Threonine dehydratase biosynthetic - Escherichia coli (strain K12)

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P04968 (THD1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 126. 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:
Threonine dehydratase biosynthetic
EC=4.3.1.19

Alternative name(s):
Threonine deaminase

Gene names

Name:	ilvA
Ordered Locus Names:	b3772, JW3745

Organism

Escherichia coli (strain K12)

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 formation of alpha-ketobutyrate from threonine in a two-step reaction. The first step is a dehydration of threonine, followed by rehydration and liberation of ammonia. Deaminates L-threonine, but also L-serine to a lesser extent.
Catalytic activity	L-threonine = 2-oxobutanoate + NH₃.
Cofactor	Pyridoxal phosphate.
Enzyme regulation	Isoleucine allosterically inhibits whereas valine allosterically activates this enzyme.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
Subunit structure	Homotetramer. Ref.9
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. Source: EcoCyc
Cellular component	cytoplasm Inferred by curator. Source: EcoliWiki
Molecular function	L-threonine ammonia-lyase activity Inferred from direct assay. Source: EcoCyc amino acid binding Inferred from direct assay. 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

Threonine dehydratase biosynthetic

PRO_0000185573

Amino acid modifications

Modified residue

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

120

A → R 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
Show »

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: 3315862] [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: 3550695] [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: 1379743] [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: 9278503] [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: 16738553] [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: 3003115] [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: 2473940] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10. Strain: K12.
[9]	"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: 9562556] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-62.
+	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.

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.

2D gel databases

ECO2DBASE

F050.1. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003513; EBESCP00000003513; EBESCG00000002874.
EBESCT00000003514; EBESCP00000003514; EBESCG00000002874.
EBESCT00000003515; EBESCP00000003515; EBESCG00000002874.
EBESCT00000003516; EBESCP00000003516; EBESCG00000002874.
EBESCT00000017647; EBESCP00000016938; EBESCG00000016703.

GeneID

948287.

GenomeReviews

Gene locus JW3745 in contig AP009048_GR.
Gene locus b3772 in contig U00096_GR.

KEGG

ecj:JW3745.
eco:b3772.

PATRIC

32123039. VBIEscCol129921_3889.

Organism-specific databases

EchoBASE

EB0488.

EcoGene

EG10493. ilvA.

Phylogenomic databases

eggNOG

COG1171.

GeneTree

EBGT00050000009483.

HOGENOM

HBG714501.

OMA

YIAPFDD.

PhylomeDB

P04968.

ProtClustDB

PRK09224.

Enzyme and pathway databases

BioCyc

EcoCyc:THREDEHYDSYN-MONOMER.
MetaCyc:THREDEHYDSYN-MONOMER.

Gene expression databases

Genevestigator

P04968.

Family and domain databases

InterPro

IPR001926. PyrdxlP-dep_enz_bsu.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_1.
IPR001721. Thr_deHydtase_C.
[Graphical view]

K01754.

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...

Entry information

Entry name

THD1_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:	January 25, 2012
This is version 126 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

Amino acid modifications

Experimental info

Secondary structure

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