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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Pseudomonas stutzeri (strain A1501)
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 (NADP(+)) (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 (NADP(+)) (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)DescriptionActionsGraphical viewLength
Metal bindingi122Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi193Iron-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:PST_4012
OrganismiPseudomonas stutzeri (strain A1501)
Taxonomic identifieri379731 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000000233 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000010381 – 612Dihydroxy-acid dehydrataseAdd BLAST612

Interactioni

Protein-protein interaction databases

STRINGi379731.PST_4012.

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C01. Bacteria.
COG0129. LUCA.
HOGENOMiHOG000173155.
KOiK01687.
OMAiQGRNMAG.
OrthoDBiPOG091H010A.

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. 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.

A4VRN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDYRSKTST HGRNMAGARA LWRATGMKDE DFKKPIIAIA NSFTQFVPGH
60 70 80 90 100
VHLKDMGQLV AREIEKHGGV AKEFNTIAVD DGIAMGHDGM LYSLPSREII
110 120 130 140 150
ADSVEYMVNA HCADAIVCIS NCDKITPGML MAALRLNIPV VFVSGGPMEA
160 170 180 190 200
GKTKLANHGL DLVDAMVVAA DDSCSDEKVA EYERSACPTC GSCSGMFTAN
210 220 230 240 250
SMNCLTEALG LSLPGNGTTL ATHADREQLF LRAGRIAVEL CKRYYQDGDE
260 270 280 290 300
SVLPRNVASR KAFENAMTLD IAMGGSTNTI LHLLAAAQEA EVDFDLRDID
310 320 330 340 350
ALSRKVPQLC KVAPNIQKYH MEDVHRAGGI FSILGELARG GLLHTDASTV
360 370 380 390 400
HSPSMADAIA EWDITQTQDE AVHTFFKAGP AGIPTQVAFS QATRWPSLDL
410 420 430 440 450
DRAEGCIRSV EHAYSQEGGL AVLYGNIALD GCVVKTAGVD ESIHVFEGTA
460 470 480 490 500
KIFESQDSAV KGILNDEVKA GDIVIIRYEG PKGGPGMQEM LYPTSYLKSK
510 520 530 540 550
GLGKECALLT DGRFSGGTSG LSIGHASPEA AAGGAIGLVQ DGDKVLIDIP
560 570 580 590 600
NRSIQLQVSD EELAHRRIEQ DKKGWKPAQP RARKVSTALK AYALLATSAD
610
KGAVRDKAML DG
Length:612
Mass (Da):65,418
Last modified:May 29, 2007 - v1
Checksum:i51E46C26EF1DEEB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000304 Genomic DNA. Translation: ABP81635.1.
RefSeqiWP_011915016.1. NC_009434.1.

Genome annotation databases

EnsemblBacteriaiABP81635; ABP81635; PST_4012.
GeneIDi25040775.
KEGGipsa:PST_4012.
PATRICi19968528. VBIPseStu31643_3993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000304 Genomic DNA. Translation: ABP81635.1.
RefSeqiWP_011915016.1. NC_009434.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi379731.PST_4012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP81635; ABP81635; PST_4012.
GeneIDi25040775.
KEGGipsa:PST_4012.
PATRICi19968528. VBIPseStu31643_3993.

Phylogenomic databases

eggNOGiENOG4105C01. Bacteria.
COG0129. LUCA.
HOGENOMiHOG000173155.
KOiK01687.
OMAiQGRNMAG.
OrthoDBiPOG091H010A.

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. 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...

Entry informationi

Entry nameiILVD_PSEU5
AccessioniPrimary (citable) accession number: A4VRN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: November 2, 2016
This is version 62 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.