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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene
N/A
Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 4 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)-lipoateBy similarityNote: Binds 3 lipoyl cofactors covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei611 – 6111Sequence analysis

GO - Molecular functioni

GO - Biological processi

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
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 638637Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-lipoyllysinePROSITE-ProRule annotation
Modified residuei157 – 1571N6-lipoyllysinePROSITE-ProRule annotation
Modified residuei262 – 2621N6-lipoyllysinePROSITE-ProRule annotation

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

STRINGi322710.Avin_44910.

Structurei

Secondary structure

1
638
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi11 – 199Combined sources
Beta strandi29 – 379Combined sources
Beta strandi42 – 465Combined sources
Beta strandi48 – 5710Combined sources
Beta strandi63 – 653Combined sources
Beta strandi68 – 747Combined sources
Helixi404 – 4063Combined sources
Helixi417 – 43216Combined sources
Beta strandi435 – 4439Combined sources
Helixi445 – 4539Combined sources
Helixi455 – 4606Combined sources
Helixi468 – 48114Combined sources
Helixi483 – 4864Combined sources
Beta strandi487 – 4893Combined sources
Beta strandi496 – 4983Combined sources
Beta strandi504 – 5063Combined sources
Beta strandi508 – 5103Combined sources
Beta strandi513 – 5153Combined sources
Beta strandi518 – 5203Combined sources
Helixi522 – 5243Combined sources
Helixi527 – 54216Combined sources
Helixi548 – 5514Combined sources
Beta strandi555 – 5606Combined sources
Turni562 – 5643Combined sources
Beta strandi577 – 5837Combined sources
Beta strandi587 – 5926Combined sources
Beta strandi594 – 61017Combined sources
Turni611 – 6133Combined sources
Helixi616 – 63116Combined sources
Helixi633 – 6375Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPBX-ray2.50A396-638[»]
1DPCX-ray2.60A396-638[»]
1DPDX-ray2.70A396-638[»]
1EAAX-ray2.60A396-638[»]
1EABX-ray2.60A396-638[»]
1EACX-ray2.60A396-638[»]
1EADX-ray2.60A396-638[»]
1EAEX-ray2.60A396-638[»]
1EAFX-ray2.60A396-638[»]
1IYUNMR-A2-79[»]
1IYVNMR-A2-79[»]
ProteinModelPortaliP10802.
SMRiP10802. Positions 2-79, 396-638.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7473Lipoyl-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini117 – 19175Lipoyl-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini222 – 29675Lipoyl-binding 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni328 – 38154E1/E3 bindingAdd
BLAST
Regioni382 – 638257CatalyticAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 3 lipoyl-binding domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiENOG4107QSN. Bacteria.
COG0508. LUCA.

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.
IPR006256. AcTrfase_Pyrv_DH_cplx.
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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10802-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEIIRVPDI GGDGEVIELL VKTGDLIEVE QGLVVLESAK ASMEVPSPKA
60 70 80 90 100
GVVKSVSVKL GDKLKEGDAI IELEPAAGAA AAPAEAAAVP AAPTQAVDEA
110 120 130 140 150
EAPSPGASAT PAPAAASQEV RVPDIGSAGK ARVIEVLVKA GDQVQAEQSL
160 170 180 190 200
IVLESDKASM EIPSPASGVV ESVAIQLNAE VGTGDLILTL RTTGAQAQPT
210 220 230 240 250
APAAAAAASP APAPLAPAAA GPQEVKVPDI GSAGKARVIE VLVKAGDQVQ
260 270 280 290 300
AEQSLIVLES DKASMEIPSP AAGVVESVAV QLNAEVGTGD QILTLRVAGA
310 320 330 340 350
APSGPRARGS PGQAAAAPGA APAPAPVGAP SRNGAKVHAG PAVRQLAREF
360 370 380 390 400
GVELAAINST GPRGRILKED VQAYVKAMMQ KAKEAPAAGA ASGAGIPPIP
410 420 430 440 450
PVDFAKYGEI EEVPMTRLMQ IGATNLHRSW LNVPHVTQFE SADITELEAF
460 470 480 490 500
RVAQKAVAEK AGVKLTVLPL LLKACAYLLK ELPDFNSSLA PSGQALIRKK
510 520 530 540 550
YVHIGFAVDT PDGLLVPVIR NVDQKSLLQL AAEAAELAEK ARSKKLGADA
560 570 580 590 600
MQGACFTISS LGHIGGTAFT PIVNAPEVAI LGVSKASMQP VWDGKAFQPR
610 620 630
LMLPLSLSYD HRVINGAAAA RFTKRLGDLL ADIRAILL
Length:638
Mass (Da):65,045
Last modified:January 23, 2007 - v3
Checksum:i8B92CB5ADEA0BEA1
GO

Sequence cautioni

The sequence CAA30987 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12455 Genomic DNA. Translation: CAA30987.1. Different initiation.
PIRiS01017. XXAV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12455 Genomic DNA. Translation: CAA30987.1. Different initiation.
PIRiS01017. XXAV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPBX-ray2.50A396-638[»]
1DPCX-ray2.60A396-638[»]
1DPDX-ray2.70A396-638[»]
1EAAX-ray2.60A396-638[»]
1EABX-ray2.60A396-638[»]
1EACX-ray2.60A396-638[»]
1EADX-ray2.60A396-638[»]
1EAEX-ray2.60A396-638[»]
1EAFX-ray2.60A396-638[»]
1IYUNMR-A2-79[»]
1IYVNMR-A2-79[»]
ProteinModelPortaliP10802.
SMRiP10802. Positions 2-79, 396-638.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_44910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QSN. Bacteria.
COG0508. LUCA.

Miscellaneous databases

EvolutionaryTraceiP10802.

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.
IPR006256. AcTrfase_Pyrv_DH_cplx.
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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODP2_AZOVI
AccessioniPrimary (citable) accession number: P10802
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 11, 2015
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.