Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
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 bindingi122 – 1221Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi196 – 1961Iron-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

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:SPO3314
OrganismiRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Taxonomic identifieri246200 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
Proteomesi
  • UP000001023 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 610610Dihydroxy-acid dehydratasePRO_0000225424Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi246200.SPO3314.

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.

Q5LN98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMYRSRTST HGRNMAGARG LWRATGMTDG DFGKPIIAIV NSFTQFVPGH
60 70 80 90 100
VHLKDLGQMV AREVEAAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSREVI
110 120 130 140 150
ADSVEYMVNA HCADAMVCIS NCDKITPGML MAAMRLNIPA IFVSGGPMEA
160 170 180 190 200
GKIDIADLEM TKIDLVDAMV AAANDKFTDE QVQHIEENAC PTCGSCSGMF
210 220 230 240 250
TANSMNCLAE ALGLALPGNG STLATHSDRK ALFLEAGRRI VEITKRHYEG
260 270 280 290 300
EEKGLLPREI ATFEAFENAM SLDIAMGGST NTVLHLLAIA HEGEVDFTMT
310 320 330 340 350
DMDRLSRKVP CLCKVAPNTA NVHMEDVHRA GGIFSILGEL SRAGLLHDDC
360 370 380 390 400
GTVHSASMGE AIAKWDIKVA NNPEAESLFK AAPGGVRTTQ AFSQSNRYKD
410 420 430 440 450
LDTDREGGVI RSKEHAFSQD GGLAVLFGNI AEDGCIVKTA GVDASILQFT
460 470 480 490 500
GTAHVCESQD DAVNNILTGK VKEGDVVVIR YEGPRGGPGM QEMLYPTSYL
510 520 530 540 550
KSKGLGKACA LLTDGRFSGG TSGLSIGHVS PEAAEGGTIG LVEDGDRIEI
560 570 580 590 600
DIPNRRIHLA VSDEVLAARR AAQEAKGWHP AKPRKRKVST ALKAYAKLTT
610
SAAKGAVRQV
Length:610
Mass (Da):64,933
Last modified:February 1, 2005 - v1
Checksum:i9BF2EFF92039E7BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000031 Genomic DNA. Translation: AAV96541.1.
RefSeqiWP_011048997.1. NC_003911.12.

Genome annotation databases

EnsemblBacteriaiAAV96541; AAV96541; SPO3314.
KEGGisil:SPO3314.
PATRICi23380077. VBIRuePom114501_3375.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000031 Genomic DNA. Translation: AAV96541.1.
RefSeqiWP_011048997.1. NC_003911.12.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246200.SPO3314.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV96541; AAV96541; SPO3314.
KEGGisil:SPO3314.
PATRICi23380077. VBIRuePom114501_3375.

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_RUEPO
AccessioniPrimary (citable) accession number: Q5LN98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: February 1, 2005
Last modified: September 7, 2016
This is version 74 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.