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A8LKI7 (A8LKI7_DINSH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydrogenase RuleBase RU004445 HAMAP-Rule MF_01033

EC=1.1.1.85 RuleBase RU004445 HAMAP-Rule MF_01033
Alternative name(s):
3-IPM-DH HAMAP-Rule MF_01033
Beta-IPM dehydrogenase HAMAP-Rule MF_01033
Gene names
Name:imdh EMBL ABV91830.1
Synonyms:leuB HAMAP-Rule MF_01033
Ordered Locus Names:Dshi_0081 EMBL ABV91830.1
OrganismDinoroseobacter shibae (strain DFL 12) [Complete proteome] [HAMAP] EMBL ABV91830.1
Taxonomic identifier398580 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeDinoroseobacter

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate By similarity. RuleBase RU004445 HAMAP-Rule MF_01033 SAAS SAAS001804

Catalytic activity

(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH. RuleBase RU004445 HAMAP-Rule MF_01033 SAAS SAAS001804

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity. RuleBase RU004445 HAMAP-Rule MF_01033 SAAS SAAS001804

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. RuleBase RU004445 HAMAP-Rule MF_01033 SAAS SAAS001804

Subunit structure

Homodimer By similarity. RuleBase RU004445 HAMAP-Rule MF_01033 SAAS SAAS001804

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01033.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. HAMAP-Rule MF_01033

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding77 – 9014NAD By similarity HAMAP-Rule MF_01033
Nucleotide binding288 – 30013NAD By similarity HAMAP-Rule MF_01033

Sites

Metal binding2251Magnesium or manganese By similarity HAMAP-Rule MF_01033
Metal binding2491Magnesium or manganese By similarity HAMAP-Rule MF_01033
Metal binding2531Magnesium or manganese By similarity HAMAP-Rule MF_01033
Binding site971Substrate By similarity HAMAP-Rule MF_01033
Binding site1071Substrate By similarity HAMAP-Rule MF_01033
Binding site1351Substrate By similarity HAMAP-Rule MF_01033
Binding site2251Substrate By similarity HAMAP-Rule MF_01033
Site1421Important for catalysis By similarity HAMAP-Rule MF_01033
Site1921Important for catalysis By similarity HAMAP-Rule MF_01033

Sequences

Sequence LengthMass (Da)Tools
A8LKI7 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 91F8C676ACDB3175

FASTA36839,244
        10         20         30         40         50         60 
MSTASLLILA GDGIGPEVMA EVRKIIDWYG AKRDLAFDVS EDLVGGAAYD VHGVPLADET 

        70         80         90        100        110        120 
MAKAQAVDAV LLGAVGGPKY DTLDFSLKPE RGLLRLRKEM DLFANLRPAQ CFDALADFSS 

       130        140        150        160        170        180 
LKKDIVAGLD IMIVRELTSG VYFGEPRGIH KEGNERVGIN TQRYTESEIA RVARSAFELA 

       190        200        210        220        230        240 
KKRGNKVCSM EKANVMESGI LWRDVVTEIH AAEYADVELS HMYADAGAMQ LVRAPKQFDV 

       250        260        270        280        290        300 
IVTDNLFGDL LSDAAAMLTG SLGMLPSASL GLPMENGRPK ALYEPVHGSA PDIAGQGKAN 

       310        320        330        340        350        360 
PCACILSFAM ALRYSFDQGA EADRLEAAVN QVLAQGIRTA DLMQAGDTAP ASTSQMGDAV 


IAALDASL 

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References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000830 Genomic DNA. Translation: ABV91830.1.
RefSeqYP_001531431.1. NC_009952.1.

3D structure databases

ProteinModelPortalA8LKI7.
SMRA8LKI7. Positions 6-366.
ModBaseSearch...

Protein-protein interaction databases

STRING398580.Dshi_0081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV91830; ABV91830; Dshi_0081.
GeneID5711704.
KEGGdsh:Dshi_0081.
PATRIC21812601. VBIDinShi9476_0076.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0473.
HOGENOMHOG000021112.
KOK00052.
OMAIYFGERQ.
ProtClustDBPRK00772.

Enzyme and pathway databases

UniPathwayUPA00048; UER00072.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
HAMAPMF_01033. LeuB_type1.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00169. leuB. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA8LKI7_DINSH
AccessionPrimary (citable) accession number: A8LKI7
Entry history
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)