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UniProtKB - P10802 (ODP2_AZOVI)
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Gene
N/A
Organism
Azotobacter vinelandii
Status
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
- (R)-N6-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N6-(S8-acetyldihydrolipoyl)-L-lysyl-[protein] + CoAEC:2.3.1.12
Cofactori
(R)-lipoateBy similarityNote: Binds 3 lipoyl cofactors covalently.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 611 | Sequence analysis | 1 |
GO - Molecular functioni
- dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC
GO - Biological processi
- glycolytic process Source: UniProtKB-KW
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | 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 |
Organismi | Azotobacter vinelandii |
Taxonomic identifieri | 354 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter |
Pathology & Biotechi
Chemistry databases
DrugBanki | DB08120, 6,8-DIMERCAPTO-OCTANOIC ACID AMIDE DB01992, Coenzyme A DB01846, Oxidized coenzyme A |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000162272 | 2 – 638 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST | 637 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 40 | N6-lipoyllysinePROSITE-ProRule annotation | 1 | |
Modified residuei | 157 | N6-lipoyllysinePROSITE-ProRule annotation | 1 | |
Modified residuei | 262 | N6-lipoyllysinePROSITE-ProRule annotation | 1 |
Interactioni
Subunit structurei
Forms a 24-polypeptide structural core with octahedral symmetry.
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P10802 |
SMRi | P10802 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P10802 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 74 | Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST | 73 | |
Domaini | 117 – 191 | Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST | 75 | |
Domaini | 222 – 296 | Lipoyl-binding 3PROSITE-ProRule annotationAdd BLAST | 75 | |
Domaini | 338 – 375 | Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST | 38 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 90 – 119 | DisorderedSequence analysisAdd BLAST | 30 | |
Regioni | 201 – 220 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 301 – 336 | DisorderedSequence analysisAdd BLAST | 36 | |
Regioni | 382 – 638 | CatalyticAdd BLAST | 257 |
Sequence similaritiesi
Belongs to the 2-oxoacid dehydrogenase family.Curated
Keywords - Domaini
Lipoyl, RepeatFamily and domain databases
Gene3Di | 3.30.559.10, 1 hit 4.10.320.10, 1 hit |
InterProi | View protein in InterPro IPR003016, 2-oxoA_DH_lipoyl-BS IPR001078, 2-oxoacid_DH_actylTfrase IPR006256, AcTrfase_Pyrv_DH_cplx IPR000089, Biotin_lipoyl IPR023213, CAT-like_dom_sf IPR036625, E3-bd_dom_sf IPR004167, PSBD IPR011053, Single_hybrid_motif |
PANTHERi | PTHR43178:SF2, PTHR43178:SF2, 4 hits |
Pfami | View protein in Pfam PF00198, 2-oxoacid_dh, 1 hit PF00364, Biotin_lipoyl, 3 hits PF02817, E3_binding, 1 hit |
SUPFAMi | SSF47005, SSF47005, 1 hit SSF51230, SSF51230, 3 hits |
TIGRFAMsi | TIGR01348, PDHac_trf_long, 1 hit |
PROSITEi | View protein in PROSITE PS50968, BIOTINYL_LIPOYL, 3 hits PS00189, LIPOYL, 3 hits PS51826, PSBD, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P10802-1 [UniParc]FASTAAdd to basket
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
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. |
PIRi | S01017, XXAV |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X12455 Genomic DNA Translation: CAA30987.1 Different initiation. |
PIRi | S01017, XXAV |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1DPB | X-ray | 2.50 | A | 396-638 | [»] | |
1DPC | X-ray | 2.60 | A | 396-638 | [»] | |
1DPD | X-ray | 2.70 | A | 396-638 | [»] | |
1EAA | X-ray | 2.60 | A | 396-638 | [»] | |
1EAB | X-ray | 2.60 | A | 396-638 | [»] | |
1EAC | X-ray | 2.60 | A | 396-638 | [»] | |
1EAD | X-ray | 2.60 | A | 396-638 | [»] | |
1EAE | X-ray | 2.60 | A | 396-638 | [»] | |
1EAF | X-ray | 2.60 | A | 396-638 | [»] | |
1IYU | NMR | - | A | 2-79 | [»] | |
1IYV | NMR | - | A | 2-79 | [»] | |
AlphaFoldDBi | P10802 | |||||
SMRi | P10802 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB08120, 6,8-DIMERCAPTO-OCTANOIC ACID AMIDE DB01992, Coenzyme A DB01846, Oxidized coenzyme A |
Miscellaneous databases
EvolutionaryTracei | P10802 |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit 4.10.320.10, 1 hit |
InterProi | View protein in InterPro IPR003016, 2-oxoA_DH_lipoyl-BS IPR001078, 2-oxoacid_DH_actylTfrase IPR006256, AcTrfase_Pyrv_DH_cplx IPR000089, Biotin_lipoyl IPR023213, CAT-like_dom_sf IPR036625, E3-bd_dom_sf IPR004167, PSBD IPR011053, Single_hybrid_motif |
PANTHERi | PTHR43178:SF2, PTHR43178:SF2, 4 hits |
Pfami | View protein in Pfam PF00198, 2-oxoacid_dh, 1 hit PF00364, Biotin_lipoyl, 3 hits PF02817, E3_binding, 1 hit |
SUPFAMi | SSF47005, SSF47005, 1 hit SSF51230, SSF51230, 3 hits |
TIGRFAMsi | TIGR01348, PDHac_trf_long, 1 hit |
PROSITEi | View protein in PROSITE PS50968, BIOTINYL_LIPOYL, 3 hits PS00189, LIPOYL, 3 hits PS51826, PSBD, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ODP2_AZOVI | |
Accessioni | P10802Primary (citable) accession number: P10802 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 140 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families