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Protein

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

Gene

hexs-b

Organism
Micrococcus luteus (Micrococcus lysodeikticus)
Status
Reviewed-Annotation score: Annotation score: 4 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

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45Isopentenyl diphosphateBy similarity1
Binding sitei48Isopentenyl diphosphateBy similarity1
Binding sitei77Isopentenyl diphosphateBy similarity1
Metal bindingi84Magnesium 11
Metal bindingi84Magnesium 21
Binding sitei84Hexaprenyl diphosphate1
Metal bindingi88Magnesium 11
Metal bindingi88Magnesium 21
Binding sitei88Hexaprenyl diphosphate1
Binding sitei93Hexaprenyl diphosphateBy similarity1
Binding sitei94Isopentenyl diphosphateBy similarity1
Binding sitei170Hexaprenyl diphosphate1
Binding sitei171Hexaprenyl diphosphateBy similarity1
Binding sitei208Hexaprenyl diphosphateBy similarity1
Metal bindingi211Magnesium 31

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Menaquinone biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13829.
BRENDAi2.5.1.83. 3348.

Names & Taxonomyi

Protein namesi
Recommended name:
Hexaprenyl-diphosphate synthase large 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-b
OrganismiMicrococcus luteus (Micrococcus lysodeikticus)
Taxonomic identifieri1270 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeMicrococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004191641 – 325Hexaprenyl-diphosphate synthase large subunit ((2E,6E)-farnesyl-diphosphate specific)Add BLAST325

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1325
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 25Combined sources20
Helixi30 – 41Combined sources12
Helixi47 – 56Combined sources10
Beta strandi58 – 60Combined sources3
Helixi64 – 88Combined sources25
Helixi99 – 102Combined sources4
Helixi105 – 122Combined sources18
Turni123 – 125Combined sources3
Helixi129 – 151Combined sources23
Turni152 – 154Combined sources3
Helixi160 – 170Combined sources11
Helixi172 – 184Combined sources13
Turni185 – 187Combined sources3
Helixi190 – 217Combined sources28
Helixi220 – 223Combined sources4
Helixi229 – 232Combined sources4
Helixi238 – 249Combined sources12
Helixi254 – 260Combined sources7
Helixi268 – 281Combined sources14
Helixi283 – 302Combined sources20
Helixi308 – 320Combined sources13
Turni321 – 324Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AQBX-ray2.40B/D1-325[»]
3AQCX-ray2.61B/D1-325[»]
ProteinModelPortaliO66129.
SMRiO66129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66129.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.Curated

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR000092. Polyprenyl_synt.
IPR033749. Polyprenyl_synt_CS.
[Graphical view]
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O66129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIALSYKAFL NPYIIEVEKR LYECIQSDSE TINKAAHHIL SSGGKRVRPM
60 70 80 90 100
FVLLSGFLND TQKDDLIRTA VSLELVHMAS LVHDDYIDNS DMRRGNTSVH
110 120 130 140 150
IAFDKDTAIR TGHFLLARAL QNIATINNSK FHQIFSKTIL EVCFGEFDQM
160 170 180 190 200
ADRFNYPVSF TAYLRRINRK TAILIEASCH LGALSSQLDE QSTYHIKQFG
210 220 230 240 250
HCIGMSYQII DDILDYTSDE ATLGKPVGSD IRNGHITYPL MAAIANLKEQ
260 270 280 290 300
DDDKLEAVVK HLTSTSDDEV YQYIVSQVKQ YGIEPAELLS RKYGDKAKYH
310 320
LSQLQDSNIK DYLEEIHEKM LKRVY
Length:325
Mass (Da):37,083
Last modified:August 1, 1998 - v1
Checksum:iE73A7D6B94DA33F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003188 Genomic DNA. Translation: BAA25268.1.

Genome annotation databases

KEGGiag:BAA25268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003188 Genomic DNA. Translation: BAA25268.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AQBX-ray2.40B/D1-325[»]
3AQCX-ray2.61B/D1-325[»]
ProteinModelPortaliO66129.
SMRiO66129.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA25268.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13829.
BRENDAi2.5.1.83. 3348.

Miscellaneous databases

EvolutionaryTraceiO66129.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR000092. Polyprenyl_synt.
IPR033749. Polyprenyl_synt_CS.
[Graphical view]
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEXB_MICLU
AccessioniPrimary (citable) accession number: O66129
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: August 1, 1998
Last modified: November 30, 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

3D-structure

Documents

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