A2RKR3 (LEUC_LACLM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	leuC
Ordered Locus Names:	llmg_1284

Organism

Lactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]

Taxonomic identifier

416870 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Lactococcus › Lactococcus lactis › Lactococcus lactis subsp. cremoris

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. HAMAP-Rule MF_01026
Catalytic activity	(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01026
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01026
Subunit structure	Heterodimer of LeuC and LeuD By similarity.
Sequence similarities	Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: HAMAP 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 458	458	3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026		PRO_1000063565
Sites
	Metal binding	339	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	399	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	402	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2RKR3 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: B1EB66517F7722C6	FASTA	458	50,244
	10 20 30 40 50 60 MSGQTIFDKL WNQHVIAGQE GEPQLLYIDL HVIHEVTSPQ AFQGLRDAGR SVRRRDLTYG 70 80 90 100 110 120 TLDHNVPTKD IFNIQDLISK KQIDTFTKNV KEFGIPAEAH GGKGQGIVHM VAPESGRTQP 130 140 150 160 170 180 GKIIVCGDSH TATNGAFGAI AFGIGTSEVE HVLATQTIWQ VKPKRMKIEF QGHPQKGVYS 190 200 210 220 230 240 KDFILALIAK YGVDAGVGYA VEYTGNAISD LSMEERMTIC NMSIEFGAKM GLMNPDEKTY 250 260 270 280 290 300 DYVKGREYAP KDFDEAVSKW EKLVSDSDAV YDKVLTLDVS QLKPMVTWGT NPGMGLEFGE 310 320 330 340 350 360 EFPKINDDLN YERAYQYMDL KPGQTASDID LGYIFIGSCT NARLGDLEEA AKIIKGNHIA 370 380 390 400 410 420 DGLTGIVVPG SRPVKRAAEE LGLDKIFKDA GFEWREPGCS ACLGMNPDQI PAYVHCASTS 430 440 450 NRNFEGRQGH NARTHLCSPA MAAAAAISGK FVDVREIV

References

[1]

"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363." Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J. J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MG1363.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM406671 Genomic DNA. Translation: CAL97877.1.
RefSeq	YP_001032591.1. NC_009004.1.
3D structure databases
ProteinModelPortal	A2RKR3.
ModBase	Search...
Protein-protein interaction databases
STRING	416870.llmg_1284.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL97877; CAL97877; llmg_1284.
GeneID	4796776.
KEGG	llm:llmg_1284.
PATRIC	22283737. VBILacLac4574_1324.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0065.
HOGENOM	HOG000226972.
KO	K01703.
OMA	DIRQGIV.
ProtClustDB	PRK05478.
Enzyme and pathway databases
UniPathway	UPA00048; UER00071.
Family and domain databases
Gene3D	3.30.499.10. 2 hits. 3.40.1060.10. 1 hit.
HAMAP	MF_01026. LeuC_type1.
InterPro	IPR004430. 3-IsopropMal_deHydase_lsu. IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR00170. leuC. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEUC_LACLM

Accession

Primary (citable) accession number: A2RKR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	March 6, 2007
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program