3-isopropylmalate dehydratase large subunit - Escherichia coli (strain K12)

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P0A6A6 (LEUC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	b0072, JW0071

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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_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. HAMAP MF_01026
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. HAMAP MF_01026
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from direct assay. Source: EcoCyc
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 intramolecular transferase activity Inferred from direct assay. Source: EcoCyc 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

Initiator methionine

Removed Ref.6 Ref.7 Ref.8

Chain

2 – 466

465

3-isopropylmalate dehydratase large subunit HAMAP MF_01026

PRO_0000076745

Sites

Metal binding

347

Iron-sulfur (4Fe-4S) By similarity

Metal binding

407

Iron-sulfur (4Fe-4S) By similarity

Metal binding

410

Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict

A → G in BAA21004. Ref.5

Sequence conflict

A → G in BAA21005. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6A6 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2B225514207C5EFA
Show »

FASTA

466

49,882

        10         20         30         40         50         60 
MAKTLYEKLF DAHVVYEAEN ETPLLYIDRH LVHEVTSPQA FDGLRAHGRP VRQPGKTFAT 

        70         80         90        100        110        120 
MDHNVSTQTK DINACGEMAR IQMQELIKNC KEFGVELYDL NHPYQGIVHV MGPEQGVTLP 

       130        140        150        160        170        180 
GMTIVCGDSH TATHGAFGAL AFGIGTSEVE HVLATQTLKQ GRAKTMKIEV QGKAAPGITA 

       190        200        210        220        230        240 
KDIVLAIIGK TGSAGGTGHV VEFCGEAIRD LSMEGRMTLC NMAIEMGAKA GLVAPDETTF 

       250        260        270        280        290        300 
NYVKGRLHAP KGKDFDDAVA YWKTLQTDEG ATFDTVVTLQ AEEISPQVTW GTNPGQVISV 

       310        320        330        340        350        360 
NDNIPDPASF ADPVERASAE KALAYMGLKP GIPLTEVAID KVFIGSCTNS RIEDLRAAAE 

       370        380        390        400        410        420 
IAKGRKVAPG VQALVVPGSG PVKAQAEAEG LDKIFIEAGF EWRLPGCSMC LAMNNDRLNP 

       430        440        450        460 
GERCASTSNR NFEGRQGRGG RTHLVSPAMA AAAAVTGHFA DIRNIK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Aphidicolin inhibits DNA polymerase II of Escherichia coli, an alpha-like DNA polymerase." Rosenthal E.R., Calvo J.M. Nucleic Acids Res. 18:7185-7186(1990) [PubMed: 2124684] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 70 AND 361. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus." Kirino H., Aoki M., Aoshima M., Hayashi Y., Ohba M., Yamagishi A., Wakagi T., Oshima T. Eur. J. Biochem. 220:275-281(1994) [PubMed: 8119295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205. Strain: K12.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[7]	"'98 Escherichia coli SWISS-2DPAGE database update." Tonella L., Walsh B.J., Sanchez J.-C., Ou K., Wilkins M.R., Tyler M., Frutiger S., Gooley A.A., Pescaru I., Appel R.D., Yan J.X., Bairoch A., Hoogland C., Morch F.S., Hughes G.J., Williams K.L., Hochstrasser D.F. Electrophoresis 19:1960-1971(1998) [PubMed: 9740056] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC73183.1. AP009048 Genomic DNA. Translation: BAB96641.2. D17631 Genomic DNA. Translation: BAA21004.1. D17632 Genomic DNA. Translation: BAA21005.1.
PIR	H64728.
RefSeq	NP_414614.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A6A6.
SMR	P0A6A6. Positions 2-462.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35834N.
IntAct	P0A6A6. 2 interactions.
2D gel databases
SWISS-2DPAGE	P0A6A6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000002539; EBESCP00000002539; EBESCG00000002073. EBESCT00000017453; EBESCP00000016744; EBESCG00000016509.
GeneID	945076.
GenomeReviews	Gene locus JW0071 in contig AP009048_GR. Gene locus b0072 in contig U00096_GR.
KEGG	ecj:JW0071. eco:b0072.
PATRIC	32115247. VBIEscCol129921_0075.
Organism-specific databases
EchoBASE	EB1536.
EcoGene	EG11576. leuC.
Phylogenomic databases
eggNOG	COG0065.
GeneTree	EBGT00050000008227.
HOGENOM	HBG330745.
OMA	DIRQGIV.
PhylomeDB	P0A6A6.
ProtClustDB	PRK05478.
Enzyme and pathway databases
BioCyc	EcoCyc:LEUC-MONOMER. MetaCyc:LEUC-MONOMER.
Gene expression databases
Genevestigator	P0A6A6.
Family and domain databases
HAMAP	MF_01026. LeuC_type1. [Tree]
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. 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.
KO	K01703.
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.
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_ECOLI

Accession

Primary (citable) accession number: P0A6A6
Secondary accession number(s): P30127, P78042, Q8FL77

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents