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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
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. no protein annotated in this organism
  2. Acetohydroxy acid isomeroreductase, catalytic domain protein (BZ14_171)
  3. Dihydroxy-acid dehydratase (ilvD), 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. no protein annotated in this organism
  2. Acetohydroxy acid isomeroreductase, catalytic domain protein (BZ14_171)
  3. Dihydroxy-acid dehydratase (ilvD), 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)DescriptionActionsGraphical viewLength
Metal bindingi125Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi197Iron-sulfur (4Fe-4S)UniRule annotation1

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

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:FTT_0640
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002253921 – 551Dihydroxy-acid dehydrataseAdd BLAST551

Interactioni

Protein-protein interaction databases

IntActiQ5NH32. 6 interactors.
STRINGi177416.FTT_0640.

Structurei

3D structure databases

ProteinModelPortaliQ5NH32.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C01. Bacteria.
COG0129. LUCA.
HOGENOMiHOG000173155.
KOiK01687.
OMAiAGCEGFD.

Family and domain databases

HAMAPiMF_00012. IlvD. 1 hit.
InterProiIPR015928. Aconitase/3IPM_dehydase_swvl.
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERiPTHR21000. PTHR21000. 1 hit.
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.

Q5NH32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVLNKYSR RLTEDKSQGA SQAMLYGTEM NDADMHKPQI GIGSVWYEGN
60 70 80 90 100
TCNMHLNQLA QFVKDSVEKE NLKGMRFNTI GVSDGISMGT DGMSYSLQSR
110 120 130 140 150
DLIADSIETV MSAHWYDGLV SIPGCDKNMP GCMMALGRLN RPGFVIYGGT
160 170 180 190 200
IQAGVMRGKP IDIVTAFQSY GACLSGQITE QERQETIKKA CPGAGACGGM
210 220 230 240 250
YTANTMACAI EALGMSLPFS SSTSATSVEK VQECDKAGET IKNLLELDIK
260 270 280 290 300
PRDIMTRKAF ENAMVLITVM GGSTNAVLHL LAMASSVDVD LSIDDFQEIA
310 320 330 340 350
NKTPVLADFK PSGKYVKANL HAIGGTPAVM KMLLKAGMLH GDCLTVTGKT
360 370 380 390 400
LAENLENVAD LPEDNTIIHK LDNPIKKTGH LQILKGNVAP EGSVAKITGK
410 420 430 440 450
EGEIFEGVAN VFDSEEEMVA AVETGKVKKG DVIVIRYEGP KGGPGMPEML
460 470 480 490 500
KPTSLIMGAG LGQDVALITD GRFSGGSHGF IVGHITPEAY EGGMIALLEN
510 520 530 540 550
GDKITIDAIN NVINVDLSDQ EIAQRKSKWR ASKQKASRGT LKKYIKTVSS

A
Length:551
Mass (Da):59,003
Last modified:February 1, 2005 - v1
Checksum:i4756489DAA902FED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45273.1.
RefSeqiWP_003020386.1. NZ_CP010290.1.
YP_169660.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG45273; CAG45273; FTT_0640.
GeneIDi3191790.
KEGGiftu:FTT_0640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45273.1.
RefSeqiWP_003020386.1. NZ_CP010290.1.
YP_169660.1. NC_006570.2.

3D structure databases

ProteinModelPortaliQ5NH32.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5NH32. 6 interactors.
STRINGi177416.FTT_0640.

Protocols and materials databases

DNASUi3191790.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG45273; CAG45273; FTT_0640.
GeneIDi3191790.
KEGGiftu:FTT_0640.

Phylogenomic databases

eggNOGiENOG4105C01. Bacteria.
COG0129. LUCA.
HOGENOMiHOG000173155.
KOiK01687.
OMAiAGCEGFD.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.

Family and domain databases

HAMAPiMF_00012. IlvD. 1 hit.
InterProiIPR015928. Aconitase/3IPM_dehydase_swvl.
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERiPTHR21000. PTHR21000. 1 hit.
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...

Entry informationi

Entry nameiILVD_FRATT
AccessioniPrimary (citable) accession number: Q5NH32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: February 1, 2005
Last modified: November 2, 2016
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, Reference 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.