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O53865 (KDC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-keto-acid decarboxylase

Short name=KDC
EC=4.1.1.-
Gene names
Name:kdc
Ordered Locus Names:Rv0853c, MT0876
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Decarboxylates branched-chain and aromatic alpha-keto acids to aldehydes. Ref.5

Cofactor

Binds 1 metal ion per subunit By similarity.

Binds 1 thiamine pyrophosphate per subunit By similarity.

Enzyme regulation

Allosterically activated by alpha-keto acids and the corresponding amino acids. L-leucine, L-valine, D-valine, L-isoleucine, L-phenylalanine, D-phenylalanine, L-tyrosine and L-valine are activators (with L-leucine and L-isoleucine being the strongest activators) whereas L-tryptophan, tryptophol, phenylacetic acid and indoleacetic acid have no effect.

Miscellaneous

Was identified as a high-confidence drug target.

Sequence similarities

Belongs to the TPP enzyme family.

Biophysicochemical properties

Kinetic parameters:

Pyruvate is converted with the lowest catalytic efficiency and displays a weak substrate inhibition. The highest catalytic efficiencies are found for indolepyruvate and alpha-ketoisocaproate. The S0.5 values are 0.26 mM for indolepyruvate, 2.90 mM for alpha-ketoisocaproate, 0.83 mM for phenylpyruvate, 0.92 mM for alpha-ketocaproate, 1.31 mM for alpha-ketovalerate, 0.93 mM for 4-hydroxyphenylpyruvate, 6.68 mM for alpha-keto-beta-methylvalerate, 8.25 mM for benzoylformate, 5=14.17 mM for alpha-ketobutyrate, 24.47 mM for alpha-ketoisovalerate, 98.89 mM for pyruvate.

KM=0.09 mM for indole pyruvate

KM=1.17 mM for phenyl pyruvate

KM=0.83 mM for alpha-keto caproate

KM=1.21 mM for alpha-keto valerate

KM=20.25 mM for alpha-keto-beta-methyl valerate

KM=26.11 mM for benzoylformate

KM=138.30 mM for alpha-keto-butyrate

KM=0.40 mM for pyruvate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 560560Alpha-keto-acid decarboxylase
PRO_0000333751

Regions

Region396 – 47883Thiamine pyrophosphate binding By similarity

Sites

Metal binding4461Magnesium By similarity
Metal binding4731Magnesium By similarity
Metal binding4751Magnesium; via carbonyl oxygen By similarity
Binding site611Thiamine pyrophosphate By similarity

Experimental info

Sequence conflict2971D → N in AAK45117. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O53865 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: F0430F720D57B7C4

FASTA56059,783
        10         20         30         40         50         60 
MTPQKSDACS DPVYTVGDYL LDRLAELGVS EIFGVPGDYN LQFLDHIVAH PTIRWVGSAN 

        70         80         90        100        110        120 
ELNAGYAADG YGRLRGMSAV VTTFGVGELS VTNAIAGSYA EHVPVVHIVG GPTKDAQGTR 

       130        140        150        160        170        180 
RALHHSLGDG DFEHFLRISR EITCAQANLM PATAGREIDR VLSEVREQKR PGYILLSSDV 

       190        200        210        220        230        240 
ARFPTEPPAA PLPRYPGGTS PRALSLFTKA AIELIADHQL TVLADLLVHR LQAVKELEAL 

       250        260        270        280        290        300 
LAADVVPHAT LMWGKSLLDE SSPNFLGIYA GAASAERVRA AIEGAPVLVT AGVVFTDMVS 

       310        320        330        340        350        360 
GFFSQRIDPA RTIDIGQYQS SVADQVFAPL EMSAALQALA TILTGRGISS PPVVPPPAEP 

       370        380        390        400        410        420 
PPAMPARDEP LTQQMVWDRV CSALTPGNVV LADQGTSFYG MADHRLPQGV TFIGQPLWGS 

       430        440        450        460        470        480 
IGYTLPAAVG AAVAHPDRRT VLLIGDGAAQ LTVQELGTFS REGLSPVIVV VNNDGYTVER 

       490        500        510        520        530        540 
AIHGETAPYN DIVSWNWTEL PSALGVTNHL AFRAQTYGQL DDALTVAAAR RDRMVLVEVV 

       550        560 
LPRLEIPRLL GQLVGSMAPQ 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv."
Camus J.-C., Pryor M.J., Medigue C., Cole S.T.
Microbiology 148:2967-2973(2002) [PubMed: 12368430] [Abstract]
Cited for: SEQUENCE REVISION.
Strain: ATCC 25618 / H37Rv.
[3]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[4]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
[5]"Amino acids allosterically regulate the thiamine diphosphate-dependent alpha-keto acid decarboxylase from Mycobacterium tuberculosis."
Werther T., Spinka M., Tittmann K., Schuetz A., Golbik R., Mrestani-Klaus C., Huebner G., Koenig S.
J. Biol. Chem. 283:5344-5354(2008) [PubMed: 18086676] [Abstract]
Cited for: FUNCTION AS AN ALPHA-KETO-ACID DECARBOXYLASE, REGULATION.
Strain: ATCC 25618 / H37Rv.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842574 Genomic DNA. Translation: CAA17659.1.
AE000516 Genomic DNA. Translation: AAK45117.1.
PIRE70814.
RefSeqNP_215368.1. NC_000962.2.
NP_335303.1. NC_002755.2.

3D structure databases

HSSPHSSP built from PDB template 1PVD based on UniProtKB P06169.
ProteinModelPortalO53865.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001239; EBMYCP00000001239; EBMYCG00000001239.
EBMYCT00000071456; EBMYCP00000069515; EBMYCG00000071451.
GeneID885576.
926185.
GenomeReviewsGene locus MT0876 in contig AE000516_GR.
Gene locus Rv0853c in contig AL123456_GR.
KEGGmtc:MT0876.
mtu:Rv0853c.
PATRIC18123680. VBIMycTub22151_0964.
TIGRMT0876.

Organism-specific databases

TubercuListRv0853c.

Phylogenomic databases

GeneTreeEBGT00050000014643.
HOGENOMHBG479104.
OMADIILADQ.
PhylomeDBO53865.
ProtClustDBCLSK790786.

Family and domain databases

InterProIPR012110. Pyruvt_ip_decrb.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
KOK04103.
PANTHERPTHR18968:SF4. PTHR18968:SF4. 1 hit.
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFPIRSF036565. Pyruvt_ip_decrb. 1 hit.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKDC_MYCTU
AccessionPrimary (citable) accession number: O53865
Secondary accession number(s): Q7D958
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families