Reviewed, UniProtKB/Swiss-Prot O53865 (KDC_MYCTU)

Names and origin

Protein names

Recommended name:
    Alpha-keto-acid decarboxylase
      Short name=KDC
    EC=4.1.1.-

Gene names

Name:	kdc
Ordered Locus Names:	Rv0853c, MT0876

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	560 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Decarboxylates branched-chain and aromatic alpha-keto acids to aldehydes. Ref.4
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.
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

Ontologies

Keywords
Ligand	Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Decarboxylase Lyase
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Molecular function	carboxy-lyase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 560	560	Alpha-keto-acid decarboxylase		PRO_0000333751
Regions
	Region	396 – 478	83	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	446	1	Magnesium By similarity
	Metal binding	473	1	Magnesium By similarity
	Metal binding	475	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	61	1	Thiamine pyrophosphate By similarity
Experimental info
	Sequence conflict	297	1	D → N in AAK45117. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O53865-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: F0430F720D57B7C4	FASTA	560	59,783
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX842574 Genomic DNA. Translation: CAA17659.1. AE000516 Genomic DNA. Translation: AAK45117.1.
PIR	E70814.
RefSeq	NP_215368.1. NP_335303.1.
3D structure databases
HSSP	HSSP built from PDB template 1PVD based on UniProtKB P06169.
ModBase	Search...
Genome annotation databases
GeneID	885576. 926185.
GenomeReviews	Gene locus MT0876 in contig AE000516_GR. Gene locus Rv0853c in contig AL123456_GR.
KEGG	mtc:MT0876. mtu:Rv0853c.
TIGR	MT0876.
Organism-specific databases
TubercuList	Rv0853c.
Phylogenomic databases
HOGENOM	O53865.
OMA	O53865. ADQGTAA.
Family and domain databases
InterPro	IPR012110. Pyruvt_ip_decrb. IPR000399. TPP_bd_CS. IPR012001. TPP_bd_enzyme_N. IPR011766. TPP_enzyme_bd_C. IPR012000. TPP_enzyme_M. [Graphical view]
Pfam	PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view]
PIRSF	PIRSF036565. Pyruvt_ip_decrb. 1 hit.
PROSITE	PS00187. TPP_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KDC_MYCTU

Accession

Primary (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:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)