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C3HNU0 (C3HNU0_BACTU) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
4-hydroxy-3-methylbut-2-enyl diphosphate reductase HAMAP MF_00191
EC=1.17.1.2 HAMAP MF_00191
Gene names
Name:ispH HAMAP MF_00191
ORF Names:bthur0012_41330 EMBL EEM87830.1
OrganismBacillus thuringiensis serovar pulsiensis BGSC 4CC1 EMBL EEM87830.1
Taxonomic identifier527028 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) By similarity. HAMAP MF_00191 SAAS SAAS003451

Catalytic activity

Dimethylallyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. HAMAP MF_00191 SAAS SAAS003451

Isopentenyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. HAMAP MF_00191 SAAS SAAS003451

Cofactor

Binds 1 3Fe-4S cluster By similarity. HAMAP MF_00191

Pathway

Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. HAMAP MF_00191 SAAS SAAS003451

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. HAMAP MF_00191 SAAS SAAS003451

Sequence similarities

Belongs to the IspH family. HAMAP MF_00191

Sequences

Sequence LengthMass (Da)Tools
C3HNU0 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 08C141F40FE642DB

FASTA31634,967
        10         20         30         40         50         60 
MKIVKISPRG YCYGVVDAMV IARNAALDTS LPRPIYILGM IVHNKHVTDA FEEDGIITLD 

        70         80         90        100        110        120 
GPSRLDILDK IDSGTVIFTA HGVSPEVKQR AKEKGLTTID ATCPDVTKTH DLIEAKKAEG 

       130        140        150        160        170        180 
YHVIYIGKKN HPEPEGAVGI APDIVHLIER ADDLKTLEIP TDKILVTNQT TMSQWDVQHL 

       190        200        210        220        230        240 
MEDIQKKFPT AEFHKEICLA TQVRQEAVAK QADVADLTIV VGDPKSNNSN RLAQVSQEIA 

       250        260        270        280        290        300 
GTKAYRVADV SEIKLEWLQG VENVAVTAGA STPTPITKEV IAFLEQYDPM NPATWERVRK 

       310 
VPLQKILPRV KVKKEQ

« Hide

References

[1]"Annotation of the Bacillus thuringiensis BGSC 4CC1 genome."
Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K., Zwick M.E.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BGSC 4CC1 EMBL EEM87830.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		ACNJ01000085 Genomic DNA. Translation: EEM87830.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000182783; EBBACP00000176257; EBBACG00000179931.
PATRIC28947662. VBIBacThu66700_5568.

Family and domain databases

HAMAPMF_00191. IspH.
[Tree]
InterProIPR003451. LytB.
[Graphical view]
PfamPF02401. LYTB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00216. IspH_lytB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC3HNU0_BACTU
AccessionPrimary (citable) accession number: C3HNU0
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: December 14, 2011
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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