SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5M729

- ODP23_ARATH

UniProt

Q5M729 - ODP23_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial
Gene
At1g54220, F20D21.4
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei512 – 5121 Reviewed prediction
Active sitei516 – 5161 Reviewed prediction

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
  2. pyruvate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciARA:AT1G54220-MONOMER.
ARA:GQT-1082-MONOMER.

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-lipoyllysine By similarity

Proteomic databases

PaxDbiQ5M729.
PRIDEiQ5M729.

Expressioni

Gene expression databases

GenevestigatoriQ5M729.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 18675Lipoyl-binding
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni250 – 28132E3-binding site By similarity
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiQ5M729.
KOiK00627.
OMAiGSADGQY.
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

MAYASRIINH SKKLKDVSTL LRRENAATIR YYSNTNRAPL NREDTFNSRL    50
GYPPLERISI CSTSTLPVSI IFSTTRSNLS SAMGRPIFGK EFSCLMQSAR 100
GFSSGSDLPP HQEIGMPSLS PTMTEGNIAR WLKKEGDKVA PGEVLCEVET 150
DKATVEMECM EEGYLAKIVK AEGSKEIQVG EVIAITVEDE EDIGKFKDYT 200
PSSTADAAPT KAEPTPAPPK EEKVKQPSSP PEPKASKPST PPTGDRVFAS 250
PLARKLAEDN NVPLSDIEGT GPEGRIVKAD IDEYLASSGK GATAKPSKST 300
DSKAPALDYV DIPHSQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKLMALR 350
SQLNSFKEAS GGKRISVNDL VVKAAALALR KVPQCNSSWT DDYIRQFKNV 400
NINVAVQTEN GLYVPVVKDA DRKGLSTIGE EVRLLAQKAK ENSLKPEDYE 450
GGTFTVSNLG GPFGIKQFCA VVNPPQAAIL AVGSAEKRVV PGNGPDQFNF 500
ASYMPVTLSC DHRVVDGAIG AEWLKAFKGY IENPKSMLL 539
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.

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi E96583.
RefSeqi NP_001031186.1. NM_001036109.1.
NP_564654.1. NM_104300.3.
UniGenei At.19093.
At.21338.

3D structure databases

ProteinModelPortali Q5M729.
SMRi Q5M729. Positions 113-192, 305-539.
ModBasei Search...

Proteomic databases

PaxDbi Q5M729.
PRIDEi Q5M729.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G54220.1 ; AT1G54220.1 ; AT1G54220 .
AT1G54220.2 ; AT1G54220.2 ; AT1G54220 .
GeneIDi 841863.
KEGGi ath:AT1G54220.

Organism-specific databases

TAIRi AT1G54220.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281566.
InParanoidi Q5M729.
KOi K00627.
OMAi GSADGQY.
PhylomeDBi Q5M729.

Enzyme and pathway databases

BioCyci ARA:AT1G54220-MONOMER.
ARA:GQT-1082-MONOMER.

Gene expression databases

Genevestigatori Q5M729.

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.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 75 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