Q7ZAG7 (LEUC_HALVD) 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:	HVO_1504

Organism

Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) [Complete proteome] [HAMAP]

Taxonomic identifier

309800 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloferax › Haloferax volcanii

Protein attributes

Sequence length	473 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.
Sequence caution	The sequence CAE00173.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 473	473	3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026		PRO_0000076852
Sites
	Metal binding	348	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	408	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	411	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7ZAG7 [UniParc]. Last modified January 10, 2006. Version 2. Checksum: 226A11315F3929CD	FASTA	473	51,620
	10 20 30 40 50 60 MSEGTLYDKV WEEHTVSELP TGQTQLFCGL HLIHEVTSPQ AFGMLQERDL EVAYPNRTHA 70 80 90 100 110 120 TVDHIVPTSD QSRPFRDDAA EEMMAELEQN VREAGINFSD PTSGEQGIVH VIGPEKGLTQ 130 140 150 160 170 180 PGMTIVCGDS HTSTHGAFGA LAFGIGTSQI RDVLATQTVA MEKKKVRKIE VTGELGPGVE 190 200 210 220 230 240 AKDVILEIIR RLGTEGGVGY VYEYAGEAIE DLDMEGRMSI CNMSIEGGAR AGYVNPDETT 250 260 270 280 290 300 YEWLKETEYF QENPERFDEL KPYWESIRSD EDAEYDDVVT IDGSELEPVV TWGTTPGQGV 310 320 330 340 350 360 GITQPIPAPE DLPEEKQETA RMAQEHMGVT PGETMEGYEI DVAFLGSCTN ARLPDLRRAA 370 380 390 400 410 420 GVVKGRQVAD SVRAMVVPGS QRVKAAAEAE GLDEVFKEAG FEWREAGCSM CLGMNEDQLE 430 440 450 460 470 GDEASASSSN RNFIGRQGSK DGRTVLMNPR MVAAAAVTGE VTDVRELKEV TTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes." Allers T., Ngo H.-P., Mevarech M., Lloyd R.G. Appl. Environ. Microbiol. 70:943-953(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DS2 / DS70.
[2]	"The complete genome sequence of Haloferax volcanii DS2, a model archaeon." Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A. PLoS ONE 5:E9605-E9605(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ571689 Genomic DNA. Translation: CAE00173.1. Different initiation. CP001956 Genomic DNA. Translation: ADE02591.1.
RefSeq	YP_003535553.1. NC_013967.1.
3D structure databases
ProteinModelPortal	Q7ZAG7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADE02591; ADE02591; HVO_1504.
GeneID	8926493.
KEGG	hvo:HVO_1504.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000226972.
KO	K01703.
OMA	DIRQGIV.
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_HALVD

Accession

Primary (citable) accession number: Q7ZAG7
Secondary accession number(s): D4GYF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	January 10, 2006
Last modified:	April 3, 2013
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program