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Q58673

- LEUD_METJA

UniProt

Q58673 - LEUD_METJA

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Protein

Isopropylmalate/citramalate isomerase small subunit

Gene
leuD, MJ1277
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-methylmalate
  3. KM=1900 µM for racemic 2-isopropylmalate
  4. KM=39 µM for racemic 3-isopropylmalate
  5. KM=400 µM for maleate

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

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

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

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

Vmax=34 µmol/min/mg enzyme for maleate hydration reaction

pH dependencei

Optimum pH is 7.5.

Temperature dependencei

Optimum temperature is 70 degrees Celsius.

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 subunitUniRule annotationPRO_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 – 119
Helixi18 – 214
Helixi24 – 263
Helixi32 – 354
Helixi36 – 383
Turni39 – 435
Helixi47 – 504
Beta strandi56 – 594
Beta strandi65 – 673
Helixi71 – 788
Beta strandi83 – 875
Helixi91 – 999
Beta strandi104 – 1063
Helixi110 – 1134
Beta strandi119 – 1235
Turni124 – 1263
Beta strandi128 – 1314
Turni132 – 1343
Beta strandi137 – 1393
Helixi145 – 1539
Helixi156 – 16510

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the LeuD family.

Phylogenomic databases

eggNOGiCOG0066.
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

MRSIIKGRVW KFGNNVDTDA ILPARYLVYT KPEELAQFVM TGADPDFPKK    50
VKPGDIIVGG KNFGCGSSRE HAPLGLKGAG ISCVIAESFA RIFYRNAINV 100
GLPLIECKGI SEKVNEGDEL EVNLETGEIK NLTTGEVLKG QKLPEFMMEI 150
LEAGGLMPYL KKKMAESQ 168
Length:168
Mass (Da):18,377
Last modified:November 1, 1996 - v1
Checksum:iA53C2CA883B6CCD7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB99283.1.
PIRiD64459.
RefSeqiNP_248273.1. NC_000909.1.
WP_010870790.1. NC_000909.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB99283.1 .
PIRi D64459.
RefSeqi NP_248273.1. NC_000909.1.
WP_010870790.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
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: September 3, 2014
This is version 93 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

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