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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Escherichia coli Xuzhou21
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalytic activityi

2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O.UniRule annotationSAAS 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 annotationSAAS annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (CDCO157_4438), Acetolactate synthase (CDCO157_4347), Acetolactate synthase (CDCO157_0080)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (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 annotationSAAS annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (CDCO157_4438), Acetolactate synthase (CDCO157_4347), Acetolactate synthase (CDCO157_0080)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (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)DescriptionActionsGraphical viewLength
Metal bindingi122Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi195Iron-sulfur (4Fe-4S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyaseUniRule annotationSAAS annotation
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesisUniRule annotationSAAS annotation
Ligand4Fe-4SUniRule annotationSAAS annotation, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroxy-acid dehydrataseUniRule annotationSAAS annotation (EC:4.2.1.9UniRule annotationSAAS annotation)
Short name:
DADUniRule annotation
Gene namesi
Name:ilvDUniRule annotation
ORF Names:CDCO157_4441Imported
OrganismiEscherichia coli Xuzhou21Imported
Taxonomic identifieri741093 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000002870 Componenti: Chromosome

Structurei

3D structure databases

SMRiA0A0F6CB87.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili287 – 307Sequence analysisAdd BLAST21

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotationSAAS annotation

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

KOiK01687.

Family and domain databases

HAMAPiMF_00012. IlvD. 1 hit.
InterProiView protein in InterPro
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
IPR037237. IlvD/EDD_N.
PfamiView protein in Pfam
PF00920. ILVD_EDD. 1 hit.
SUPFAMiSSF143975. SSF143975. 1 hit.
TIGRFAMsiTIGR00110. ilvD. 1 hit.
PROSITEiView protein in PROSITE
PS00886. ILVD_EDD_1. 1 hit.
PS00887. ILVD_EDD_2. 1 hit.

Sequencei

Sequence statusi: Complete.

A0A0F6CB87-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKYRSATTT HGRNMAGARA LWRATGMTDA DFGKPIIAVV NSFTQFVPGH
60 70 80 90 100
VHLRDLGKLV AEQIEAAGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRELI
110 120 130 140 150
ADSVEYMVNA HCADAMVCIS NCDKITPGML MASLRLNIPV IFVSGGPMEA
160 170 180 190 200
GKTKLSDQII KLDLVDAMIQ GADPKVSDSQ SDQVERSACP TCGSCSGMFT
210 220 230 240 250
ANSMNCLTEA LGLSQPGNGS LLATHSDRKQ LFLNAGKRIV ELTKRYYEQN
260 270 280 290 300
DESALPRNIA SKAAFENAMT LDIAMGGSTN TVLHLLAAAQ EAEIDFTMSD
310 320 330 340 350
IDKLSRKVPQ LCKVAPSTQK YHMEDVHRAG GVIGILGELD RAGLLNRDVK
360 370 380 390 400
NVLGLTLPQT LEQYDVMLTQ DDAVKNMFRA GPAGIRTTQA FSQDCRWDTL
410 420 430 440 450
DDDRANGCIR SLEHAYSKDG GLAVLYGNFA ENGCIVKTAG VDDSILKFTG
460 470 480 490 500
PAKVYESQDD AVEAILGGKV VAGDVVVIRY EGPKGGPGMQ EMLYPTSFLK
510 520 530 540 550
SMGLGKACAL ITDGRFSGGT SGLSIGHVSP EAASGGSIGL IEDGDLIAID
560 570 580 590 600
IPNRGIQLQV SDAELAARRE AQEARGDKAW TPKNRERQIS FALRAYASLA
610
TSADKGAVRD KSKLGG
Length:616
Mass (Da):65,576
Last modified:June 24, 2015 - v1
Checksum:iCBD645B7505083C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001925 Genomic DNA. Translation: AFJ31493.1.
RefSeqiWP_001127409.1. NC_017906.1.

Genome annotation databases

EnsemblBacteriaiAFJ31493; AFJ31493; CDCO157_4441.
KEGGielx:CDCO157_4441.
PATRICifig|741093.3.peg.4763.

Similar proteinsi

Entry informationi

Entry nameiA0A0F6CB87_ECOLX
AccessioniPrimary (citable) accession number: A0A0F6CB87
Entry historyiIntegrated into UniProtKB/TrEMBL: June 24, 2015
Last sequence update: June 24, 2015
Last modified: December 20, 2017
This is version 21 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported