNNNTQRK QKDVEEFIDD DEGSGVTIGD
MFGELFEE
//
