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Protein

Dihydroxy-acid dehydratase

Gene

ilvD

Organism
Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi198 – 1981Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. dihydroxy-acid dehydratase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. isoleucine biosynthetic process Source: UniProtKB-HAMAP
  2. valine biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciSSP321332:GH1B-1987-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:CYB_1987
OrganismiSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
Taxonomic identifieri321332 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001938 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 565565Dihydroxy-acid dehydratasePRO_0000321608Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi321332.CYB_1987.

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0129.
HOGENOMiHOG000173155.
KOiK01687.
OMAiRTPKIAD.
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.

Q2JK60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANSPFPLRS QVVTQGVQRS PNRAMLRAVG FRDEDFGKPI VGIANAHSTL
60 70 80 90 100
TPCNMGIQTL AERAEAALRT AGCMPQVFGT ITISDGISMG TEGMKYSLVS
110 120 130 140 150
REVIADSIET VVNGQSMDGL LAIGGCDKNM PGAMIAMARL NVPSIFVYGG
160 170 180 190 200
TIKPGHYNGR DLTIVSAFEA VGEFSAGRIS EEELLAVERH ACPGAGSCGG
210 220 230 240 250
MYTANTMSSA FEAMGMSLPY SSTMAAEDEE KAESAAQSAK VLAEAIKANI
260 270 280 290 300
RPRDIITRKS IENAISVIMA VGGSTNAVLH FLAIAHAAEV PLTLDDFETI
310 320 330 340 350
RARVPVLCDL KPSGRFVATD LHRAGGIPQV MKMLLNHGLL HGDCLTISGQ
360 370 380 390 400
TIVEVLRDVP DEPSPDQEVI RPWHSPLYPQ GHLAILKGNL APEGAVAKIT
410 420 430 440 450
GVKNPQITGP ARVFDSEESC LQAILSGQIR AGDVVVIRYE GPKGGPGMRE
460 470 480 490 500
MLSPTSAIIG AGLGDSVGLI TDGRFSGGTY GMVVGHVAPE AYVGGTIALV
510 520 530 540 550
EEGDLITIDA PARQLHLHVS EEELARRRAR WSPPEPRYKR GTLAKYAKLV
560
SSSSLGAVTD LNLWD
Length:565
Mass (Da):59,804
Last modified:March 7, 2006 - v1
Checksum:i3CB28147B1DD4C6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000240 Genomic DNA. Translation: ABD02935.1.
RefSeqiWP_011433574.1. NC_007776.1.
YP_478198.1. NC_007776.1.

Genome annotation databases

EnsemblBacteriaiABD02935; ABD02935; CYB_1987.
KEGGicyb:CYB_1987.
PATRICi23806322. VBISynSp29577_1995.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000240 Genomic DNA. Translation: ABD02935.1.
RefSeqiWP_011433574.1. NC_007776.1.
YP_478198.1. NC_007776.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi321332.CYB_1987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD02935; ABD02935; CYB_1987.
KEGGicyb:CYB_1987.
PATRICi23806322. VBISynSp29577_1995.

Phylogenomic databases

eggNOGiCOG0129.
HOGENOMiHOG000173155.
KOiK01687.
OMAiRTPKIAD.
OrthoDBiEOG6MSS24.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.
BioCyciSSP321332:GH1B-1987-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. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
    Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
    ISME J. 1:703-713(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JA-2-3B'a(2-13).

Entry informationi

Entry nameiILVD_SYNJB
AccessioniPrimary (citable) accession number: Q2JK60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 7, 2006
Last modified: April 1, 2015
This is version 62 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

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.