O59391 (LEUC_PYRHO) 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:	PH1726

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	380 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. HAMAP MF_01027
Catalytic activity	(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H2O. HAMAP MF_01027 (2S)-2-isopropylmaleate + H2O = (2S)-2-isopropylmalate. HAMAP MF_01027
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP MF_01027
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP MF_01027
Subunit structure	Heterodimer of LeuC and LeuD By similarity. HAMAP MF_01027
Sequence similarities	Belongs to the aconitase/IPM isomerase family. LeuC type 2 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: UniProtKB-KW
Molecular function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: EC 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 – 380	380	3-isopropylmalate dehydratase large subunit HAMAP MF_01027		PRO_0000076882
Sites
	Metal binding	262	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	320	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	323	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O59391 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 05BBAA1227B59E9A	FASTA	380	41,054
	10 20 30 40 50 60 MTLVEEILDA KAGEVVIRNV DLVYAHDGTM PLIIEAFNKV FNSVKARAYV FFDHVYPAPT 70 80 90 100 110 120 VKVANLQKEI REFARRHGIP VVEGKGISHQ LVVEMGLAEK SRIVVGGDSH TPTLGALGVF 130 140 150 160 170 180 AVGMGATDVA VVLGLGKTWL RVPESVAVIF EGKPSRTTMA ADVMIRLITS LRNYDMNYKA 190 200 210 220 230 240 LEFFNVPFTA DERLTLTNFS VEANAKTALI GEEYDGRNYI KEISFELSSL GPMVAKPFSP 250 260 270 280 290 300 ANGVEVEKVE GTKIDQVFIG SCTNGRFEHI KRAAEILKGE EVAVRTIIGP ASVNVYKRMV 310 320 330 340 350 360 REGIVDILLD AGATILPPGC GPCLGRHMGV LGDKEVVLST TNRNFRGRMG SPTAEIYLAS 370 380 PLTAAVSALY GEITSPGGEV

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000001 Genomic DNA. Translation: BAA30840.1.
PIR	A71181.
RefSeq	NP_143565.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O59391.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000001481; EBPYRP00000001481; EBPYRG00000001481.
GeneID	1442570.
GenomeReviews	Gene locus PH1726 in contig BA000001_GR.
KEGG	pho:PH1726.
NMPDR	fig|70601.1.peg.1684.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000022452.
HOGENOM	HBG330745.
OMA	VEVDQVM.
ProtClustDB	PRK00402.
Enzyme and pathway databases
BioCyc	PHOR70601:PH1726-MONOMER.
Family and domain databases
HAMAP	MF_01027. LeuC_type2. [Tree]
InterPro	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. IPR011826. HAcnase/IPMdehydase_lsu_prok. IPR006251. Homoacnase/IPMdehydase_lsu. [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.
KO	K01703.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF16. PTHR11670:SF16. 1 hit.
Pfam	PF00330. Aconitase. 2 hits. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR02086. IPMI_arch. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEUC_PYRHO

Accession

Primary (citable) accession number: O59391

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	August 1, 1998
Last modified:	November 16, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program