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P10802

- ODP2_AZOVI

UniProt

P10802 - ODP2_AZOVI

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene
N/A
Organism
Azotobacter vinelandii
Status
Reviewed - 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

Binds 3 lipoyl cofactors covalently.By similarity

Sites

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

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

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 638637Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-lipoyllysineSequence Analysis
Modified residuei157 – 1571N6-lipoyllysineSequence Analysis
Modified residuei262 – 2621N6-lipoyllysineSequence Analysis

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 – 7372Lipoyl-binding 1Add
BLAST
Domaini118 – 19073Lipoyl-binding 2Add
BLAST
Domaini223 – 29573Lipoyl-binding 3Add
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.Curated

Keywords - Domaini

Lipoyl, Repeat

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 CAA30987.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12455 Genomic DNA. Translation: CAA30987.1. Different initiation.
PIRiS01017. XXAV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12455 Genomic DNA. Translation: CAA30987.1 . Different initiation.
PIRi S01017. XXAV.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P10802.
SMRi P10802. Positions 2-79, 396-638.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P10802.

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.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis."
    Hanemaaijer R., Janssen A., de Kok A., Veeger C.
    Eur. J. Biochem. 174:593-599(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.
  2. "The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
    Hanemaaijer R., de Kok A., Jolles J., Veeger C.
    Eur. J. Biochem. 169:245-252(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16 AND 381-416.
  3. "Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2-oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H-NMR spectroscopy."
    Hanemaaijer R., Vervoort J., Westphal A.H., de Kok A., Veeger C.
    FEBS Lett. 240:205-210(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPOYL DOMAIN CONFORMATION.
  4. "Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex."
    Mattevi A., Obmolova G., Schulze E., Kalk K.H., Westphal A.H., de Kok A., Hol W.G.J.
    Science 255:1544-1550(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 382-638.
  5. "Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the N-terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
    Berg A., de Kok A., Vervoort J.
    Eur. J. Biochem. 221:87-100(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-79.
  6. "Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
    Berg A., Vervoort J., de Kok A.
    Eur. J. Biochem. 244:352-360(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-79.

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: October 1, 2014
This is version 112 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

External Data

Dasty 3