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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei155 – 1551Proton acceptor1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi104 – 11411ATPUniRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi196 – 1961R → K: 13.5-fold decrease in affinity for mevalonate, whereas only little effect on affinity for ATP and on reaction rate. 1 Publication
Mutagenesisi196 – 1961R → Q: 1900-fold decrease in catalytic efficiency. 1 Publication
Mutagenesisi196 – 1961R → V: 63-fold decrease in catalytic efficiency. 1 Publication
Mutagenesisi272 – 2721K → R or A: 13- to 26-fold decrease in catalytic efficiency. Still thermostable. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Mevalonate kinasePRO_0000156665Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_1087.

Structurei

Secondary structure

312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 1212Combined sources
Helixi16 – 194Combined sources
Beta strandi23 – 3816Combined sources
Beta strandi41 – 488Combined sources
Turni49 – 513Combined sources
Beta strandi54 – 585Combined sources
Turni59 – 613Combined sources
Helixi62 – 643Combined sources
Helixi67 – 693Combined sources
Helixi71 – 733Combined sources
Helixi74 – 8613Combined sources
Beta strandi95 – 1017Combined sources
Beta strandi105 – 1095Combined sources
Helixi111 – 12515Combined sources
Turni126 – 1283Combined sources
Helixi133 – 14715Combined sources
Beta strandi148 – 1503Combined sources
Helixi154 – 1618Combined sources
Beta strandi163 – 1708Combined sources
Beta strandi172 – 1754Combined sources
Helixi177 – 1848Combined sources
Beta strandi188 – 1947Combined sources
Helixi200 – 2089Combined sources
Helixi213 – 22917Combined sources
Helixi233 – 24816Combined sources
Turni249 – 2513Combined sources
Helixi255 – 26713Combined sources
Beta strandi268 – 2736Combined sources
Beta strandi275 – 28511Combined sources
Helixi288 – 2903Combined sources
Helixi291 – 2999Combined sources
Beta strandi304 – 3085Combined sources

3D structure databases

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

Genome annotation databases

EnsemblBacteriaiAAB99088; AAB99088; MJ_1087.
KEGGimja:MJ_1087.

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

STRINGi243232.MJ_1087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99088; AAB99088; MJ_1087.
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: February 17, 2016
This is version 120 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.