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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O.UniRule annotation2 Publications

Cofactori

[4Fe-4S] clusterUniRule annotation2 PublicationsNote: Binds 1 [4Fe-4S] cluster.UniRule annotation2 Publications

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-valine from pyruvate.UniRule annotation1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi122 – 1221Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi195 – 1951Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • dihydroxy-acid dehydratase activity Source: EcoCyc
  • iron-sulfur cluster binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • isoleucine biosynthetic process Source: EcoCyc
  • valine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:DIHYDROXYACIDDEHYDRAT-MONOMER.
ECOL316407:JW5605-MONOMER.
MetaCyc:DIHYDROXYACIDDEHYDRAT-MONOMER.
UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroxy-acid dehydrataseUniRule annotation (EC:4.2.1.9UniRule annotation)
Short name:
DADUniRule annotation
Gene namesi
Name:ilvDUniRule annotation
Ordered Locus Names:b3771, JW5605
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10496. ilvD.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 616615Dihydroxy-acid dehydratasePRO_0000103465Add
BLAST

Proteomic databases

EPDiP05791.
PaxDbiP05791.
PRIDEiP05791.

2D gel databases

SWISS-2DPAGEP05791.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4263329. 5 interactions.
DIPiDIP-10021N.
IntActiP05791. 1 interaction.
MINTiMINT-1302071.
STRINGi511145.b3771.

Structurei

3D structure databases

ProteinModelPortaliP05791.
SMRiP05791. Positions 198-568.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C01. Bacteria.
COG0129. LUCA.
HOGENOMiHOG000173155.
InParanoidiP05791.
KOiK01687.
OMAiQGRNMAG.
OrthoDBiEOG6MSS24.
PhylomeDBiP05791.

Family and domain databases

HAMAPiMF_00012. IlvD.
InterProiIPR015928. Aconitase/3IPM_dehydase_swvl.
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERiPTHR21000. PTHR21000. 2 hits.
PfamiPF00920. ILVD_EDD. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR00110. ilvD. 1 hit.
PROSITEiPS00886. ILVD_EDD_1. 1 hit.
PS00887. ILVD_EDD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05791-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKYRSATTT HGRNMAGARA LWRATGMTDA DFGKPIIAVV NSFTQFVPGH
60 70 80 90 100
VHLRDLGKLV AEQIEAAGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRELI
110 120 130 140 150
ADSVEYMVNA HCADAMVCIS NCDKITPGML MASLRLNIPV IFVSGGPMEA
160 170 180 190 200
GKTKLSDQII KLDLVDAMIQ GADPKVSDSQ SDQVERSACP TCGSCSGMFT
210 220 230 240 250
ANSMNCLTEA LGLSQPGNGS LLATHADRKQ LFLNAGKRIV ELTKRYYEQN
260 270 280 290 300
DESALPRNIA SKAAFENAMT LDIAMGGSTN TVLHLLAAAQ EAEIDFTMSD
310 320 330 340 350
IDKLSRKVPQ LCKVAPSTQK YHMEDVHRAG GVIGILGELD RAGLLNRDVK
360 370 380 390 400
NVLGLTLPQT LEQYDVMLTQ DDAVKNMFRA GPAGIRTTQA FSQDCRWDTL
410 420 430 440 450
DDDRANGCIR SLEHAYSKDG GLAVLYGNFA ENGCIVKTAG VDDSILKFTG
460 470 480 490 500
PAKVYESQDD AVEAILGGKV VAGDVVVIRY EGPKGGPGMQ EMLYPTSFLK
510 520 530 540 550
SMGLGKACAL ITDGRFSGGT SGLSIGHVSP EAASGGSIGL IEDGDLIAID
560 570 580 590 600
IPNRGIQLQV SDAELAARRE AQDARGDKAW TPKNRERQVS FALRAYASLA
610
TSADKGAVRD KSKLGG
Length:616
Mass (Da):65,532
Last modified:January 23, 2007 - v5
Checksum:i6F6DA053CFDA475B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 2423PKYRS…ALWRA → VVIWRVLVRCGP in AAA24023 (PubMed:3550695).CuratedAdd
BLAST
Sequence conflicti164 – 1641L → P in AAA24023 (PubMed:3550695).Curated
Sequence conflicti408 – 43730CIRSL…GCIVK → VSARWNTPTAKTAAWRCSTV ILRKRLHRE in AAA24023 (PubMed:3550695).CuratedAdd
BLAST
Sequence conflicti610 – 6101D → H in AAA24023 (PubMed:3550695).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04890 Genomic DNA. Translation: CAA28576.1.
M10313 Genomic DNA. Translation: AAB59053.1.
M87049 Genomic DNA. Translation: AAA67574.1.
U00096 Genomic DNA. Translation: AAT48208.1.
AP009048 Genomic DNA. Translation: BAE77526.1.
M32253 Genomic DNA. Translation: AAA24023.1.
X02413 Genomic DNA. Translation: CAA26263.1.
K03503 Genomic DNA. Translation: AAA24013.1.
PIRiA27310. DWECDA.
RefSeqiWP_001127399.1. NZ_LN832404.1.
YP_026248.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48208; AAT48208; b3771.
BAE77526; BAE77526; BAE77526.
GeneIDi948277.
KEGGiecj:JW5605.
eco:b3771.
PATRICi32123037. VBIEscCol129921_3888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04890 Genomic DNA. Translation: CAA28576.1.
M10313 Genomic DNA. Translation: AAB59053.1.
M87049 Genomic DNA. Translation: AAA67574.1.
U00096 Genomic DNA. Translation: AAT48208.1.
AP009048 Genomic DNA. Translation: BAE77526.1.
M32253 Genomic DNA. Translation: AAA24023.1.
X02413 Genomic DNA. Translation: CAA26263.1.
K03503 Genomic DNA. Translation: AAA24013.1.
PIRiA27310. DWECDA.
RefSeqiWP_001127399.1. NZ_LN832404.1.
YP_026248.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP05791.
SMRiP05791. Positions 198-568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263329. 5 interactions.
DIPiDIP-10021N.
IntActiP05791. 1 interaction.
MINTiMINT-1302071.
STRINGi511145.b3771.

