O59393 (LEUD_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-isopropylmalate dehydratase small subunit
EC=4.2.1.33

Alternative name(s):
Alpha-IPM isomerase
Short name=IPMI
Isopropylmalate isomerase

Gene names

Name:	leuD
Ordered Locus Names:	PH1724

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	163 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. HAMAP MF_01032
Catalytic activity	(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H2O. HAMAP MF_01032 (2S)-2-isopropylmaleate + H2O = (2S)-2-isopropylmalate. HAMAP MF_01032
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP MF_01032
Subunit structure	Heterodimer of LeuC and LeuD By similarity. HAMAP MF_01032
Sequence similarities	Belongs to the LeuD family. LeuD type 2 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	3-isopropylmalate dehydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 163

163

3-isopropylmalate dehydratase small subunit HAMAP MF_01032

PRO_0000141949

Secondary structure

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163

Helix Strand Turn

Details...

Beta strand

2 – 9

8

Helix

16 – 19

4

Helix

30 – 36

7

Turn

37 – 41

5

Helix

45 – 48

4

Beta strand

54 – 56

3

Beta strand

59 – 61

3

Helix

69 – 77

9

Beta strand

81 – 85

5

Helix

89 – 98

10

Beta strand

102 – 105

4

Beta strand

115 – 119

5

Turn

120 – 123

4

Beta strand

124 – 127

4

Beta strand

130 – 133

4

Helix

139 – 146

8

Helix

150 – 156

7

Sequences

	Sequence		Length	Mass (Da)
	O59393 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: AEFBDDE1CBCDD266	FASTA	163	18,011
	10 20 30 40 50 60 MITTGKVWKF GDDISTDEIT PGRYNLTKDP KELAKIAFIE VRPDFARNVR PGDVVVAGKN 70 80 90 100 110 120 FGIGSSRESA ALALKALGIA GVIAESFGRI FYRNAINIGI PLLLGKTEGL KDGDLVTVNW 130 140 150 160 ETGEVRKGDE ILMFEPLEDF LLEIVREGGI LEYIRRRGDL CIR

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.

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Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30838.1.

PIR

G71180.

RefSeq

NP_143564.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V7L	X-ray	1.98	A/B	1-163	[»]

ProteinModelPortal

O59393.

SMR

O59393. Positions 1-163.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000001527; EBPYRP00000001527; EBPYRG00000001527.

GeneID

1442569.

GenomeReviews

Gene locus PH1724 in contig BA000001_GR.

KEGG

pho:PH1724.

NMPDR

fig|70601.1.peg.1683.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022453.

HOGENOM

HBG304838.

OMA

ITPGRYN.

PhylomeDB

O59393.

ProtClustDB

PRK00439.

Enzyme and pathway databases

BioCyc

PHOR70601:PH1724-MONOMER.

Family and domain databases

HAMAP

MF_01032. LeuD_type2.
[Tree]

InterPro

IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR011827. IsopropMal_deHydtase_ssu.
[Graphical view]

Gene3D

G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit.

KO

K01704.

Pfam

PF00694. Aconitase_C. 1 hit.
[Graphical view]

SUPFAM

SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.

TIGRFAMs

TIGR02087. LEUD_arch. 1 hit.

ProtoNet

Search...

Entry information

Entry name

LEUD_PYRHO

Accession

Primary (citable) accession number: O59393

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program