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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: -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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(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

Keywordsi

Molecular functionAcyltransferase, 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

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
Domaini119 – 157Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST39

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4107RN0 Bacteria
COG0508 LUCA
HOGENOMiHOG000281564
InParanoidiO06159
KOiK00627
OMAiSWRLGCD
PhylomeDBiO06159

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR001078 2-oxoacid_DH_actylTfrase
IPR015761 BCKADH_E2
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PANTHERiPTHR43178:SF5 PTHR43178:SF5, 2 hits
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS51826 PSBD, 1 hit

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
PATRICifig|83332.12.peg.2797

Similar proteinsi

Entry informationi

Entry nameiBKDC_MYCTU
AccessioniPrimary (citable) accession number: O06159
Secondary accession number(s): L0TBD7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: August 1, 1998
Last modified: March 28, 2018
This is version 123 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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