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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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).

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 sitei399Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

Enzyme and pathway databases

BRENDAi2.3.1.12 623

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
Gene namesi
Name:pdhC
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001622732 – 428Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST427

Amino acid modifications

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

Interactioni

Subunit structurei

Forms a 60-polypeptide structural core with icosahedral symmetry.

Binary interactionsi

WithEntry#Exp.IntActNotes
pdhDP119593EBI-1040691,EBI-9021392

Protein-protein interaction databases

DIPiDIP-6156N
IntActiP11961, 3 interactors

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Beta strandi16 – 21Combined sources6
Beta strandi37 – 40Combined sources4
Beta strandi45 – 48Combined sources4
Beta strandi59 – 61Combined sources3
Beta strandi63 – 67Combined sources5
Beta strandi69 – 71Combined sources3
Helixi133 – 141Combined sources9
Turni146 – 148Combined sources3
Helixi154 – 156Combined sources3
Helixi160 – 167Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B5SX-ray4.40A/B/C/D/E185-426[»]
1EBDX-ray2.60C130-170[»]
1LABNMR-A2-81[»]
1LACNMR-A2-81[»]
1W3DNMR-A119-171[»]
1W4ENMR-A126-170[»]
1W4FNMR-A126-170[»]
1W4GNMR-A126-170[»]
1W85X-ray2.00I/J123-171[»]
1W88X-ray2.30I/J123-171[»]
2PDDNMR-A129-171[»]
2PDENMR-A129-171[»]
3DUFX-ray2.50I/J1-428[»]
3DV0X-ray2.50I/J1-428[»]
3DVAX-ray2.35I/J1-428[»]
ProteinModelPortaliP11961
SMRiP11961
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11961

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini130 – 167Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

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.

P11961-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV NEDDVLCEVQ NDKAVVEIPS
60 70 80 90 100
PVKGKVLEIL VPEGTVATVG QTLITLDAPG YENMTFKGQE QEEAKKEEKT
110 120 130 140 150
ETVSKEEKVD AVAPNAPAAE AEAGPNRRVI AMPSVRKYAR EKGVDIRLVQ
160 170 180 190 200
GTGKNGRVLK EDIDAFLAGG AKPAPAAAEE KAAPAAAKPA TTEGEFPETR
210 220 230 240 250
EKMSGIRRAI AKAMVHSKHT APHVTLMDEA DVTKLVAHRK KFKAIAAEKG
260 270 280 290 300
IKLTFLPYVV KALVSALREY PVLNTSIDDE TEEIIQKHYY NIGIAADTDR
310 320 330 340 350
GLLVPVIKHA DRKPIFALAQ EINELAEKAR DGKLTPGEMK GASCTITNIG
360 370 380 390 400
SAGGQWFTPV INHPEVAILG IGRIAEKPIV RDGEIVAAPM LALSLSFDHR
410 420
MIDGATAQKA LNHIKRLLSD PELLLMEA
Length:428
Mass (Da):46,326
Last modified:January 23, 2007 - v3
Checksum:i2600CD150261ACB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA Translation: CAA37630.1
PIRiS10799 S14426
RefSeqiWP_033016211.1, NZ_LUCR01000041.1

Similar proteinsi

Entry informationi

Entry nameiODP2_GEOSE
AccessioniPrimary (citable) accession number: P11961
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 129 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
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Main funding by: National Institutes of Health