Reviewed, UniProtKB/Swiss-Prot Q8YJC9 (LEUC_BRUME)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydratase large subunit
    EC=4.2.1.33
Alternative name(s):
    Isopropylmalate isomerase
    Alpha-IPM isomerase
      Short name=IPMI

Gene names

Name:	leuC
Ordered Locus Names:	BMEI0157

Organism

Brucella melitensis [Complete proteome] [HAMAP]

Taxonomic identifier

29459 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. HAMAP MF_01026
Catalytic activity	(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H2O. HAMAP MF_01026 (2S)-2-isopropylmaleate + H2O = (2S)-2-isopropylmalate. HAMAP 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 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 iron 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 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)
	Q8YJC9-1 [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: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008917 Genomic DNA. Translation: AAL51339.1.
PIR	AH3271.
RefSeq	NP_539075.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1195869.
GenomeReviews	Gene locus BMEI0157 in contig AE008917_GR.
KEGG	bme:BMEI0157.
NMPDR	fig|224914.1.peg.157.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8YJC9.
OMA	RPHAPKG
Enzyme and pathway databases
BioCyc	BMEL224914:BMEI0157-MON.
BRENDA	4.2.1.33. 277959.
Family and domain databases
HAMAP	MF_01026. [Tree]
InterPro	IPR004430. 3-IsopropMal_deHydase_lsu_regn. IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR015936. Homoacnase/3IPM_deHydtase_su. [Graphical view]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF6. Homoacnase/3IPM_dehydase_s/lsu. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
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:	November 24, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)