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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
The B.subtilis PDH complex possesses also branched-chain 2-oxoacid dehydrogenase (BCDH) activity.

Catalytic activityi

Acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei413Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciBSUB:BSU14600-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2
S complex, 48 kDa subunit
Gene namesi
Name:pdhC
Synonyms:aceC
Ordered Locus Names:BSU14600
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001622742 – 442Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST441

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-lipoyllysinePROSITE-ProRule annotation1 Publication1

Proteomic databases

PaxDbiP21883
PRIDEiP21883

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

IntActiP21883, 1 interactor
STRINGi224308.Bsubs1_010100008096

Structurei

3D structure databases

ProteinModelPortaliP21883
SMRiP21883
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini141 – 178Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4105C7S Bacteria
COG0508 LUCA
HOGENOMiHOG000281564
InParanoidiP21883
KOiK00627
OMAiTMEFESF
PhylomeDBiP21883

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
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
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFEFKLPDI GEGIHEGEIV KWFVKPNDEV DEDDVLAEVQ NDKAVVEIPS
60 70 80 90 100
PVKGKVLELK VEEGTVATVG QTIITFDAPG YEDLQFKGSD ESDDAKTEAQ
110 120 130 140 150
VQSTAEAGQD VAKEEQAQEP AKATGAGQQD QAEVDPNKRV IAMPSVRKYA
160 170 180 190 200
REKGVDIRKV TGSGNNGRVV KEDIDSFVNG GAQEAAPQET AAPQETAAKP
210 220 230 240 250
AAAPAPEGEF PETREKMSGI RKAIAKAMVN SKHTAPHVTL MDEVDVTNLV
260 270 280 290 300
AHRKQFKQVA ADQGIKLTYL PYVVKALTSA LKKFPVLNTS IDDKTDEVIQ
310 320 330 340 350
KHYFNIGIAA DTEKGLLVPV VKNADRKSVF EISDEINGLA TKAREGKLAP
360 370 380 390 400
AEMKGASCTI TNIGSAGGQW FTPVINHPEV AILGIGRIAE KAIVRDGEIV
410 420 430 440
AAPVLALSLS FDHRMIDGAT AQNALNHIKR LLNDPQLILM EA
Length:442
Mass (Da):47,539
Last modified:January 23, 2007 - v2
Checksum:i73AFC68220717C34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57435 Genomic DNA Translation: AAA62683.1
AF012285 Genomic DNA Translation: AAC24934.1
AL009126 Genomic DNA Translation: CAB13333.1
PIRiD36718
RefSeqiNP_389343.1, NC_000964.3
WP_003232311.1, NZ_JNCM01000035.1

Genome annotation databases

EnsemblBacteriaiCAB13333; CAB13333; BSU14600
GeneIDi936010
KEGGibsu:BSU14600
PATRICifig|224308.179.peg.1592

Similar proteinsi

Entry informationi

Entry nameiODP2_BACSU
AccessioniPrimary (citable) accession number: P21883
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 131 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

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health