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Protein

Mevalonate kinase

Gene

mvk

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.UniRule annotation2 Publications

Catalytic activityi

ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation1 Publication

Enzyme regulationi

Farnesyl- and geranyl-pyrophosphates are competitive inhibitors. Slightly inhibited by high concentration of ATP.1 Publication

Kineticsi

  1. KM=68.5 µM for (RS)-mevalonate (at 70 degrees Celsius)2 Publications
  2. KM=106 µM for (RS)-mevalonate (at 34 degrees Celsius)2 Publications
  3. KM=92 µM for ATP (at 70 degrees Celsius)2 Publications
  4. KM=1180 µM for ATP (at 34 degrees Celsius)2 Publications
  1. Vmax=387 µmol/min/mg enzyme (at 70 degrees Celsius)2 Publications
  2. Vmax=50.3 µmol/min/mg enzyme (at 34 degrees Celsius)2 Publications

pH dependencei

Optimum pH is 8.0-8.5. Exhibits at least 60% of its optimal activity over a rather broad pH range, from 5 to 7.1 Publication

Temperature dependencei

Optimum temperature is 70-75 degrees Celsius. Highly thermostable. Retains 100% of its activity after 24 hours of incubation at 70 degrees Celsius. At 90 and 100 degrees Celsius, the enzyme shows a half-life of 15 and 5 min, respectively.1 Publication

Pathwayi: isopentenyl diphosphate biosynthesis via mevalonate pathway

This protein is involved in step 1 of the subpathway that synthesizes isopentenyl diphosphate from (R)-mevalonate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Mevalonate kinase (mvk)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via mevalonate 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 (R)-mevalonate, the pathway isopentenyl diphosphate biosynthesis via mevalonate pathway and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei155Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi104 – 114ATPUniRule annotationAdd BLAST11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14622.
BRENDAi2.7.1.36. 3260.
SABIO-RKQ58487.
UniPathwayiUPA00057; UER00098.

Names & Taxonomyi

Protein namesi
Recommended name:
Mevalonate kinaseUniRule annotation (EC:2.7.1.36UniRule annotation)
Short name:
MKUniRule annotation
Short name:
MVKUniRule annotation
Gene namesi
Name:mvkUniRule annotation
Ordered Locus Names:MJ1087
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi196R → K: 13.5-fold decrease in affinity for mevalonate, whereas only little effect on affinity for ATP and on reaction rate. 1 Publication1
Mutagenesisi196R → Q: 1900-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi196R → V: 63-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi272K → R or A: 13- to 26-fold decrease in catalytic efficiency. Still thermostable. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001566651 – 312Mevalonate kinaseAdd BLAST312

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_1087.

Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 12Combined sources12
Helixi16 – 19Combined sources4
Beta strandi23 – 38Combined sources16
Beta strandi41 – 48Combined sources8
Turni49 – 51Combined sources3
Beta strandi54 – 58Combined sources5
Turni59 – 61Combined sources3
Helixi62 – 64Combined sources3
Helixi67 – 69Combined sources3
Helixi71 – 73Combined sources3
Helixi74 – 86Combined sources13
Beta strandi95 – 101Combined sources7
Beta strandi105 – 109Combined sources5
Helixi111 – 125Combined sources15
Turni126 – 128Combined sources3
Helixi133 – 147Combined sources15
Beta strandi148 – 150Combined sources3
Helixi154 – 161Combined sources8
Beta strandi163 – 170Combined sources8
Beta strandi172 – 175Combined sources4
Helixi177 – 184Combined sources8
Beta strandi188 – 194Combined sources7
Helixi200 – 208Combined sources9
Helixi213 – 229Combined sources17
Helixi233 – 248Combined sources16
Turni249 – 251Combined sources3
Helixi255 – 267Combined sources13
Beta strandi268 – 273Combined sources6
Beta strandi275 – 285Combined sources11
Helixi288 – 290Combined sources3
Helixi291 – 299Combined sources9
Beta strandi304 – 308Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKHX-ray2.40A1-312[»]
1VISX-ray2.69A2-312[»]
ProteinModelPortaliQ58487.
SMRiQ58487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58487.

Family & Domainsi

Sequence similaritiesi

Belongs to the GHMP kinase family. Mevalonate kinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01028. Archaea.
COG1577. LUCA.
InParanoidiQ58487.
KOiK00869.
OMAiCMYALAP.
PhylomeDBiQ58487.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPiMF_00217. Mevalonate_kinase. 1 hit.
InterProiIPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR006205. Mev_gal_kin.
IPR006206. Mevalonate/galactokinase.
IPR022937. Mevalonate_kinase_arc.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10457. PTHR10457. 1 hit.
PfamiPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PRINTSiPR00959. MEVGALKINASE.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR00549. mevalon_kin. 1 hit.
PROSITEiPS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q58487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIETPSKVI LFGEHAVVYG YRAISMAIDL TSTIEIKETQ EDEIILNLND
60 70 80 90 100
LNKSLGLNLN EIKNINPNNF GDFKYCLCAI KNTLDYLNIE PKTGFKINIS
110 120 130 140 150
SKIPISCGLG SSASITIGTI KAVSGFYNKE LKDDEIAKLG YMVEKEIQGK
160 170 180 190 200
ASITDTSTIT YKGILEIKNN KFRKIKGEFE EFLKNCKFLI VYAEKRKKKT
210 220 230 240 250
AELVNEVAKI ENKDEIFKEI DKVIDEALKI KNKEDFGKLM TKNHELLKKL
260 270 280 290 300
NISTPKLDRI VDIGNRFGFG AKLTGAGGGG CVIILVNEEK EKELLKELNK
310
EDVRIFNCRM MN
Length:312
Mass (Da):35,177
Last modified:November 1, 1996 - v1
Checksum:iDFF9E5B869728298
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99088.1.
PIRiF64435.
RefSeqiWP_010870599.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB99088; AAB99088; MJ_1087.
GeneIDi1451983.
KEGGimja:MJ_1087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99088.1.
PIRiF64435.
RefSeqiWP_010870599.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKHX-ray2.40A1-312[»]
1VISX-ray2.69A2-312[»]
ProteinModelPortaliQ58487.
SMRiQ58487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99088; AAB99088; MJ_1087.
GeneIDi1451983.
KEGGimja:MJ_1087.

Phylogenomic databases

eggNOGiarCOG01028. Archaea.
COG1577. LUCA.
InParanoidiQ58487.
KOiK00869.
OMAiCMYALAP.
PhylomeDBiQ58487.

Enzyme and pathway databases

UniPathwayiUPA00057; UER00098.
BioCyciMetaCyc:MONOMER-14622.
BRENDAi2.7.1.36. 3260.
SABIO-RKQ58487.

Miscellaneous databases

EvolutionaryTraceiQ58487.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPiMF_00217. Mevalonate_kinase. 1 hit.
InterProiIPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR006205. Mev_gal_kin.
IPR006206. Mevalonate/galactokinase.
IPR022937. Mevalonate_kinase_arc.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10457. PTHR10457. 1 hit.
PfamiPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PRINTSiPR00959. MEVGALKINASE.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR00549. mevalon_kin. 1 hit.
PROSITEiPS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMVK_METJA
AccessioniPrimary (citable) accession number: Q58487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 123 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, Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.