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 acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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) (By similarity).By similarity

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei412Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciZMOB264203:G1FZK-445-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
Gene namesi
Name:pdhC
Synonyms:pdhB
Ordered Locus Names:ZMO0510
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622961 – 440Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST440

Amino acid modifications

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

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

Structurei

3D structure databases

ProteinModelPortaliO66119
SMRiO66119
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 78Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST77
Domaini149 – 186Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

HOGENOMiHOG000281566
KOiK00627
OMAiLEMPKWG

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
IPR006257 LAT1
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
TIGRFAMsiTIGR01349 PDHac_trf_mito, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

O66119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIEVKMPAL SPTMTEGTLA KWLVKEGDAV KAGDILAEIE TDKAIMEFET
60 70 80 90 100
VDAGIIAKIL VPEGSENIAV GQVIAVMAEA GEDVSQVAAS ASSQISEPSE
110 120 130 140 150
KADVAQKETA DSETISIDAS LDKAISNAGY GNKTENMTAS YQEKAGRIKA
160 170 180 190 200
SPLAKRLAKK NHVDLKQVNG SGPHGRIIKA DIEAFIAEAN QASSNPSVST
210 220 230 240 250
PEASGKITHD TPHNSIKLSN MRRVIARRLT ESKQNIPHIY LTVDVQMDAL
260 270 280 290 300
LKLRSELNES LAVQNIKISV NDMLIKAQAL ALKATPNVNV AFDGDQMLQF
310 320 330 340 350
SQADISVAVS VEGGLITPIL KQADTKSLSA LSVEMKELIA RAREGRLQPQ
360 370 380 390 400
EYQGGTSSIS NMGMFGIKQF NAVINPPQAS ILAIGSGERR PWVIDDAITI
410 420 430 440
ATVATITGSF DHRVIDGADA AAFMSAFKHL VEKPLGILAQ
Length:440
Mass (Da):46,833
Last modified:February 15, 2005 - v2
Checksum:i6BC8A592FC0AF6B3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti169N → S in CAA63808 (PubMed:9515924).Curated1
Sequence conflicti186 – 188IAE → VTG in CAA63808 (PubMed:9515924).Curated3
Sequence conflicti203A → V in CAA63808 (PubMed:9515924).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93605 Genomic DNA Translation: CAA63808.1
AE008692 Genomic DNA Translation: AAV89134.1
RefSeqiWP_011240414.1, NC_006526.2

Genome annotation databases

EnsemblBacteriaiAAV89134; AAV89134; ZMO0510
KEGGizmo:ZMO0510

Similar proteinsi

Entry informationi

Entry nameiODP2_ZYMMO
AccessioniPrimary (citable) accession number: O66119
Secondary accession number(s): Q5NQ71
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: March 28, 2018
This is version 115 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health