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Protein

4-hydroxy-3-methylbut-2-enyl diphosphate reductase

Gene

ispH

Organism
Bacillus thuringiensis (strain Al Hakam)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).UniRule annotation

Catalytic activityi

Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+.UniRule annotation
Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+.UniRule annotation

Cofactori

[3Fe-4S] clusterUniRule annotationNote: Binds 1 [3Fe-4S] cluster per subunit.UniRule annotation

Pathwayi: dimethylallyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
This subpathway is part of the pathway dimethylallyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate, the pathway dimethylallyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 6 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr)
  2. 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD)
  3. 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE)
  4. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF)
  5. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG), 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG)
  6. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi12Iron-sulfur (3Fe-4S)UniRule annotation1
Binding sitei43SubstrateUniRule annotation1
Binding sitei81SubstrateUniRule annotation1
Metal bindingi103Iron-sulfur (3Fe-4S)UniRule annotation1
Binding sitei131SubstrateUniRule annotation1
Binding sitei170SubstrateUniRule annotation1
Metal bindingi198Iron-sulfur (3Fe-4S)UniRule annotation1
Binding sitei271SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Isoprene biosynthesis

Keywords - Ligandi

3Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

UniPathwayiUPA00056; UER00097.
UPA00059; UER00105.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-3-methylbut-2-enyl diphosphate reductaseUniRule annotation (EC:1.17.7.4UniRule annotation)
Gene namesi
Name:ispHUniRule annotation
Ordered Locus Names:BALH_3881
OrganismiBacillus thuringiensis (strain Al Hakam)
Taxonomic identifieri412694 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000761 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000210871 – 3164-hydroxy-3-methylbut-2-enyl diphosphate reductaseAdd BLAST316

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni226 – 228Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the IspH family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000220192.
KOiK03527.
OMAiHTIDATC.

Family and domain databases

CDDicd13944. lytB_ispH. 1 hit.
HAMAPiMF_00191. IspH. 1 hit.
InterProiIPR003451. LytB/IspH.
[Graphical view]
PfamiPF02401. LYTB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00216. ispH_lytB. 1 hit.

Sequencei

Sequence statusi: Complete.

A0RIR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIVKISPRG YCYGVVDAMV IARNAALDTS LPRPIYILGM IVHNKHVTDA
60 70 80 90 100
FEEDGIITLD GPSRLDILDK IDSGTVIFTA HGVSPEVKQR AKEKGLTTID
110 120 130 140 150
ATCPDVTKTH DLIEAKKAEG YHVIYIGKKN HPEPEGAVGI APDIVHLIEK
160 170 180 190 200
ADDLKTLEIP TNKILVTNQT TMSQWDVQHL MEDIQKKFPT AEFHKEICLA
210 220 230 240 250
TQVRQEAVAK QADVADLTIV VGDPKSNNSN RLAQVSQEIA GTKAYRVADV
260 270 280 290 300
SEIKLEWLQG VENVAVTAGA STPTPITKEV IAFLEQYDPM NPATWERVRK
310
VPLQKILPRV KVKKEQ
Length:316
Mass (Da):34,938
Last modified:January 9, 2007 - v1
Checksum:i622569575169DCBB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000485 Genomic DNA. Translation: ABK87104.1.
RefSeqiWP_000706666.1. NC_008600.1.

Genome annotation databases

EnsemblBacteriaiABK87104; ABK87104; BALH_3881.
KEGGibtl:BALH_3881.
PATRICi19000614. VBIBacThu63319_4305.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000485 Genomic DNA. Translation: ABK87104.1.
RefSeqiWP_000706666.1. NC_008600.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK87104; ABK87104; BALH_3881.
KEGGibtl:BALH_3881.
PATRICi19000614. VBIBacThu63319_4305.

Phylogenomic databases

HOGENOMiHOG000220192.
KOiK03527.
OMAiHTIDATC.

Enzyme and pathway databases

UniPathwayiUPA00056; UER00097.
UPA00059; UER00105.

Family and domain databases

CDDicd13944. lytB_ispH. 1 hit.
HAMAPiMF_00191. IspH. 1 hit.
InterProiIPR003451. LytB/IspH.
[Graphical view]
PfamiPF02401. LYTB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00216. ispH_lytB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiISPH_BACAH
AccessioniPrimary (citable) accession number: A0RIR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: November 2, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.