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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 large subunit (ilvB), Acetolactate synthase small subunit (ilvH)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase 2 (ilvK), Branched-chain-amino-acid transaminase 1 (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 annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase large subunit (ilvB), Acetolactate synthase small subunit (ilvH)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase 2 (ilvK), Branched-chain-amino-acid transaminase 1 (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

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

BioCyciBSUB:BSU21870-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
Alternative name(s):
Vegetative protein 110
Short name:
VEG110
Gene namesi
Name:ilvDUniRule annotation
Ordered Locus Names:BSU21870
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 558557Dihydroxy-acid dehydratasePRO_0000103431Add
BLAST

Proteomic databases

PaxDbiP51785.

Interactioni

Protein-protein interaction databases

IntActiP51785. 1 interaction.
MINTiMINT-8366038.
STRINGi224308.Bsubs1_010100012041.

Structurei

3D structure databases

ProteinModelPortaliP51785.
SMRiP51785. Positions 65-557.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C01. Bacteria.
COG0129. LUCA.
HOGENOMiHOG000173155.
InParanoidiP51785.
KOiK01687.
OMAiQGRNMAG.
PhylomeDBiP51785.

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.

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

P51785-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELRSNMIT QGIDRAPHRS LLRAAGVKEE DFGKPFIAVC NSYIDIVPGH
60 70 80 90 100
VHLQEFGKIV KEAIREAGGV PFEFNTIGVD DGIAMGHIGM RYSLPSREII
110 120 130 140 150
ADSVETVVSA HWFDGMVCIP NCDKITPGML MAAMRINIPT IFVSGGPMAA
160 170 180 190 200
GRTSDGRKIS LSSVFEGVGA YQAGKINENE LQELEQFGCP TCGSCSGMFT
210 220 230 240 250
ANSMNCLSEA LGLALPGNGT ILATSPERKE FVRKSAAQLM ETIRKDIKPR
260 270 280 290 300
DIVTVKAIDN AFALDMALGG STNTVLHTLA LANEAGVEYS LERINEVAER
310 320 330 340 350
VPHLAKLAPA SDVFIEDLHE AGGVSAALNE LSKKEGALHL DALTVTGKTL
360 370 380 390 400
GETIAGHEVK DYDVIHPLDQ PFTEKGGLAV LFGNLAPDGA IIKTGGVQNG
410 420 430 440 450
ITRHEGPAVV FDSQDEALDG IINRKVKEGD VVIIRYEGPK GGPGMPEMLA
460 470 480 490 500
PTSQIVGMGL GPKVALITDG RFSGASRGLS IGHVSPEAAE GGPLAFVENG
510 520 530 540 550
DHIIVDIEKR ILDVQVPEEE WEKRKANWKG FEPKVKTGYL ARYSKLVTSA

NTGGIMKI
Length:558
Mass (Da):59,500
Last modified:July 7, 2009 - v4
Checksum:iCFFFF203CD555E61
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551D → Y in AAA96629 (PubMed:8969496).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77246 Genomic DNA. Translation: AAA96629.1.
AL009126 Genomic DNA. Translation: CAB14105.2.
PIRiD69644.
RefSeqiNP_390070.2. NC_000964.3.
WP_009967560.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14105; CAB14105; BSU21870.
GeneIDi939084.
KEGGibsu:BSU21870.
PATRICi18976179. VBIBacSub10457_2280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77246 Genomic DNA. Translation: AAA96629.1.
AL009126 Genomic DNA. Translation: CAB14105.2.
PIRiD69644.
RefSeqiNP_390070.2. NC_000964.3.
WP_009967560.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP51785.
SMRiP51785. Positions 65-557.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP51785. 1 interaction.
MINTiMINT-8366038.
STRINGi224308.Bsubs1_010100012041.

Proteomic databases

PaxDbiP51785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14105; CAB14105; BSU21870.
GeneIDi939084.
KEGGibsu:BSU21870.
PATRICi18976179. VBIBacSub10457_2280.

Phylogenomic databases

eggNOGiENOG4105C01. Bacteria.
COG0129. LUCA.
HOGENOMiHOG000173155.
InParanoidiP51785.
KOiK01687.
OMAiQGRNMAG.
PhylomeDBiP51785.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.
BioCyciBSUB:BSU21870-MONOMER.

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_BACSU
AccessioniPrimary (citable) accession number: P51785
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: September 7, 2016
This is version 119 of the entry and version 4 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.