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Protein

Mevalonate kinase

Gene

mvk

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Unreviewed-Annotation score: Annotation score: 3 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 annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Pathway: 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 sitei138 – 1381Proton acceptorUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi87 – 9711ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotation, Transferase

Keywords - Biological processi

Isoprene biosynthesisUniRule annotation, Lipid biosynthesisUniRule annotation, Lipid metabolism

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18243.
MMAZ192952:GCK2-1806-MONOMER.
BRENDAi2.7.1.36. 3270.
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:MM_1762Imported
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)Imported
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000000595 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi192952.MM_1762.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HACX-ray1.92A/B1-301[»]
ProteinModelPortaliQ8PW39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1577.
HOGENOMiHOG000080810.
KOiK00869.
OMAiLMNINQG.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPiMF_00217. Mevalonate_kinase.
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:SF10. PTHR10457:SF10. 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.

Q8PW39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSCSAPGKI YLFGEHAVVY GETAIACAVE LRTRVRAELN DSITIQSQIG
60 70 80 90 100
RTGLDFEKHP YVSAVIEKMR KSIPINGVFL TVDSDIPVGS GLGSSAAVTI
110 120 130 140 150
ASIGALNELF GFGLSLQEIA KLGHEIEIKV QGAASPTDTY VSTFGGVVTI
160 170 180 190 200
PERRKLKTPD CGIVIGDTGV FSSTKELVAN VRQLRESYPD LIEPLMTSIG
210 220 230 240 250
KISRIGEQLV LSGDYASIGR LMNVNQGLLD ALGVNILELS QLIYSARAAG
260 270 280 290 300
AFGAKITGAG GGGCMVALTA PEKCNQVAEA VAGAGGKVTI TKPTEQGLKV

D
Length:301
Mass (Da):31,412
Last modified:October 1, 2002 - v1
Checksum:iCF223C2CE893D62D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM31458.1.
RefSeqiNP_633786.1. NC_003901.1.
WP_011033702.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM31458; AAM31458; MM_1762.
GeneIDi1480104.
KEGGimma:MM_1762.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM31458.1.
RefSeqiNP_633786.1. NC_003901.1.
WP_011033702.1. NC_003901.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HACX-ray1.92A/B1-301[»]
ProteinModelPortaliQ8PW39.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi192952.MM_1762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM31458; AAM31458; MM_1762.
GeneIDi1480104.
KEGGimma:MM_1762.

Phylogenomic databases

eggNOGiCOG1577.
HOGENOMiHOG000080810.
KOiK00869.
OMAiLMNINQG.

Enzyme and pathway databases

UniPathwayiUPA00057; UER00098.
BioCyciMetaCyc:MONOMER-18243.
MMAZ192952:GCK2-1806-MONOMER.
BRENDAi2.7.1.36. 3270.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPiMF_00217. Mevalonate_kinase.
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:SF10. PTHR10457:SF10. 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...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
    Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
    , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88Imported.
  2. "Crystallization and preliminary X-ray diffraction analysis of mevalonate kinase from Methanosarcina mazei."
    Zhuang N., Seo K.H., Chen C., Zhou J., Kim S.W., Lee K.H.
    Acta Crystallogr. F 68:1560-1563(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).

Entry informationi

Entry nameiQ8PW39_METMA
AccessioniPrimary (citable) accession number: Q8PW39
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2002
Last sequence update: October 1, 2002
Last modified: June 24, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.