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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)DescriptionActionsGraphical viewLength
Active sitei611Sequence analysis1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001622722 – 638Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST637

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei157N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei262N6-lipoyllysinePROSITE-ProRule annotation1

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

STRINGi322710.Avin_44910.

Structurei

Secondary structure

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi11 – 19Combined sources9
Beta strandi29 – 37Combined sources9
Beta strandi42 – 46Combined sources5
Beta strandi48 – 57Combined sources10
Beta strandi63 – 65Combined sources3
Beta strandi68 – 74Combined sources7
Helixi404 – 406Combined sources3
Helixi417 – 432Combined sources16
Beta strandi435 – 443Combined sources9
Helixi445 – 453Combined sources9
Helixi455 – 460Combined sources6
Helixi468 – 481Combined sources14
Helixi483 – 486Combined sources4
Beta strandi487 – 489Combined sources3
Beta strandi496 – 498Combined sources3
Beta strandi504 – 506Combined sources3
Beta strandi508 – 510Combined sources3
Beta strandi513 – 515Combined sources3
Beta strandi518 – 520Combined sources3
Helixi522 – 524Combined sources3
Helixi527 – 542Combined sources16
Helixi548 – 551Combined sources4
Beta strandi555 – 560Combined sources6
Turni562 – 564Combined sources3
Beta strandi577 – 583Combined sources7
Beta strandi587 – 592Combined sources6
Beta strandi594 – 610Combined sources17
Turni611 – 613Combined sources3
Helixi616 – 631Combined sources16
Helixi633 – 637Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 74Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST73
Domaini117 – 191Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST75
Domaini222 – 296Lipoyl-binding 3PROSITE-ProRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni328 – 381E1/E3 bindingAdd BLAST54
Regioni382 – 638CatalyticAdd BLAST257

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
PDB 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.
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 2, 2016
This is version 121 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.