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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Status
Unreviewed-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 annotationSAAS annotation

Cofactori

[4Fe-4S] clusterUniRule annotationSAAS annotationNote: Binds 1 [4Fe-4S] cluster.UniRule annotationSAAS annotation

Pathway:iL-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. no protein annotated in this organism
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (Swit_0778)
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.

Pathway:iL-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. no protein annotated in this organism
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (Swit_0778)
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

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

4Fe-4SUniRule annotationSAAS annotation, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciSWIT392499:GHZK-3072-MONOMER.
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
Ordered Locus Names:Swit_3037Imported
OrganismiSphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)Imported
Taxonomic identifieri392499 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas
ProteomesiUP000001989 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi392499.Swit_3037.

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0129.
HOGENOMiHOG000173155.
KOiK01687.
OMAiRTIMRIT.
OrthoDBiEOG6MSS24.

Family and domain databases

HAMAPiMF_00012. IlvD.
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.

A5VAS1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAYRSRTST HGRNMAGARA LWRATGIKDG DFGKPIIAIA NSFTQFVPGH
60 70 80 90 100
IHLKDLGQMV AREIEAHGGI AKEFNTIAVD DGIAQGHLGM LYSLPSREII
110 120 130 140 150
ADAVEYMVNA HCADALVCIS NCDKITPGML MAALRLNVPT VFVSGGPMEA
160 170 180 190 200
GKIVAADGKL RVIDTVDPMV LAGDPTVSDE EVEAYEKSAC PTCGSCAGMF
210 220 230 240 250
TANSMNCLTE ALGLSLPGNG TTLATHADRR SLFLEAARTI MRITRRYYEE
260 270 280 290 300
EDGSILPRGI AGFAAFENAM RLDMAMGGST NTILHLLAAA REAEVDFTMA
310 320 330 340 350
DIDRLSRDTP CLCKVAPNNS NVHIEDIHRA GGIMSILGQI DRAGLLNRDC
360 370 380 390 400
ATIHSPTLAE ALDRWDISRT DDAEVESFYK AAPGGVRTTE AFSQAKRWSE
410 420 430 440 450
LDTDRETGVI RSADHAFFKD GGLAVLYGNI ARDGCIVKTA GVDEAILKFS
460 470 480 490 500
GSAVICESQD DAVAKILGDK VKAGDVVVVR YEGPKGGPGM QEMLYPTSYL
510 520 530 540 550
KARGLGKACA LITDGRFSGA TSGLSIGHVS PEAAEGGAIG LIEDGDIIEI
560 570 580 590 600
DIPARRIDVR LSEAELAARR AAMEARGTVA WQPVDRDRPV SMALRAYAAL
610
TTSAAHGAVR DATQLARR
Length:618
Mass (Da):65,813
Last modified:July 10, 2007 - v1
Checksum:iAB211610947573E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000699 Genomic DNA. Translation: ABQ69387.1.
RefSeqiWP_012049236.1. NC_009511.1.

Genome annotation databases

EnsemblBacteriaiABQ69387; ABQ69387; Swit_3037.
KEGGiswi:Swit_3037.
PATRICi23685271. VBISphWit55028_3578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000699 Genomic DNA. Translation: ABQ69387.1.
RefSeqiWP_012049236.1. NC_009511.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi392499.Swit_3037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ69387; ABQ69387; Swit_3037.
KEGGiswi:Swit_3037.
PATRICi23685271. VBISphWit55028_3578.

Phylogenomic databases

eggNOGiCOG0129.
HOGENOMiHOG000173155.
KOiK01687.
OMAiRTIMRIT.
OrthoDBiEOG6MSS24.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.
BioCyciSWIT392499:GHZK-3072-MONOMER.

Family and domain databases

HAMAPiMF_00012. IlvD.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RW1 / DSM 6014 / JCM 10273Imported.

Entry informationi

Entry nameiA5VAS1_SPHWW
AccessioniPrimary (citable) accession number: A5VAS1
Entry historyi
Integrated into UniProtKB/TrEMBL: July 10, 2007
Last sequence update: July 10, 2007
Last modified: July 22, 2015
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.