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Protein

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

Gene

ispH

Organism
Bacillus anthracis
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), 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 1 (dxr1), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr2), 1-deoxy-D-xylulose 5-phosphate reductoisomerase 2 (dxr2), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr1), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (ABW01_09670), 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 (ipk), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ipk), 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), 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), 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), 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Iron-sulfur (3Fe-4S)UniRule annotation
Binding sitei43 – 431SubstrateUniRule annotation
Binding sitei81 – 811SubstrateUniRule annotation
Metal bindingi103 – 1031Iron-sulfur (3Fe-4S)UniRule annotation
Binding sitei131 – 1311SubstrateUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Metal bindingi198 – 1981Iron-sulfur (3Fe-4S)UniRule annotation
Binding sitei271 – 2711SubstrateUniRule annotation

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

BioCyciANTHRA:LYTB-MONOMER.
BANT260799:GJAJ-4246-MONOMER.
BANT261594:GJ7F-4388-MONOMER.
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
Synonyms:lytB
Ordered Locus Names:BA_4511, GBAA_4511, BAS4190
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3163164-hydroxy-3-methylbut-2-enyl diphosphate reductasePRO_0000128768Add
BLAST

Proteomic databases

PRIDEiQ81LU9.

Interactioni

Protein-protein interaction databases

IntActiQ81LU9. 1 interaction.
STRINGi198094.BA_4511.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni226 – 2283Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the IspH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C48. Bacteria.
COG0761. LUCA.
HOGENOMiHOG000220192.
KOiK03527.
OMAiHTIDATC.
OrthoDBiEOG6HF624.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q81LU9-1 [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 APDIVHLIER
160 170 180 190 200
ADDLKTLEIP TDKILVTNQT 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):34,967
Last modified:June 1, 2003 - v1
Checksum:i08C141F40FE642DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28221.1.
AE017334 Genomic DNA. Translation: AAT33631.1.
AE017225 Genomic DNA. Translation: AAT56489.1.
RefSeqiNP_846735.1. NC_003997.3.
WP_000706669.1. NZ_LHUO01000006.1.
YP_030438.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP28221; AAP28221; BA_4511.
AAT33631; AAT33631; GBAA_4511.
AAT56489; AAT56489; BAS4190.
GeneIDi1088236.
2852179.
KEGGiban:BA_4511.
bar:GBAA_4511.
bat:BAS4190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28221.1.
AE017334 Genomic DNA. Translation: AAT33631.1.
AE017225 Genomic DNA. Translation: AAT56489.1.
RefSeqiNP_846735.1. NC_003997.3.
WP_000706669.1. NZ_LHUO01000006.1.
YP_030438.1. NC_005945.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81LU9. 1 interaction.
STRINGi198094.BA_4511.

Proteomic databases

PRIDEiQ81LU9.

Protocols and materials databases

DNASUi1088236.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP28221; AAP28221; BA_4511.
AAT33631; AAT33631; GBAA_4511.
AAT56489; AAT56489; BAS4190.
GeneIDi1088236.
2852179.
KEGGiban:BA_4511.
bar:GBAA_4511.
bat:BAS4190.

Phylogenomic databases

eggNOGiENOG4105C48. Bacteria.
COG0761. LUCA.
HOGENOMiHOG000220192.
KOiK03527.
OMAiHTIDATC.
OrthoDBiEOG6HF624.

Enzyme and pathway databases

UniPathwayiUPA00056; UER00097.
UPA00059; UER00105.
BioCyciANTHRA:LYTB-MONOMER.
BANT260799:GJAJ-4246-MONOMER.
BANT261594:GJ7F-4388-MONOMER.

Family and domain databases

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

Publicationsi

  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.

Entry informationi

Entry nameiISPH_BACAN
AccessioniPrimary (citable) accession number: Q81LU9
Secondary accession number(s): Q6HTA0, Q6KMJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 85 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, Reference 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.