ISPH1_MYCTU
ID ISPH1_MYCTU Reviewed; 329 AA.
AC P9WKF9; L0TCD3; O50409; P0A5I2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1 {ECO:0000255|HAMAP-Rule:MF_00191, ECO:0000303|PubMed:23091471, ECO:0000303|PubMed:26309039};
DE Short=HDR 1 {ECO:0000303|PubMed:26309039};
DE Short=HMBPP reductase 1 {ECO:0000255|HAMAP-Rule:MF_00191};
DE EC=1.17.7.4 {ECO:0000255|HAMAP-Rule:MF_00191, ECO:0000305|PubMed:23091471};
GN Name=ispH1 {ECO:0000305};
GN Synonyms=lytB1 {ECO:0000303|PubMed:23091471, ECO:0000303|PubMed:26309039,
GN ECO:0000312|EMBL:CCP46203.1}; OrderedLocusNames=Rv3382c;
GN ORFNames=MTV004.40c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23091471; DOI=10.3389/fmicb.2012.00368;
RA Mann F.M., Xu M., Davenport E.K., Peters R.J.;
RT "Functional characterization and evolution of the isotuberculosinol operon
RT in Mycobacterium tuberculosis and related Mycobacteria.";
RL Front. Microbiol. 3:368-368(2012).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=26309039; DOI=10.1371/journal.pone.0135638;
RA Brown A.C., Kokoczka R., Parish T.;
RT "LytB1 and LytB2 of Mycobacterium tuberculosis are not genetically
RT redundant.";
RL PLoS ONE 10:E0135638-E0135638(2015).
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) (PubMed:23091471). Acts in the
CC terminal step of the DOXP/MEP pathway for isoprenoid precursor
CC biosynthesis. Has a reduced activity compared with LytB2
CC (PubMed:23091471). Is unable to functionally complement the loss of
CC lytB2 in M.tuberculosis (PubMed:26309039). {ECO:0000255|HAMAP-
CC Rule:MF_00191, ECO:0000269|PubMed:23091471,
CC ECO:0000269|PubMed:26309039}.
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:0000255|HAMAP-Rule:MF_00191,
CC ECO:0000305|PubMed:23091471};
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:0000255|HAMAP-Rule:MF_00191,
CC ECO:0000305|PubMed:23091471};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00191};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00191}.
CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP-
CC Rule:MF_00191}.
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DR EMBL; AL123456; CCP46203.1; -; Genomic_DNA.
DR PIR; E70973; E70973.
DR RefSeq; WP_003417912.1; NZ_NVQJ01000021.1.
DR RefSeq; YP_177967.1; NC_000962.3.
DR AlphaFoldDB; P9WKF9; -.
DR SMR; P9WKF9; -.
DR STRING; 83332.Rv3382c; -.
DR PaxDb; P9WKF9; -.
DR DNASU; 887953; -.
DR GeneID; 887953; -.
DR KEGG; mtu:Rv3382c; -.
DR TubercuList; Rv3382c; -.
DR eggNOG; COG0761; Bacteria.
DR OMA; NDSICRQ; -.
DR PhylomeDB; P9WKF9; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR Proteomes; UP000001584; 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: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 PANTHER; PTHR30426; PTHR30426; 1.
DR Pfam; PF02401; LYTB; 1.
DR TIGRFAMs; TIGR00216; ispH_lytB; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..329
FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase
FT 1"
FT /id="PRO_0000128842"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 243..245
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
SQ SEQUENCE 329 AA; 34666 MW; 00540C5C87B2AB6B CRC64;
MAEVFVGPVA QGYASGEVTV LLASPRSFCA GVERAIETVK RVLDVAEGPV YVRKQIVHNT
VVVAELRDRG AVFVEDLDEI PDPPPPGAVV VFSAHGVSPA VRAGADERGL QVVDATCPLV
AKVHAEAARF AARGDTVVFI GHAGHEETEG TLGVAPRSTL LVQTPADVAA LNLPEGTQLS
YLTQTTLALD ETADVIDALR ARFPTLGQPP SEDICYATTN RQRALQSMVG ECDVVLVIGS
CNSSNSRRLV ELAQRSGTPA YLIDGPDDIE PEWLSSVSTI GVTAGASAPP RLVGQVIDAL
RGYASITVVE RSIATETVRF GLPKQVRAQ
