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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster.UniRule annotation

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (ilvI)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
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 annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (ilvI)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
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 bindingi193 – 1931Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciPAER208963:GI5K-370-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:PA14_04630
OrganismiPseudomonas aeruginosa (strain UCBPP-PA14)
Taxonomic identifieri208963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000000653 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 612612Dihydroxy-acid dehydratasePRO_1000001034Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ02U62.
SMRiQ02U62. Positions 196-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000173155.
KOiK01687.
OMAiQGRNMAG.
OrthoDBiEOG6MSS24.

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.

Q02U62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDYRSKTST HGRNMAGARA LWRATGMKDE DFKKPIIAIA NSFTQFVPGH
60 70 80 90 100
VHLKDLGQLV AREIEKAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSREII
110 120 130 140 150
ADSVEYMVNA HCADAIVCIS NCDKITPGML MAALRLNIPV VFVSGGPMEA
160 170 180 190 200
GKTKLASHGL DLVDAMVVAA DDSCSDEKVA EYERSACPTC GSCSGMFTAN
210 220 230 240 250
SMNCLTEALG LSLPGNGSTL ATHADREQLF LRAGRLAVEL CQRYYGEGDD
260 270 280 290 300
SVLPRNIANF KAFENAMTLD IAMGGSTNTI LHLLAAAQEA EVPFDLRDID
310 320 330 340 350
RLSRKVPQLC KVAPNIQKYH MEDVHRAGGI FSILGELARG GLLHTDVPTV
360 370 380 390 400
HSPSMADAIA QWDITQTRDE AVHTFFKAGP AGIPTQTAFS QNTRWPSLDD
410 420 430 440 450
DRAEGCIRSV EHAYSKEGGL AVLYGNIALD GCVVKTAGVD ESIHVFEGSA
460 470 480 490 500
KIFESQDAAV KGILGDEVKA GDIVIIRYEG PKGGPGMQEM LYPTSYLKSK
510 520 530 540 550
GLGKQCALLT DGRFSGGTSG LSIGHASPEA AAGGAIGLVQ DGDKVLIDIP
560 570 580 590 600
NRSINLLVSD EELAARRAEQ DKKGWKPAAP RARRVSTALK AYALLATSAD
610
KGAVRNKALL DG
Length:612
Mass (Da):65,160
Last modified:November 14, 2006 - v1
Checksum:iEE6C5F22697841F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000438 Genomic DNA. Translation: ABJ15317.1.
RefSeqiWP_003084436.1. NC_008463.1.

Genome annotation databases

EnsemblBacteriaiABJ15317; ABJ15317; PA14_04630.
KEGGipau:PA14_04630.
PATRICi19846792. VBIPseAer79785_0380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000438 Genomic DNA. Translation: ABJ15317.1.
RefSeqiWP_003084436.1. NC_008463.1.

3D structure databases

ProteinModelPortaliQ02U62.
SMRiQ02U62. Positions 196-570.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ15317; ABJ15317; PA14_04630.
KEGGipau:PA14_04630.
PATRICi19846792. VBIPseAer79785_0380.

Phylogenomic databases

HOGENOMiHOG000173155.
KOiK01687.
OMAiQGRNMAG.
OrthoDBiEOG6MSS24.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.
BioCyciPAER208963:GI5K-370-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UCBPP-PA14.

Entry informationi

Entry nameiILVD_PSEAB
AccessioniPrimary (citable) accession number: Q02U62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: November 11, 2015
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.