Reviewed, UniProtKB/Swiss-Prot P04968 (THD1_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-threonine ammonia-lyase activity Inferred from electronic annotation. Source: EC 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

62

1

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

120

1

A → R Ref.2

Sequence conflict

140

1

A → R in AAA24014. Ref.2

Sequence conflict

140

1

A → R in AAA67575. Ref.2

Sequence conflict

195

1

G → C in AAA24014. Ref.2

Sequence conflict

243

1

A → G in AAA24024. Ref.3

Sequence conflict

334

1

G → V in AAA24014. Ref.2

Secondary structure

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514

Helix Strand Turn

Details...

Helix

13 – 22

10

Helix

25 – 27

3

Beta strand

34 – 36

3

Helix

38 – 43

6

Beta strand

46 – 51

6

Helix

53 – 55

3

Beta strand

59 – 61

3

Helix

63 – 71

9

Turn

72 – 75

4

Beta strand

79 – 81

3

Beta strand

83 – 86

4

Beta strand

88 – 90

3

Helix

91 – 100

10

Beta strand

105 – 108

4

Helix

115 – 124

10

Beta strand

127 – 129

3

Helix

135 – 149

15

Helix

160 – 176

17

Beta strand

182 – 186

5

Beta strand

188 – 190

3

Helix

191 – 203

13

Beta strand

208 – 214

7

Turn

215 – 217

3

Helix

219 – 226

8

Beta strand

237 – 240

4

Helix

250 – 255

6

Beta strand

261 – 265

5

Helix

267 – 279

13

Helix

287 – 303

17

Beta strand

309 – 313

5

Helix

323 – 335

13

Beta strand

338 – 344

7

Beta strand

347 – 350

4

Helix

353 – 357

5

Beta strand

360 – 370

11

Beta strand

374 – 376

3

Beta strand

378 – 384

7

Helix

389 – 399

11

Beta strand

401 – 403

3

Beta strand

405 – 407

3

Helix

413 – 417

5

Helix

419 – 421

3

Beta strand

434 – 439

6

Helix

446 – 454

9

Beta strand

462 – 464

3

Turn

468 – 470

3

Beta strand

475 – 479

5

Beta strand

498 – 501

4

Helix

506 – 511

6

Sequences

	Sequence		Length	Mass (Da)
	P04968-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 9D389A0EDD8DE692	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

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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_004024.1.
NP_418220.1.

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10018N.

2-D gel databases

ECO2DBASE

F050.1. 6TH EDITION.

Genome annotation databases

GeneID

948287.

GenomeReviews

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

KEGG

ecj:JW3745.
eco:b3772.

Organism-specific databases

EchoBASE

EB0488.

EcoGene

EG10493. ilvA.

CMR

Search...

Phylogenomic databases

HOGENOM

P04968.

OMA

P04968. YIAPFDD.

Enzyme and pathway databases

BioCyc

EcoCyc:THREDEHYDSYN-MON.
MetaCyc:THREDEHYDSYN-MON.

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]

Pfam

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

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:	June 16, 2009
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)