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 3 of pyruvate dehydrogenase complex, mitochondrial

Gene

At1g54220

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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).1 Publication

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei512 – 5121Sequence Analysis
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

Enzyme and pathway databases

BioCyciARA:AT1G54220-MONOMER.
ARA:GQT-1082-MONOMER.
ReactomeiREACT_235684. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_242640. Pyruvate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide S-acetyltransferase component 3 of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2 3
Short name:
PDC-E2 3
Short name:
PDCE2 3
Gene namesi
Ordered Locus Names:At1g54220
ORF Names:F20D21.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G54220.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: TAIR
  3. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 539Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrialPRO_0000260027
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei152 – 1521N6-lipoyllysineBy similarityPROSITE-ProRule annotation

Proteomic databases

PaxDbiQ5M729.
PRIDEiQ5M729.

Expressioni

Gene expression databases

GenevestigatoriQ5M729.

Structurei

3D structure databases

ProteinModelPortaliQ5M729.
SMRiQ5M729. Positions 113-192, 305-539.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 18777Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni250 – 28132E3-binding siteBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiQ5M729.
KOiK00627.
OMAiHEIPHAW.
PhylomeDBiQ5M729.

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.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5M729-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAYASRIINH SKKLKDVSTL LRRENAATIR YYSNTNRAPL NREDTFNSRL
60 70 80 90 100
GYPPLERISI CSTSTLPVSI IFSTTRSNLS SAMGRPIFGK EFSCLMQSAR
110 120 130 140 150
GFSSGSDLPP HQEIGMPSLS PTMTEGNIAR WLKKEGDKVA PGEVLCEVET
160 170 180 190 200
DKATVEMECM EEGYLAKIVK AEGSKEIQVG EVIAITVEDE EDIGKFKDYT
210 220 230 240 250
PSSTADAAPT KAEPTPAPPK EEKVKQPSSP PEPKASKPST PPTGDRVFAS
260 270 280 290 300
PLARKLAEDN NVPLSDIEGT GPEGRIVKAD IDEYLASSGK GATAKPSKST
310 320 330 340 350
DSKAPALDYV DIPHSQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKLMALR
360 370 380 390 400
SQLNSFKEAS GGKRISVNDL VVKAAALALR KVPQCNSSWT DDYIRQFKNV
410 420 430 440 450
NINVAVQTEN GLYVPVVKDA DRKGLSTIGE EVRLLAQKAK ENSLKPEDYE
460 470 480 490 500
GGTFTVSNLG GPFGIKQFCA VVNPPQAAIL AVGSAEKRVV PGNGPDQFNF
510 520 530
ASYMPVTLSC DHRVVDGAIG AEWLKAFKGY IENPKSMLL
Length:539
Mass (Da):58,467
Last modified:February 1, 2005 - v1
Checksum:i0C4E141079A2698F
GO

Sequence cautioni

The sequence AAD25602.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451T → I in AAK53067. 1 PublicationCurated
Sequence conflicti267 – 2671I → T in AAK53067. 1 PublicationCurated
Sequence conflicti442 – 4421N → S in AAM97076. (PubMed:14593172)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033001 mRNA. Translation: AAK53067.1.
AC005287 Genomic DNA. Translation: AAD25602.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33067.1.
CP002684 Genomic DNA. Translation: AEE33068.1.
AY136410 mRNA. Translation: AAM97076.1.
BT020419 mRNA. Translation: AAV97810.1.
PIRiE96583.
RefSeqiNP_001031186.1. NM_001036109.1.
NP_564654.1. NM_104300.3.
UniGeneiAt.19093.
At.21338.

Genome annotation databases

EnsemblPlantsiAT1G54220.1; AT1G54220.1; AT1G54220.
AT1G54220.2; AT1G54220.2; AT1G54220.
GeneIDi841863.
KEGGiath:AT1G54220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033001 mRNA. Translation: AAK53067.1.
AC005287 Genomic DNA. Translation: AAD25602.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33067.1.
CP002684 Genomic DNA. Translation: AEE33068.1.
AY136410 mRNA. Translation: AAM97076.1.
BT020419 mRNA. Translation: AAV97810.1.
PIRiE96583.
RefSeqiNP_001031186.1. NM_001036109.1.
NP_564654.1. NM_104300.3.
UniGeneiAt.19093.
At.21338.

3D structure databases

ProteinModelPortaliQ5M729.
SMRiQ5M729. Positions 113-192, 305-539.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ5M729.
PRIDEiQ5M729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G54220.1; AT1G54220.1; AT1G54220.
AT1G54220.2; AT1G54220.2; AT1G54220.
GeneIDi841863.
KEGGiath:AT1G54220.

Organism-specific databases

TAIRiAT1G54220.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiQ5M729.
KOiK00627.
OMAiHEIPHAW.
PhylomeDBiQ5M729.

Enzyme and pathway databases

BioCyciARA:AT1G54220-MONOMER.
ARA:GQT-1082-MONOMER.
ReactomeiREACT_235684. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_242640. Pyruvate metabolism.

Gene expression databases

GenevestigatoriQ5M729.

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.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mono-lipoyl E2 from pyruvate dehydrogenase complex from Arabidopsis."
    Broz A.K., Randall D.D., Miernyk J.A., Mooney B.P.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Arabidopsis ORF clones."
    Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.
  7. "Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis."
    Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.
    Plant Physiol. 134:838-848(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiODP23_ARATH
AccessioniPrimary (citable) accession number: Q5M729
Secondary accession number(s): Q8L787, Q94IP5, Q9SLL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2006
Last sequence update: February 1, 2005
Last modified: February 4, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.