L-threonine dehydratase biosynthetic IlvA - Escherichia coli (strain K12)

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P04968 (ILVA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 137. History...

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

Documents (4) |

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:
L-threonine dehydratase biosynthetic IlvA
EC=4.3.1.19

Alternative name(s):
Threonine deaminase

Gene names

Name:	ilvA
Ordered Locus Names:	b3772, JW3745

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. Ref.10
Catalytic activity	L-threonine = 2-oxobutanoate + NH₃.
Cofactor	Pyridoxal phosphate. Ref.11
Enzyme regulation	Isoleucine allosterically inhibits whereas valine allosterically activates this enzyme. Ref.9
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
Subunit structure	Homotetramer. Ref.13
Induction	Constitutively expressed. Ref.9 Ref.10
Sequence similarities	Belongs to the serine/threonine dehydratase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from direct assay PubMed 4573981. Source: EcoCyc threonine metabolic process Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	L-threonine ammonia-lyase activity Inferred from direct assay PubMed 4573981. Source: EcoCyc amino acid binding Inferred from direct assay PubMed 2005118. Source: EcoliWiki pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 514

514

L-threonine dehydratase biosynthetic IlvA

PRO_0000185573

Regions

Region

189 – 192

Pyridoxal phosphate binding

Sites

Binding site

Pyridoxal phosphate

Binding site

315

Pyridoxal phosphate

Amino acid modifications

Modified residue

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

120

A → R in AAA24014. Ref.2

Sequence conflict

140

A → R in AAA24014. Ref.2

Sequence conflict

140

A → R in AAA67575. Ref.2

Sequence conflict

195

G → C in AAA24014. Ref.2

Sequence conflict

243

A → G in AAA24024. Ref.3

Sequence conflict

334

G → V in AAA24014. Ref.2

Secondary structure

514

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04968 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 9D389A0EDD8DE692
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FASTA

514

56,195

        10         20         30         40         50         60 
MADSQPLSGA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV KREDRQPVHS 

        70         80         90        100        110        120 
FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR LGVKALIVMP TATADIKVDA 

       130        140        150        160        170        180 
VRGFGGEVLL HGANFDEAKA KAIELSQQQG FTWVPPFDHP MVIAGQGTLA LELLQQDAHL 

       190        200        210        220        230        240 
DRVFVPVGGG GLAAGVAVLI KQLMPQIKVI AVEAEDSACL KAALDAGHPV DLPRVGLFAE 

       250        260        270        280        290        300 
GVAVKRIGDE TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI 

       310        320        330        340        350        360 
ALHNIRGERL AHILSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG SFLKFCQLLG 

       370        380        390        400        410        420 
GRSVTEFNYR FADAKNACIF VGVRLSRGLE ERKEILQMLN DGGYSVVDLS DDEMAKLHVR 

       430        440        450        460        470        480 
YMVGGRPSHP LQERLYSFEF PESPGALLRF LNTLGTYWNI SLFHYRSHGT DYGRVLAAFE 

       490        500        510 
LGDHEPDFET RLNELGYDCH DETNNPAFRF FLAG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete nucleotide sequence of the ilvGMEDA cluster of Escherichia coli K-12." Cox J.L., Cox B.J., Fidanza V., Calhoun D.H. Gene 56:185-198(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	Garrison E., Harms E., Umbarger H.E. Submitted (AUG-1986) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12." Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E., Hatfield G.W. Nucleic Acids Res. 15:2137-2155(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R. Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Nucleotide sequence and in vivo expression of the ilvY and ilvC genes in Escherichia coli K12. Transcription from divergent overlapping promoters." Wek R.C., Hatfield G.W. J. Biol. Chem. 261:2441-2450(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 439-514. Strain: K12.
[8]	"Physical identification of an internal promoter, ilvAp, in the distal portion of the ilvGMEDA operon." Lopes J.M., Lawther R.P. Gene 76:255-269(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10. Strain: K12.
[9]	"Evidence for a negative-feedback mechanism in the biosynthesis of isoleucine." Umbarger H.E. Science 123:848-848(1956) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[10]	"Threonine deamination in Escherichia coli. II. Evidence for two L-threonine deaminases." Umbarger H.E., Brown B. J. Bacteriol. 73:105-112(1957) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A THREONINE DEHYDRATASE AND IN THE L-ISOLEUCINE BIOSYNTHESIS, INDUCTION.
[11]	"The mechanism of action of 5'-adenylic acid-activated threonine dehydrase." Phillips A.T., Wood W.A. J. Biol. Chem. 240:4703-4709(1965) [PubMed] [Europe PMC] [Abstract] Cited for: REACTION MECHANISM, COFACTOR.
[12]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[13]	"Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase." Gallagher D.T., Gilliland G.L., Xiao G., Zondlo J., Fisher K.E., Chinchilla D., Eisenstein E. Structure 6:465-475(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04890 Genomic DNA. Translation: CAA28577.1.
K03503 Genomic DNA. Translation: AAA24014.1.
M10313 Genomic DNA. Translation: AAB59054.1.
M11689 Genomic DNA. Translation: AAA24027.1.
M32253 Genomic DNA. Translation: AAA24024.1.
M87049 Genomic DNA. Translation: AAA67575.1.
U00096 Genomic DNA. Translation: AAC77492.1.
AP009048 Genomic DNA. Translation: BAE77525.1.
M25497 Genomic DNA. Translation: AAA24015.1.

PIR

DWECTS. B27310.

RefSeq

NP_418220.1. NC_000913.2.
YP_491666.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TDJ	X-ray	2.80	A	1-514	[»]

ProteinModelPortal

P04968.

SMR

P04968. Positions 5-514.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10018N.

IntAct

P04968. 9 interactions.

MINT

MINT-1305200.

STRING

511145.b3772.

Proteomic databases

PaxDb

P04968.

PRIDE

P04968.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77492; AAC77492; b3772.
BAE77525; BAE77525; BAE77525.

GeneID

12930592.
948287.

KEGG

ecj:Y75_p3403.
eco:b3772.

PATRIC

32123039. VBIEscCol129921_3889.

Organism-specific databases

EchoBASE

EB0488.

EcoGene

EG10493. ilvA.

Phylogenomic databases

eggNOG

COG1171.

HOGENOM

HOG000046975.

K01754.

OMA

AAYYKAV.

ProtClustDB

PRK09224.

Enzyme and pathway databases

BioCyc

EcoCyc:THREDEHYDSYN-MONOMER.
ECOL316407:JW3745-MONOMER.
MetaCyc:THREDEHYDSYN-MONOMER.

UniPathway

UPA00047; UER00054.

Gene expression databases

Genevestigator

P04968.

Family and domain databases

InterPro

IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001721. Thr_deHydtase_C_reg_dom.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]

Pfam

PF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view]

SUPFAM

SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.

TIGRFAMs

TIGR01124. ilvA_2Cterm. 1 hit.

PROSITE

PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P04968.

Entry information

Entry name

ILVA_ECOLI

Accession

Primary (citable) accession number: P04968
Secondary accession number(s): Q2M881

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	November 1, 1988
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents