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Protein

Hexaprenyl-diphosphate synthase small subunit ((2E,6E)-farnesyl-diphosphate specific)

Gene

hexs-a

Organism
Micrococcus luteus (Micrococcus lysodeikticus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of three molecules of isopentenyl diphosphate with farnesyl diphosphate (FPP) to yield (all-E)-hexaprenyl diphosphate (HexPP; C30), the precursor of the prenyl side chain of menaquinone-6. Large subunit Hexs-B catalyzes the condensation reaction and the final product chain length is cooperatively regulated by both the Hexs-A and Hexs-B subunits using the whole size of the hydrophobic cleft as a ruler.3 Publications

Catalytic activityi

(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + all-trans-hexaprenyl diphosphate.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Menaquinone biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13828.
BRENDAi2.5.1.83. 3348.

Names & Taxonomyi

Protein namesi
Recommended name:
Hexaprenyl-diphosphate synthase small subunit ((2E,6E)-farnesyl-diphosphate specific) (EC:2.5.1.83)
Short name:
HexPS
Alternative name(s):
Hexaprenyl diphosphate synthase
Hexaprenyl pyrophosphate synthetase
Gene namesi
Name:hexs-a
OrganismiMicrococcus luteus (Micrococcus lysodeikticus)
Taxonomic identifieri1270 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeMicrococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 143143Hexaprenyl-diphosphate synthase small subunit ((2E,6E)-farnesyl-diphosphate specific)PRO_0000419165Add
BLAST

Interactioni

Subunit structurei

Dimer of heterodimer or heterotetramer composed of a small (Hexs-a) and large (Hexs-B) subunit.1 Publication

Structurei

Secondary structure

1
143
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1716Combined sources
Helixi28 – 358Combined sources
Helixi41 – 5616Combined sources
Helixi57 – 593Combined sources
Turni62 – 643Combined sources
Helixi65 – 8218Combined sources
Turni83 – 875Combined sources
Helixi89 – 11022Combined sources
Helixi115 – 12612Combined sources
Turni127 – 1304Combined sources
Helixi131 – 1333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AQBX-ray2.40A/C1-143[»]
3AQCX-ray2.61A/C1-143[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66127.

Sequencei

Sequence statusi: Complete.

O66127-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYLHKIELE LNRLTSRYPF FKKIAFDAEI IKLVDDLNVD ENVKCAIVAI
60 70 80 90 100
DTSMRMQDFI NEDNKDSFVL STDVLSALFY KYLSQPFYQH DFLVLTDCVS
110 120 130 140
RINELKSIRA TITDEIALHN INKQIHYMFI QPYMNNEKVV SYE
Length:143
Mass (Da):16,942
Last modified:August 1, 1998 - v1
Checksum:i0D923F9A52BE564B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003188 Genomic DNA. Translation: BAA25266.1.

Genome annotation databases

KEGGiag:BAA25266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003188 Genomic DNA. Translation: BAA25266.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AQBX-ray2.40A/C1-143[»]
3AQCX-ray2.61A/C1-143[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA25266.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13828.
BRENDAi2.5.1.83. 3348.

Miscellaneous databases

EvolutionaryTraceiO66127.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase."
    Shimizu N., Koyama T., Ogura K.
    J. Bacteriol. 180:1578-1581(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A HEXAPRENYL-DIPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY, NOMENCLATURE.
    Strain: B-P 26.
  2. "Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26. Separation of two essential components."
    Fujii H., Koyama T., Ogura K.
    J. Biol. Chem. 257:14610-14612(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A HEXAPRENYL-DIPHOSPHATE SYNTHASE.
  3. "Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases."
    Nagaki M., Kimura K., Kimura H., Maki Y., Goto E., Nishino T., Koyama T.
    Bioorg. Med. Chem. Lett. 11:2157-2159(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A HEXAPRENYL-DIPHOSPHATE SYNTHASE.
    Strain: B-P 26.
  4. "Crystal structure of heterodimeric hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26 reveals that the small subunit is directly involved in the product chain length regulation."
    Sasaki D., Fujihashi M., Okuyama N., Kobayashi Y., Noike M., Koyama T., Miki K.
    J. Biol. Chem. 286:3729-3740(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS, REACTION MECHANISM, SUBUNIT.
    Strain: B-P 26.

Entry informationi

Entry nameiHEXA_MICLU
AccessioniPrimary (citable) accession number: O66127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: August 1, 1998
Last modified: March 16, 2016
This is version 41 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.