B5ENJ1 (LEUC_ACIF5) 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:	Lferr_0775

Organism

Acidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP]

Taxonomic identifier

380394 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus › Thiobacillus ferrooxidans

Protein attributes

Sequence length	470 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 – 470	470	3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026		PRO_1000135658
Sites
	Metal binding	348	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	409	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	412	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B5ENJ1 [UniParc]. Last modified October 14, 2008. Version 1. Checksum: ADD01E679CA01E97	FASTA	470	50,109
	10 20 30 40 50 60 MSAKTLYDKL WESHVVHTEQ DGGVLLYIDR QLLHEVTSPQ AFSGLRAAGR KAWRIDANIA 70 80 90 100 110 120 TADHNVPTTD RAAGIADATS RLQVDTLDRN CAEFGIEEFG MHDKRQGIVH VIAPEQGLTL 130 140 150 160 170 180 PGMTVVCGDS HTATHGALGA LAFGIGTTEV EHVLATQCLW ARKSRSMRIW VEGELGNGVT 190 200 210 220 230 240 AKDLVLAIIG RIGTAGGTGY AIEFAGPAVH ALSVEGRMTL CNMAIEAGAR SGMVGVDAVT 250 260 270 280 290 300 IDYLRGRPYA PVGKIWDQAV AVWGELHSDP DAQFDAEIRL EATDVAPQVT WGTSPEMVVD 310 320 330 340 350 360 ISARVPDPAL EKDPVRRKGW SDALAYMDLA AATPISSIAL DKVFIGSCTN ARIEDLRAAA 370 380 390 400 410 420 AVARGHHKAA SVKAVLVVPG SGLVKAQAEA EGLDRIFRDA GFEWREPGCS MCLAMNADRL 430 440 450 460 470 EPGERCASTS NRNFEGRQGA GGRTHLVSPA MAAAAAIAGH FVDVRDWIMH

References

[1]

"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 53993.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001132 Genomic DNA. Translation: ACH83025.1.
RefSeq	YP_002219232.1. NC_011206.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	380394.Lferr_0775.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACH83025; ACH83025; Lferr_0775.
GeneID	6876739.
KEGG	afe:Lferr_0775.
PATRIC	20659122. VBIAciFer6930_0774.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0065.
HOGENOM	HOG000226972.
KO	K01703.
OMA	DIRQGIV.
ProtClustDB	PRK05478.
Enzyme and pathway databases
BioCyc	AFER380394:GHE0-790-MONOMER.
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_ACIF5

Accession

Primary (citable) accession number: B5ENJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	October 14, 2008
Last modified:	May 1, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program