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P35489

- ODP2_ACHLA

UniProt

P35489 - ODP2_ACHLA

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Acholeplasma laidlawii
Status
Reviewed - Annotation score: 3 out of 5- 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 N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateCuratedNote: Binds 2 lipoyl cofactors covalently.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei516 – 5161Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

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
OrganismiAcholeplasma laidlawii
Taxonomic identifieri2148 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeAcholeplasma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 544544Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-lipoyllysineBy similarityPROSITE-ProRule annotation
Modified residuei154 – 1541N6-lipoyllysineBy similarityPROSITE-ProRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP35489.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Lipoyl-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini113 – 18876Lipoyl-binding 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 2 lipoyl-binding domains.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl, Repeat

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35489-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYEFKFADIG EGIHEGTVLQ WNFKVGDKVK EGETLVIVET DKVNAELPSP
60 70 80 90 100
VDGTIVSLGA KEGEEIHVGQ IIVTIDDGTG TPAAAPAPAQ VSAPTPAPAA
110 120 130 140 150
APQVAAPAAS GDIYDFKFAD IGEGIHEGTI LQWNFKVGDK VKEGETLVVV
160 170 180 190 200
ETDKVNAELP SPVDGTILKL GKAEGEVIHV GETVVLIGQN GATLEQAQAP
210 220 230 240 250
KAEAPVSEPK KGAGVVGEIE VSDDIIGGSE EVHVVATTGK VLASPVARKL
260 270 280 290 300
ASDLGVDIAT IKGSGEQGRV MKDDVQNSKA PAEAQAPVQQ TQAPAQAAAS
310 320 330 340 350
VAPSFAAAGK PQGDVEVVKI TRLRKAVSNA MTRSKSIIPE TVLMDEINVD
360 370 380 390 400
ALVNFRNEAK GLAESKGIKL TYMAFIAKAV LIALKEFPMF NASFNHDTDE
410 420 430 440 450
VYIKKFINLG MAVDTPDGLI VPNIKNADRL SVFELASQVR SLADDTIARK
460 470 480 490 500
ISMDQQTGGT FTITNFGSAG IAFGTPVINY PELAILGIGK IDRKPWVVGN
510 520 530 540
EIKIAHTLPL SLAVDHRIID GADGGRFLMR VKELLTNPTL LLLS
Length:544
Mass (Da):57,261
Last modified:June 1, 1994 - v1
Checksum:i81E92D869CFD5424
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81753 Genomic DNA. Translation: AAA21909.1.
PIRiC42653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81753 Genomic DNA. Translation: AAA21909.1 .
PIRi C42653.

3D structure databases

ProteinModelPortali P35489.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii."
    Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.
    J. Bacteriol. 174:1388-1396(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiODP2_ACHLA
AccessioniPrimary (citable) accession number: P35489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3