Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei364Sequence analysis1
Active sitei368Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6731-MONOMER.

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004205201 – 393Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complexAdd BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

PaxDbiO06159.
PRIDEiO06159.

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

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi172 – 187Combined sources16
Beta strandi190 – 198Combined sources9
Helixi200 – 209Combined sources10
Turni210 – 212Combined sources3
Helixi218 – 232Combined sources15
Helixi234 – 236Combined sources3
Beta strandi237 – 241Combined sources5
Turni243 – 245Combined sources3
Beta strandi248 – 251Combined sources4
Beta strandi257 – 259Combined sources3
Beta strandi261 – 263Combined sources3
Beta strandi266 – 268Combined sources3
Helixi275 – 277Combined sources3
Helixi280 – 296Combined sources17
Helixi301 – 304Combined sources4
Beta strandi308 – 312Combined sources5
Helixi314 – 317Combined sources4
Beta strandi331 – 336Combined sources6
Beta strandi340 – 346Combined sources7
Beta strandi349 – 363Combined sources15
Turni364 – 366Combined sources3
Helixi369 – 384Combined sources16
Helixi386 – 389Combined sources4
Turni390 – 392Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L60X-ray2.00A154-393[»]
ProteinModelPortaliO06159.
SMRiO06159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO06159.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 82Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini116 – 155E3-bindingAdd BLAST40

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L60X-ray2.00A154-393[»]
ProteinModelPortaliO06159.
SMRiO06159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2495c.

Proteomic databases

PaxDbiO06159.
PRIDEiO06159.

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.

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6731-MONOMER.

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: November 2, 2016
This is version 116 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.