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ECOLI:ILVD

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ilvD (ECO:0000255 with HAMAP-Rule:MF_00012)
Protein Name(s) Dihydroxy-acid dehydratase (ECO:0000255 with HAMAP-Rule:MF_00012)

DAD (ECO:0000255 with HAMAP-Rule:MF_00012)

External Links
UniProt P05791
EMBL X04890
M10313
M87049
U00096
AP009048
M32253
X02413
K03503
PIR A27310
RefSeq YP_026248.1
YP_491667.1
ProteinModelPortal P05791
SMR P05791
DIP DIP-10021N
IntAct P05791
MINT MINT-1302071
STRING 511145.b3771
SWISS-2DPAGE P05791
PaxDb P05791
PRIDE P05791
EnsemblBacteria AAT48208
BAE77526
GeneID 12934335
948277
KEGG ecj:Y75_p3404
eco:b3771
PATRIC 32123037
EchoBASE EB0491
EcoGene EG10496
eggNOG COG0129
HOGENOM HOG000173155
InParanoid P05791
KO K01687
OMA QGRNMAG
OrthoDB EOG6MSS24
PhylomeDB P05791
BioCyc EcoCyc:DIHYDROXYACIDDEHYDRAT-MONOMER
ECOL316407:JW5605-MONOMER
MetaCyc:DIHYDROXYACIDDEHYDRAT-MONOMER
UniPathway UPA00047
UPA00049
PRO PR:P05791
Proteomes UP000000318
UP000000625
Genevestigator P05791
GO GO:0051539
GO:0004160
GO:0051536
GO:0046872
GO:0009097
GO:0009099
HAMAP MF_00012
InterPro IPR015928
IPR004404
IPR000581
IPR020558
PANTHER PTHR21000
Pfam PF00920
SUPFAM SSF52016
TIGRFAMs TIGR00110
PROSITE PS00886
PS00887

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004160

dihydroxy-acid dehydratase activity

PMID:13727223[1]

ECO:0000314

F

Fig. 1. As the concentration of the enzyme increases, concentration of the product of the reaction increases as well. The reaction is seen on the first page in the first paragraph.

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10496
PANTHER:PTN000470254

C

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:8325851[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051536

iron-sulfur cluster binding

PMID:8325851[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009099

valine biosynthetic process

PMID:8325851[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

PMID:13727223[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004160

dihydroxy-acid dehydratase activity

PMID:8325851[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000581
InterPro:IPR020558

F

Seeded From UniProt

complete

enables

GO:0004160

dihydroxy-acid dehydratase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004404

F

Seeded From UniProt

complete

involved_in

GO:0009082

branched-chain amino acid biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004404

P

Seeded From UniProt

complete

enables

GO:0004160

dihydroxy-acid dehydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.9

F

Seeded From UniProt

complete

involved_in

GO:0009099

valine biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001403

P

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001403

P

Seeded From UniProt

complete

enables

GO:0004160

dihydroxy-acid dehydratase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001403

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

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: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:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0004

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

enables

GO:0051536

iron-sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0411

F

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00047

P

Seeded From UniProt

complete

involved_in

GO:0009099

valine biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00049

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 MYERS, JW (1961) Dihydroxy acid dehydrase: an enzyme involved in the biosynthesis of isoleucine and valine. J. Biol. Chem. 236 1414-8 PubMed GONUTS page
  2. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Flint, DH et al. (1993) The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase. J. Biol. Chem. 268 14732-42 PubMed GONUTS page
  4. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page