O06160 (BKDB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-methyl-2-oxobutanoate dehydrogenase subunit beta
EC=1.2.4.4

Alternative name(s):
Branched-chain alpha-ketoacid dehydrogenase E1 component subunit beta
Short name=BCKADH E1-beta

Gene names

Name:	bkdB
Synonyms:	pdhB
Ordered Locus Names:	Rv2496c, MT2571

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO2. Ref.4 Ref.5
Catalytic activity	3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate By similarity.
Subunit structure	Heteromer of E1 alpha (BkdA) and beta (BkdB) subunits. Makes part of the BCKADH complex, consisting of multiple copies of BkdA/BkdB (E1), BkdC (E2) and Lpd (E3). Ref.4 Ref.5
Induction	Up-regulated upon nutrient starvation. Is also highly up-regulated in a DlaT-deficient strain. Part of the bkdABC operon. Ref.3 Ref.5

Ontologies

Keywords
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 14532352PubMed 15525680. Source: MTBBASE
Molecular_function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 348	348	3-methyl-2-oxobutanoate dehydrogenase subunit beta		PRO_0000420519
Regions
	Region	80 – 82	3	Thiamine pyrophosphate By similarity
	Region	105 – 108	4	Substrate By similarity
	Region	108 – 111	4	Thiamine pyrophosphate By similarity
Sites
	Active site	151	1	Proton acceptor By similarity
	Binding site	51	1	Thiamine pyrophosphate By similarity
	Binding site	104	1	Thiamine pyrophosphate By similarity
	Binding site	151	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O06160 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 71D54633EEEB9A3E	FASTA	348	38,064
	10 20 30 40 50 60 MTQIADRPAR PDETLAVAVS DITQSLTMVQ AINRALYDAM AADERVLVFG EDVAVEGGVF 70 80 90 100 110 120 RVTEGLADTF GADRCFDTPL AESAIIGIAV GLALRGFVPV PEIQFDGFSY PAFDQVVSHL 130 140 150 160 170 180 AKYRTRTRGE VDMPVTVRIP SFGGIGAAEH HSDSTESYWV HTAGLKVVVP STPGDAYWLL 190 200 210 220 230 240 RHAIACPDPV MYLEPKRRYH GRGMVDTSRP EPPIGHAMVR RSGTDVTVVT YGNLVSTALS 250 260 270 280 290 300 SADTAEQQHD WSLEVIDLRS LAPLDFDTIA ASIQRTGRCV VMHEGPRSLG YGAGLAARIQ 310 320 330 340 EEMFYQLEAP VLRACGFDTP YPPARLEKLW LPGPDRLLDC VERVLRQP

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling." Betts J.C., Lukey P.T., Robb L.C., McAdam R.A., Duncan K. Mol. Microbiol. 43:717-731(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY STARVATION. Strain: ATCC 25618 / H37Rv.
[4]	"Mycobacterium tuberculosis appears to lack alpha-ketoglutarate dehydrogenase and encodes pyruvate dehydrogenase in widely separated genes." Tian J., Bryk R., Shi S., Erdjument-Bromage H., Tempst P., Nathan C. Mol. Microbiol. 57:859-868(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NO FUNCTION AS A PDH COMPONENT, SUBUNIT. Strain: ATCC 25618 / H37Rv.
[5]	"Virulence of Mycobacterium tuberculosis depends on lipoamide dehydrogenase, a member of three multienzyme complexes." Venugopal A., Bryk R., Shi S., Rhee K., Rath P., Schnappinger D., Ehrt S., Nathan C. Cell Host Microbe 9:21-31(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A BCKADH COMPONENT, INDUCTION, GENE NAME, IDENTIFICATION IN THE BCKADH COMPLEX. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842580 Genomic DNA. Translation: CAB08929.1. AE000516 Genomic DNA. Translation: AAK46875.1. AL123456 Genomic DNA. Translation: CCP45290.1.
PIR	H70549.
RefSeq	NP_217012.1. NC_000962.3. NP_337061.1. NC_002755.2. YP_006515935.1. NC_018143.1.
3D structure databases
HSSP	HSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
ProteinModelPortal	O06160.
SMR	O06160. Positions 26-345.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv2496c.
Proteomic databases
PRIDE	O06160.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK46875; AAK46875; MT2571.
GeneID	13319211. 888571. 925755.
KEGG	mtc:MT2571. mtu:Rv2496c. mtv:RVBD_2496c.
PATRIC	18127408. VBIMycTub22151_2809.
Organism-specific databases
TubercuList	Rv2496c.
Phylogenomic databases
HOGENOM	HOG000281451.
KO	K00162.
OMA	FRPVVEM.
ProtClustDB	CLSK791883.
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
InterPro	IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view]
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BKDB_MYCTU

Accession

Primary (citable) accession number: O06160
Secondary accession number(s): F2GH62, L0T9T3, Q7D715

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program