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ECOLI:THD1

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ilvA
Protein Name(s) L-threonine dehydratase biosynthetic IlvA

Threonine deaminase

External Links
UniProt P04968
EMBL X04890
K03503
M10313
M11689
M32253
M87049
U00096
AP009048
M25497
PIR B27310
RefSeq NP_418220.1
YP_491666.1
PDB 1TDJ
PDBsum 1TDJ
ProteinModelPortal P04968
SMR P04968
DIP DIP-10018N
IntAct P04968
MINT MINT-1305200
STRING 511145.b3772
PaxDb P04968
PRIDE P04968
EnsemblBacteria AAC77492
BAE77525
GeneID 12930592
948287
KEGG ecj:Y75_p3403
eco:b3772
PATRIC 32123039
EchoBASE EB0488
EcoGene EG10493
eggNOG COG1171
HOGENOM HOG000046975
InParanoid P04968
KO K01754
OMA AHCFELC
OrthoDB EOG6ZSP7D
PhylomeDB P04968
BioCyc EcoCyc:THREDEHYDSYN-MONOMER
ECOL316407:JW3745-MONOMER
MetaCyc:THREDEHYDSYN-MONOMER
UniPathway UPA00047
EvolutionaryTrace P04968
PRO PR:P04968
Proteomes UP000000318
UP000000625
Genevestigator P04968
GO GO:0005737
GO:0016597
GO:0004794
GO:0030170
GO:0009082
GO:0009097
GO:0006566
InterPro IPR001721
IPR000634
IPR005787
IPR001926
Pfam PF00291
PF00585
SUPFAM SSF53686
TIGRFAMs TIGR01124
PROSITE PS51672
PS00165

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0030170

pyridoxal phosphate binding

PMID:5321308[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006566

threonine metabolic process

PMID:13405870[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10493
PANTHER:PTN002463966
PomBase:SPBC1677.03c
SGD:S000000888
TAIR:locus:2100078
UniProtKB:Q59P56

P

Seeded From UniProt

complete

involved_in

GO:0006567

threonine catabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002463966
SGD:S000000888

P

Seeded From UniProt

complete

involved_in

GO:0006566

threonine metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10493
PANTHER:PTN002463966
SGD:S000000888

P

Seeded From UniProt

complete

enables

GO:0004794

L-threonine ammonia-lyase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10493
PANTHER:PTN002463966
PomBase:SPBC1677.03c
SGD:S000000888
TAIR:locus:2100078

F

Seeded From UniProt

complete

enables

GO:0016597

amino acid binding

PMID:2005118[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

PMID:8407838[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

PMID:4604254[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009082

branched-chain amino acid biosynthetic process

PMID:348689[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004794

L-threonine ammonia-lyase activity

PMID:8407838[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004794

L-threonine ammonia-lyase activity

PMID:4604254[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004794

L-threonine ammonia-lyase activity

PMID:2005118[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030170

pyridoxal phosphate binding

PMID:2005118[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

PMID:4573981[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004794

L-threonine ammonia-lyase activity

PMID:4573981[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004794

L-threonine ammonia-lyase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005787

F

Seeded From UniProt

complete

involved_in

GO:0006520

cellular amino acid metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000634

P

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005787

P

Seeded From UniProt

complete

enables

GO:0030170

pyridoxal phosphate binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000634

F

Seeded From UniProt

complete

enables

GO:0004794

L-threonine ammonia-lyase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.3.1.19

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

Seeded From UniProt

complete

involved_in

GO:0009082

branched-chain amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0100

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

F

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0028

P

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0412
UniPathway:UPA00047

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Phillips, AT & Wood, WA (1965) The mechanism of action of 5'-adenylic acid-activated threonine dehydrase. J. Biol. Chem. 240 4703-9 PubMed GONUTS page
  2. UMBARGER, HE & BROWN, B (1957) Threonine deamination in Escherichia coli. II. Evidence for two L-threonine deaminases. J. Bacteriol. 73 105-12 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. 4.0 4.1 4.2 Eisenstein, E (1991) Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli. J. Biol. Chem. 266 5801-7 PubMed GONUTS page
  5. 5.0 5.1 Fisher, KE & Eisenstein, E (1993) An efficient approach to identify ilvA mutations reveals an amino-terminal catalytic domain in biosynthetic threonine deaminase from Escherichia coli. J. Bacteriol. 175 6605-13 PubMed GONUTS page
  6. 6.0 6.1 Favre, R et al. (1974) Complementation between different mutations in the ilvA gene of Escherichia coli K-12. J. Bacteriol. 119 1069-71 PubMed GONUTS page
  7. Williams, AL et al. (1978) Synthesis and activities of branched-chain aminoacyl-tRNA synthetases in threonine deaminase mutants of Escherichia coli. J. Bacteriol. 134 92-9 PubMed GONUTS page
  8. 8.0 8.1 Calhoun, DH et al. (1973) Threonine deaminase from Escherichia coli. I. Purification and properties. J. Biol. Chem. 248 3511-6 PubMed GONUTS page