Isopropylmalate/citramalate isomerase small subunit - Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

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Q58673 (LEUD_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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
Short name=Malease
EC=4.2.1.31

Gene names

Name:	leuD
Ordered Locus Names:	MJ1277

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus ›

Protein attributes

Sequence length	168 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2
Catalytic activity	(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. Ref.2 (R)-2-methylmalate = 2-methylmaleate + H₂O. Ref.2 2-methylmaleate + H₂O = (2R,3S)-3-methylmalate. Ref.2 (R)-malate = maleate + H₂O. Ref.2
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01032 Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 2/3. HAMAP-Rule MF_01032
Subunit structure	Heterotetramer of 2 LeuC and 2 LeuD. The heterotetramer that can be formed in vitro between HacA and LeuD is inactive. Ref.2
Sequence similarities	Belongs to the LeuD family.
Biophysicochemical properties	Kinetic parameters: K_M=80 µM for 2-methylmaleate Ref.2 K_M=810 µM for (R)-2-methylmalate K_M=1900 µM for racemic 2-isopropylmalate K_M=39 µM for racemic 3-isopropylmalate K_M=400 µM for maleate V_max=15 µmol/min/mg enzyme for 2-methylmaleate hydration reaction V_max=1.5 µmol/min/mg enzyme for (R)-2-methylmalate dehydration reaction V_max=4.2 µmol/min/mg enzyme for 2-isopropylmalate dehydration reaction V_max=1.8 µmol/min/mg enzyme for 3-isopropylmalate dehydration reaction V_max=34 µmol/min/mg enzyme for maleate hydration reaction pH dependence: Optimum pH is 7.5. Temperature dependence: Optimum temperature is 70 degrees Celsius.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis Leucine biosynthesis
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	3-isopropylmalate dehydratase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	(R)-2-methylmalate dehydratase activity Inferred from electronic annotation. Source: EC 3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: HAMAP maleate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 168

168

Isopropylmalate/citramalate isomerase small subunit HAMAP-Rule MF_01032

PRO_0000141937

Secondary structure

168

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q58673 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A53C2CA883B6CCD7
Show »

FASTA

168

18,377

        10         20         30         40         50         60 
MRSIIKGRVW KFGNNVDTDA ILPARYLVYT KPEELAQFVM TGADPDFPKK VKPGDIIVGG 

        70         80         90        100        110        120 
KNFGCGSSRE HAPLGLKGAG ISCVIAESFA RIFYRNAINV GLPLIECKGI SEKVNEGDEL 

       130        140        150        160 
EVNLETGEIK NLTTGEVLKG QKLPEFMMEI LEAGGLMPYL KKKMAESQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L77117 Genomic DNA. Translation: AAB99283.1.

PIR

D64459.

RefSeq

NP_248273.1. NC_000909.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3VBA	X-ray	2.00	A/B/C/D/E/F	1-168	[»]

ProteinModelPortal

Q58673.

SMR

Q58673. Positions 4-167.

ModBase

Search...

Protein-protein interaction databases

STRING

243232.MJ1277.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAB99283; AAB99283; MJ_1277.

GeneID

1452175.

KEGG

mja:MJ_1277.

Phylogenomic databases

eggNOG

COG0066.

K01704.

OMA

FVIPYET.

ProtClustDB

CLSK876515.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13648.

SABIO-RK

Q58673.

UniPathway

UPA00047; UER00067.
UPA00048; UER00071.

Family and domain databases

Gene3D

3.20.19.10. 1 hit.

HAMAP

MF_01032. LeuD_type2. Divergent sequence.

InterPro

IPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR011827. IsopropMal_deHydtase_ssu.
[Graphical view]

PANTHER

PTHR11670. PTHR11670. 1 hit.

Pfam

PF00694. Aconitase_C. 1 hit.
[Graphical view]

SUPFAM

SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.

TIGRFAMs

TIGR02087. LEUD_arch. 1 hit.

ProtoNet

Search...

Entry information

Entry name

LEUD_METJA

Accession

Primary (citable) accession number: Q58673

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents