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Protein

Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex

Gene

bkdC

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO2.1 Publication

Catalytic activityi

2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.

Cofactori

(R)-lipoate1 PublicationNote: Binds 1 lipoyl cofactor covalently.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei364 – 3641Sequence analysis
Active sitei368 – 3681Sequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex (EC:2.3.1.168)
Alternative name(s):
Branched-chain alpha-ketoacid dehydrogenase complex component E2
Short name:
BCKADH E2
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
Gene namesi
Name:bkdC
Synonyms:pdhC
Ordered Locus Names:Rv2495c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2495c.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complexPRO_0000420520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Proteomic databases

PaxDbiO06159.

Expressioni

Inductioni

Up-regulated upon nutrient starvation. Is also highly up-regulated in a DlaT-deficient strain. Part of the bkdABC operon.2 Publications

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry (By similarity). Part of the BCKADH complex, consisting of multiple copies of BkdA/BkdB (E1), BkdC (E2) and Lpd (E3).By similarity1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2495c.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi172 – 18716Combined sources
Beta strandi190 – 1989Combined sources
Helixi200 – 20910Combined sources
Turni210 – 2123Combined sources
Helixi218 – 23215Combined sources
Helixi234 – 2363Combined sources
Beta strandi237 – 2415Combined sources
Turni243 – 2453Combined sources
Beta strandi248 – 2514Combined sources
Beta strandi257 – 2593Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi266 – 2683Combined sources
Helixi275 – 2773Combined sources
Helixi280 – 29617Combined sources
Helixi301 – 3044Combined sources
Beta strandi308 – 3125Combined sources
Helixi314 – 3174Combined sources
Beta strandi331 – 3366Combined sources
Beta strandi340 – 3467Combined sources
Beta strandi349 – 36315Combined sources
Turni364 – 3663Combined sources
Helixi369 – 38416Combined sources
Helixi386 – 3894Combined sources
Turni390 – 3923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L60X-ray2.00A154-393[»]
ProteinModelPortaliO06159.
SMRiO06159. Positions 10-83, 117-155, 165-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO06159.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 8276Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini116 – 15540E3-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 E3-binding domain.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4107RN0. Bacteria.
COG0508. LUCA.
HOGENOMiHOG000281564.
InParanoidiO06159.
KOiK00627.
OMAiEVELVEW.
PhylomeDBiO06159.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O06159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGEDSIRSF PVPDLGEGLQ EVTVTCWSVA VGDDVEINQT LCSVETAKAE
60 70 80 90 100
VEIPSPYAGR IVELGGAEGD VLKVGAELVR IDTGPTAVAQ PNGEGAVPTL
110 120 130 140 150
VGYGADTAIE TSRRTSRPLA APVVRKLAKE LAVDLAALQR GSGAGGVITR
160 170 180 190 200
ADVLAAARGG VGAGPDVRPV HGVHARMAEK MTLSHKEIPT AKASVEVICA
210 220 230 240 250
ELLRLRDRFV SAAPEITPFA LTLRLLVIAL KHNVILNSTW VDSGEGPQVH
260 270 280 290 300
VHRGVHLGFG AATERGLLVP VVTDAQDKNT RELASRVAEL ITGAREGTLT
310 320 330 340 350
PAELRGSTFT VSNFGALGVD DGVPVINHPE AAILGLGAIK PRPVVVGGEV
360 370 380 390
VARPTMTLTC VFDHRVVDGA QVAQFMCELR DLIESPETAL LDL
Length:393
Mass (Da):41,061
Last modified:August 1, 1998 - v2
Checksum:i555F4941FC7B487E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45289.1.
PIRiG70549.
RefSeqiNP_217011.1. NC_000962.3.
WP_010886148.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP45289; CCP45289; Rv2495c.
GeneIDi888237.
KEGGimtu:Rv2495c.
PATRICi18154153. VBIMycTub87468_2797.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45289.1.
PIRiG70549.
RefSeqiNP_217011.1. NC_000962.3.
WP_010886148.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L60X-ray2.00A154-393[»]
ProteinModelPortaliO06159.
SMRiO06159. Positions 10-83, 117-155, 165-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2495c.

Proteomic databases

PaxDbiO06159.

Protocols and materials databases

DNASUi888237.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45289; CCP45289; Rv2495c.
GeneIDi888237.
KEGGimtu:Rv2495c.
PATRICi18154153. VBIMycTub87468_2797.

Organism-specific databases

TubercuListiRv2495c.

Phylogenomic databases

eggNOGiENOG4107RN0. Bacteria.
COG0508. LUCA.
HOGENOMiHOG000281564.
InParanoidiO06159.
KOiK00627.
OMAiEVELVEW.
PhylomeDBiO06159.

Miscellaneous databases

EvolutionaryTraceiO06159.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBKDC_MYCTU
AccessioniPrimary (citable) accession number: O06159
Secondary accession number(s): L0TBD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.