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Q58673

- LEUD_METJA

UniProt

Q58673 - LEUD_METJA

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Protein

Isopropylmalate/citramalate isomerase small subunit

Gene

leuD

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

Functioni

Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.1 Publication

Catalytic activityi

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.1 Publication
(R)-2-methylmalate = 2-methylmaleate + H2O.1 Publication
2-methylmaleate + H2O = (2R,3S)-3-methylmalate.1 Publication
(R)-malate = maleate + H2O.1 Publication

Kineticsi

  1. KM=80 µM for 2-methylmaleate1 Publication
  2. KM=810 µM for (R)-2-methylmalate1 Publication
  3. KM=1900 µM for racemic 2-isopropylmalate1 Publication
  4. KM=39 µM for racemic 3-isopropylmalate1 Publication
  5. KM=400 µM for maleate1 Publication

Vmax=15 µmol/min/mg enzyme for 2-methylmaleate hydration reaction1 Publication

Vmax=1.5 µmol/min/mg enzyme for (R)-2-methylmalate dehydration reaction1 Publication

Vmax=4.2 µmol/min/mg enzyme for 2-isopropylmalate dehydration reaction1 Publication

Vmax=1.8 µmol/min/mg enzyme for 3-isopropylmalate dehydration reaction1 Publication

Vmax=34 µmol/min/mg enzyme for maleate hydration reaction1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 70 degrees Celsius.1 Publication

Pathwayi

GO - Molecular functioni

  1. (R)-2-methylmalate dehydratase activity Source: UniProtKB-EC
  2. 3-isopropylmalate dehydratase activity Source: UniProtKB-HAMAP
  3. maleate hydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. isoleucine biosynthetic process Source: UniProtKB-UniPathway
  2. leucine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis, Leucine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13648.
SABIO-RKQ58673.
UniPathwayiUPA00047; UER00067.
UPA00048; UER00071.

Names & Taxonomyi

Protein namesi
Recommended name:
Isopropylmalate/citramalate isomerase small subunit (EC:4.2.1.33, EC:4.2.1.35)
Alternative name(s):
(R)-2-methylmalate dehydratase
(R)-citramalate dehydratase
3-isopropylmalate dehydratase
Alpha-isopropylmalate dehydratase
Citraconate hydratase
Isopropylmalate isomerase
Short name:
IPMI
Maleate hydratase (EC:4.2.1.31)
Short name:
Malease
Gene namesi
Name:leuD
Ordered Locus Names:MJ1277
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
ProteomesiUP000000805: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. 3-isopropylmalate dehydratase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168Isopropylmalate/citramalate isomerase small subunitPRO_0000141937Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of 2 LeuC and 2 LeuD. The heterotetramer that can be formed in vitro between HacA and LeuD is inactive.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ1277.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi18 – 214Combined sources
Helixi24 – 263Combined sources
Helixi32 – 354Combined sources
Helixi36 – 383Combined sources
Turni39 – 435Combined sources
Helixi47 – 504Combined sources
Beta strandi56 – 594Combined sources
Beta strandi65 – 673Combined sources
Helixi71 – 788Combined sources
Beta strandi83 – 875Combined sources
Helixi91 – 999Combined sources
Beta strandi104 – 1063Combined sources
Helixi110 – 1134Combined sources
Beta strandi119 – 1235Combined sources
Turni124 – 1263Combined sources
Beta strandi128 – 1314Combined sources
Turni132 – 1343Combined sources
Beta strandi137 – 1393Combined sources
Helixi145 – 1539Combined sources
Helixi156 – 16510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VBAX-ray2.00A/B/C/D/E/F1-168[»]
ProteinModelPortaliQ58673.
SMRiQ58673. Positions 4-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LeuD family.Curated

Phylogenomic databases

eggNOGiCOG0066.
InParanoidiQ58673.
KOiK01704.
OMAiCMEDIDL.
PhylomeDBiQ58673.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
HAMAPiMF_01032. LeuD_type2.
InterProiIPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR011827. IsopropMal_deHydtase_ssu.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR02087. LEUD_arch. 1 hit.

Sequencei

Sequence statusi: Complete.

Q58673-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSIIKGRVW KFGNNVDTDA ILPARYLVYT KPEELAQFVM TGADPDFPKK
60 70 80 90 100
VKPGDIIVGG KNFGCGSSRE HAPLGLKGAG ISCVIAESFA RIFYRNAINV
110 120 130 140 150
GLPLIECKGI SEKVNEGDEL EVNLETGEIK NLTTGEVLKG QKLPEFMMEI
160
LEAGGLMPYL KKKMAESQ
Length:168
Mass (Da):18,377
Last modified:November 1, 1996 - v1
Checksum:iA53C2CA883B6CCD7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99283.1.
PIRiD64459.
RefSeqiNP_248273.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB99283; AAB99283; MJ_1277.
GeneIDi1452175.
KEGGimja:MJ_1277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99283.1 .
PIRi D64459.
RefSeqi NP_248273.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VBA X-ray 2.00 A/B/C/D/E/F 1-168 [» ]
ProteinModelPortali Q58673.
SMRi Q58673. Positions 4-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243232.MJ1277.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB99283 ; AAB99283 ; MJ_1277 .
GeneIDi 1452175.
KEGGi mja:MJ_1277.

Phylogenomic databases

eggNOGi COG0066.
InParanoidi Q58673.
KOi K01704.
OMAi CMEDIDL.
PhylomeDBi Q58673.

Enzyme and pathway databases

UniPathwayi UPA00047 ; UER00067 .
UPA00048 ; UER00071 .
BioCyci MetaCyc:MONOMER-13648.
SABIO-RK Q58673.

Family and domain databases

Gene3Di 3.20.19.10. 1 hit.
HAMAPi MF_01032. LeuD_type2.
InterProi IPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR011827. IsopropMal_deHydtase_ssu.
[Graphical view ]
PANTHERi PTHR11670. PTHR11670. 1 hit.
Pfami PF00694. Aconitase_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52016. SSF52016. 1 hit.
TIGRFAMsi TIGR02087. LEUD_arch. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. "Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii."
    Drevland R.M., Waheed A., Graham D.E.
    J. Bacteriol. 189:4391-4400(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  3. "Crystal structure of LeuD from Methanococcus jannaschii."
    Lee E.H., Cho Y.W., Hwang K.Y.
    Biochem. Biophys. Res. Commun. 419:160-164(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiLEUD_METJA
AccessioniPrimary (citable) accession number: Q58673
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 96 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

External Data

Dasty 3