Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q3AEQ2 (LEU3_CARHZ)

Last modified November 4, 2008. Version 25. 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:
    3-isopropylmalate dehydrogenase
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase
      Short name=IMDH
    3-IPM-DH
Gene names
Name: leuB
Ordered Locus Names: CHY_0524
OrganismCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP]
Taxonomic identifier246194 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteriaceaeCarboxydothermus

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.

Subunit structure

Homodimer By similarity.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3743743-isopropylmalate dehydrogenase
PRO_0000250110

Regions

Nucleotide binding83 – 9614NAD By similarity
Nucleotide binding288 – 30013NAD By similarity

Sites

Metal binding2311Magnesium or manganese By similarity
Metal binding2551Magnesium or manganese By similarity
Metal binding2591Magnesium or manganese By similarity
Binding site1041Substrate By similarity
Binding site1141Substrate By similarity
Binding site1421Substrate By similarity
Binding site2311Substrate By similarity
Site1491Important for catalysis By similarity
Site1991Important for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3AEQ2-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: FBA85D58E1DE8446

FASTA37440,975
        10         20         30         40         50         60 
MSGRSCKGPF KILVLPGDGI GPEIIKEAVK VLKALGEKKG ITFNFQYGLI GGAAIDERGV 

        70         80         90        100        110        120 
PLPEETVELG KQCDAILLGA VGGPKWDNLP PEIRPELGGL LKIRKVFDLY ANLRPVMFFP 

       130        140        150        160        170        180 
ELKNASPLKP DIIEGVDILM VRELTGGLYF GEKKRFTTEQ GEQAVIDTLI YTEKEVERVV 

       190        200        210        220        230        240 
RLGFELAQKR RGKLTLVDKA NVLESSRFWR EITGEIKKEY PDVELSYMYV DNCAMQLIRN 

       250        260        270        280        290        300 
PRQFDVIVTE NMFGDILTDE GSVLAGSIGL LPSASLNGKF GLYEPIHGSA PDIAGQNKAN 

       310        320        330        340        350        360 
PLATILSAGM MLRYSLDCPE EALLIEKAVK AVLQKGYRTG DILEPGTTLV TCEEMGDLVA 

       370 
EEILGGVYDE GLPL 

« Hide

References

[1]"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901."
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.
PLoS Genet. 1:563-574(2005) [PubMed: 16311624] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000141 Genomic DNA. Translation: ABB15752.1.
RefSeqYP_359382.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3727861.
GenomeReviewsGene locus CHY_0524 in contig CP000141_GR.
KEGGchy:CHY_0524.
NMPDRfig|246194.3.peg.1091.
TIGRCHY_0524.

Phylogenomic databases

HOGENOMQ3AEQ2.

Enzyme and pathway databases

BioCycCHYD246194:CHY_0524-MON.

Family and domain databases

HAMAPMF_01033.
[Tree]
InterProIPR004429. 3-isopropylmalate_DHase.
IPR001804. IsoCit_IM_DHase.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PTHR11835:SF13. IPMDH. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00169. leuB. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEU3_CARHZ
AccessionPrimary (citable) accession number: Q3AEQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: November 22, 2005
Last modified: November 4, 2008
This is version 25 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