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Reviewed, UniProtKB/Swiss-Prot A0RCL3 (ILVD_BACAH)

Last modified February 9, 2010. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydroxy-acid dehydratase
      Short name=DAD
    EC=4.2.1.9
Gene names
Name: ilvD
Ordered Locus Names: BALH_1628
OrganismBacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]
Taxonomic identifier412694 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O. HAMAP MF_00012

Cofactor

Binds 1 4Fe-4S cluster Potential. HAMAP MF_00012

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4. HAMAP MF_00012

Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4. HAMAP MF_00012

Sequence similarities

Belongs to the ilvD/edd family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Dihydroxy-acid dehydratase HAMAP MF_00012
PRO_1000000957

Sites

Metal binding1191Iron-sulfur (4Fe-4S) Potential
Metal binding1921Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
A0RCL3-1 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 39AACA4DC2C3C30B

FASTA55759,992
        10         20         30         40         50         60 
MRSDMIKKGF DKAPHRSLLK ATGLKDEDFD KPFIAICNSF IEIIPGHKHL NEFGKLVKEA 

        70         80         90        100        110        120 
VRAAGMVPFE FNTIGVDDGI AMGHIGMRYS LPSREIIADS VETVVNAHWF DGMICIPNCD 

       130        140        150        160        170        180 
KITPGMMMAA LRINIPTVFV SGGPMAAGKT SKGDVVDLSS VFEGVGAYQS GKISEEELKD 

       190        200        210        220        230        240 
IEDHGCPSCG SCSGMFTANS MNCLCEVLGL ALPGNGSILA IDPRREELIK QAAEKLKILI 

       250        260        270        280        290        300 
ERDIKPRDIV TEEAIDDAFA LDMAMGGSTN TVLHTLALAQ EAGLDYDMNR IDAVSRRVPH 

       310        320        330        340        350        360 
LCKVSPASNW HMEDIDRAGG ISAILKEMSR KEGVLHLDRI TATGQTLREN IAHAEIKDKE 

       370        380        390        400        410        420 
VIHSLENPHS EEGGLRILKG NLAKDGAVIK SGATEVKRFE GPCVIFNSQD EALAGIMLGK 

       430        440        450        460        470        480 
VKKGDVVVIR YEGPRGGPGM PEMLAPTSAI AGMGLGADVA LLTDGRFSGA SRGISVGHIS 

       490        500        510        520        530        540 
PEAAAGGTIA LLEQGDIVCI DVEERLLEVR VSDEELDKRK KEWKRPEPKV KTGWLGRYAQ 

       550 
MVTSANTGAV LKIPNFD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000485 Genomic DNA. Translation: ABK84956.1.
RefSeqYP_894463.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0RCL3.

Genome annotation databases

GeneID4546731.
GenomeReviewsGene locus BALH_1628 in contig CP000485_GR.
KEGGbtl:BALH_1628.
NMPDRfig|412694.5.peg.1624.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0129.
HOGENOMHBG671001.
OMASRKVPCL.

Family and domain databases

HAMAPMF_00012. IlvD.
[Tree]
InterProIPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERPTHR21000. ILVD_EDD_family. 1 hit.
PfamPF00920. ILVD_EDD. 1 hit.
[Graphical view]
TIGRFAMsTIGR00110. ilvD. 1 hit.
PROSITEPS00886. ILVD_EDD_1. 1 hit.
PS00887. ILVD_EDD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameILVD_BACAH
AccessionPrimary (citable) accession number: A0RCL3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: February 9, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents