Q8YJC9 (LEUC_BRUME) 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:	BMEI0157

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella melitensis › Brucella melitensis bv. 1

Protein attributes

Sequence length	469 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 – 469	469	3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026		PRO_0000076713
Sites
	Metal binding	350	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	410	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	413	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YJC9 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 14442D949C40BCDF	FASTA	469	50,692
	10 20 30 40 50 60 MSAPRTLYDK IWDDHVVDQQ EDGTCLLYID RHLVHEVTSP QAFEGLHMAG RPVRHPEKTL 70 80 90 100 110 120 AVVDHNVPTS PDRINGIQNE ESRIQVEALA RNAADFGVEY YSERDKRQGI VHIVGPEQGF 130 140 150 160 170 180 TLPGMTIVCG DSHTSTHGAF GALAHGIGTS EVEHVLATQT LIQKKAKNML VRVDGKLPAG 190 200 210 220 230 240 VTAKDIVLAI IGEIGTAGGT GYVIEYAGEA IRSLSMEGRM TICNMSIEGG ARAGLIAPDE 250 260 270 280 290 300 TTFEYIKGRP RAPQGETLEQ AINYWKTLHS DEGAHFDKIV TLDAGSLPPI VSWGSSPEDV 310 320 330 340 350 360 VSVTGVVPNP DDIADETKRA SKWRALDYMG LKPGTKITDI AVDRVFIGSC TNGRIEDLRA 370 380 390 400 410 420 AAKVVEGKKV APTVNAMIVP GSGLVKEQAE AEGLHKIFIE AGFDWREPGC SMCLAMNDDR 430 440 450 460 LKPGERCAST SNRNFEGRQG FKGRTHLVSP AMAAAAAIAG HFVDIRAWK

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008917 Genomic DNA. Translation: AAL51339.1.
PIR	AH3271.
RefSeq	NP_539075.1. NC_003317.1.
3D structure databases
ProteinModelPortal	Q8YJC9.
ModBase	Search...
Protein-protein interaction databases
STRING	224914.BMEI0157.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL51339; AAL51339; BMEI0157.
GeneID	1195869.
KEGG	bme:BMEI0157.
PATRIC	17795361. VBIBruMel146950_0847.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000226972.
KO	K01703.
OMA	DIRQGIV.
ProtClustDB	PRK05478.
Enzyme and pathway databases
UniPathway	UPA00048; UER00071.
Family and domain databases
Gene3D	3.30.499.10. 3 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_BRUME

Accession

Primary (citable) accession number: Q8YJC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program