2D gel databases

SWISS-2DPAGEP05791.

Proteomic databases

EPDiP05791.
PaxDbiP05791.
PRIDEiP05791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48208; AAT48208; b3771.
BAE77526; BAE77526; BAE77526.
GeneIDi948277.
KEGGiecj:JW5605.
eco:b3771.
PATRICi32123037. VBIEscCol129921_3888.

Organism-specific databases

EchoBASEiEB0491.
EcoGeneiEG10496. ilvD.

Phylogenomic databases

eggNOGiENOG4105C01. Bacteria.
COG0129. LUCA.
HOGENOMiHOG000173155.
InParanoidiP05791.
KOiK01687.
OMAiQGRNMAG.
OrthoDBiEOG6MSS24.
PhylomeDBiP05791.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.
BioCyciEcoCyc:DIHYDROXYACIDDEHYDRAT-MONOMER.
ECOL316407:JW5605-MONOMER.
MetaCyc:DIHYDROXYACIDDEHYDRAT-MONOMER.

Miscellaneous databases

PROiP05791.

Family and domain databases

HAMAPiMF_00012. IlvD.
InterProiIPR015928. Aconitase/3IPM_dehydase_swvl.
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERiPTHR21000. PTHR21000. 2 hits.
PfamiPF00920. ILVD_EDD. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR00110. ilvD. 1 hit.
PROSITEiPS00886. ILVD_EDD_1. 1 hit.
PS00887. ILVD_EDD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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], PATHWAY.
    Strain: K12.
  3. "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.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: SEQUENCE REVISION.
  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. "Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence."
    Kuramitsu S., Ogawa T., Ogawa H., Kagamiyama H.
    J. Biochem. 97:993-999(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
    Strain: K12.
  8. Garrison E., Harms E.H., Umbarger H.E.
    Submitted (JUN-1987) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 575-616.
  9. "The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase."
    Flint D.H., Emptage M.H., Finnegan M.G., Fu W., Johnson M.K.
    J. Biol. Chem. 268:14732-14742(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-23, CATALYTIC ACTIVITY, COFACTOR, PRESENCE OF A 4FE--4S IRON-SULFUR CLUSTER, SUBUNIT.
    Strain: K12 / JA221 / ATCC 33875 / DSM 5209.
  10. "Dihydroxy-acid dehydratase, a 4Fe-4S cluster-containing enzyme in Escherichia coli: effects of intracellular superoxide dismutase on its inactivation by oxidant stress."
    Brown O.R., Smyk-Randall E., Draczynska-Lusiak B., Fee J.A.
    Arch. Biochem. Biophys. 319:10-22(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, PRESENCE OF A 4FE--4S IRON-SULFUR CLUSTER.

Entry informationi

Entry nameiILVD_ECOLI
AccessioniPrimary (citable) accession number: P05791
Secondary accession number(s): Q2M880
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 158 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.