P30126 (LEUD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-isopropylmalate dehydratase small subunit
EC=4.2.1.33

Alternative name(s):
Alpha-IPM isomerase
Short name=IPMI
Isopropylmalate isomerase

Gene names

Name:	leuD
Ordered Locus Names:	b0071, JW0070

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. HAMAP-Rule MF_01031
Catalytic activity	(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01031
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01031
Subunit structure	Heterodimer of LeuC and LeuD By similarity.
Sequence similarities	Belongs to the LeuD family. LeuD type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	leucine biosynthetic process Inferred from direct assay PubMed 4587614. Source: EcoCyc
Cellular_component	3-isopropylmalate dehydratase complex Inferred from mutant phenotype PubMed 4587614. Source: EcoliWiki
Molecular_function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: HAMAP intramolecular transferase activity Inferred from direct assay PubMed 4587614. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 201	200	3-isopropylmalate dehydratase small subunit HAMAP-Rule MF_01031		PRO_0000141819

Sequences

	Sequence		Length	Mass (Da)
	P30126 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E5A98B58468E7787	FASTA	201	22,487
	10 20 30 40 50 60 MAEKFIKHTG LVVPLDAANV DTDAIIPKQF LQKVTRTGFG AHLFNDWRFL DEKGQQPNPD 70 80 90 100 110 120 FVLNFPQYQG ASILLARENF GCGSSREHAP WALTDYGFKV VIAPSFADIF YGNSFNNQLL 130 140 150 160 170 180 PVKLSDAEVD ELFALVKANP GIHFDVDLEA QEVKAGEKTY RFTIDAFRRH CMMNGLDSIG 190 200 LTLQHDDAIA AYEAKQPAFM N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC73182.1. AP009048 Genomic DNA. Translation: BAB96640.1.
PIR	S40585.
RefSeq	NP_414613.1. NC_000913.2. YP_488377.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P30126.
SMR	P30126. Positions 3-181.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10092N.
IntAct	P30126. 4 interactions.
STRING	511145.b0071.
2D gel databases
SWISS-2DPAGE	P30126.
Proteomic databases
PaxDb	P30126.
PRIDE	P30126.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73182; AAC73182; b0071. BAB96640; BAB96640; BAB96640.
GeneID	12933055. 945642.
KEGG	ecj:Y75_p0071. eco:b0071.
PATRIC	32115245. VBIEscCol129921_0074.
Organism-specific databases
EchoBASE	EB1535.
EcoGene	EG11575. leuD.
Phylogenomic databases
eggNOG	COG0066.
HOGENOM	HOG000222939.
KO	K01704.
OMA	KALFSDW.
ProtClustDB	PRK01641.
Enzyme and pathway databases
BioCyc	EcoCyc:LEUD-MONOMER. ECOL316407:JW0070-MONOMER. MetaCyc:LEUD-MONOMER.
UniPathway	UPA00048; UER00071.
Gene expression databases
Genevestigator	P30126.
Family and domain databases
Gene3D	3.20.19.10. 1 hit.
HAMAP	MF_01031. LeuD_type1.
InterPro	IPR004431. 3-IsopropMal_deHydase_ssu. IPR015937. Acoase/IPM_deHydtase. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF2. PTHR11670:SF2. 1 hit.
Pfam	PF00694. Aconitase_C. 1 hit. [Graphical view]
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
TIGRFAMs	TIGR00171. leuD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LEUD_ECOLI

Accession

Primary (citable) accession number: P30126

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program