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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
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 (ilvB)
  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 (ilvB)
  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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi119 – 1191Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi191 – 1911Iron-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

BioCyciCACE272562:GJIH-3255-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:CA_C3170
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000814 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Dihydroxy-acid dehydratasePRO_0000103459Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272562.CA_C3170.

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Phylogenomic databases

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

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.

Q97EE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSDKAMKGV ERAPHRSLFK ALGFIDEEMD RPLIGIANSY SELIPGHMNL
60 70 80 90 100
DKIVKAVKDG IRMAGGVPVE FGTIGVCDGI SMNHKGMSYS LPSRQIIADS
110 120 130 140 150
VEIVAKAHAL DGLVLVPNCD KVVPGMLMAA GRVNIPSIVI SGGPMLSGRT
160 170 180 190 200
NGRVTDLNSV FEAVGAVSAG KMSLEELAEL ENTACPTCGS CSGMFTANSM
210 220 230 240 250
NCLSEVLGLA LPYNGTIPAV FSERLRLAKK AGMKIVELVQ KDIRPSDILT
260 270 280 290 300
EAAFMNAVAM DMALGGSTNS LLHLPAIAYE CDVDINFDKI NEISEKIPHV
310 320 330 340 350
CKLSPAGFHH IEDLHMAGGI PAVVNGIIKK GLLNGECMTV TGKTLYENVK
360 370 380 390 400
DAKIKNIDVI RIDNPYSETG GLSVLRGNLA PDGAIVKKAA VAPEMMQHTG
410 420 430 440 450
PARVFNSEEE VSKAILGGKI NPGDVVVIRY EGPKGGPGMK EMLSPTASLA
460 470 480 490 500
GMGLDKSVAL ITDGRFSGAT RGASIGHVSP EAAEGGPIGL VEEGDTIEID
510 520 530 540 550
IEKKTINLLV PEEKLKNRKP EKVEKPVKGY LNTYRQGVSS ACTGAVFHST

KE
Length:552
Mass (Da):58,367
Last modified:October 1, 2001 - v1
Checksum:i9309A73FE7CD81F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK81107.1.
PIRiH97289.
RefSeqiNP_349767.1. NC_003030.1.
WP_010966447.1. NC_003030.1.

Genome annotation databases

EnsemblBacteriaiAAK81107; AAK81107; CA_C3170.
GeneIDi1119352.
KEGGicac:CA_C3170.
PATRICi32040749. VBICloAce74127_3351.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK81107.1.
PIRiH97289.
RefSeqiNP_349767.1. NC_003030.1.
WP_010966447.1. NC_003030.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272562.CA_C3170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK81107; AAK81107; CA_C3170.
GeneIDi1119352.
KEGGicac:CA_C3170.
PATRICi32040749. VBICloAce74127_3351.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.
BioCyciCACE272562:GJIH-3255-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_CLOAB
AccessioniPrimary (citable) accession number: Q97EE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: October 1, 2001
Last modified: September 7, 2016
This is version 84 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.