P10802 (ODP2_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	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
Organism	Azotobacter vinelandii
Taxonomic identifier	354 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter group › Azotobacter

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 3 lipoyl cofactors covalently By similarity.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 3 lipoyl-binding domains.
Sequence caution	The sequence CAA30987.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Lipoyl Repeat
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	pyruvate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 638

637

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

PRO_0000162272

Regions

Domain

2 – 73

72

Lipoyl-binding 1

Domain

118 – 190

73

Lipoyl-binding 2

Domain

223 – 295

73

Lipoyl-binding 3

Region

328 – 381

54

E1/E3 binding

Region

382 – 638

257

Catalytic

Sites

Active site

611

1

Potential

Amino acid modifications

Modified residue

40

1

N6-lipoyllysine Potential

Modified residue

157

1

N6-lipoyllysine Potential

Modified residue

262

1

N6-lipoyllysine Potential

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

638

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

11 – 19

9

Beta strand

29 – 37

9

Beta strand

42 – 46

5

Beta strand

48 – 57

10

Beta strand

63 – 65

3

Beta strand

68 – 74

7

Helix

404 – 406

3

Helix

417 – 432

16

Beta strand

435 – 443

9

Helix

445 – 453

9

Helix

455 – 460

6

Helix

468 – 481

14

Helix

483 – 486

4

Beta strand

487 – 489

3

Beta strand

496 – 498

3

Beta strand

504 – 506

3

Beta strand

508 – 510

3

Beta strand

513 – 515

3

Beta strand

518 – 520

3

Helix

522 – 524

3

Helix

527 – 542

16

Helix

548 – 551

4

Beta strand

555 – 560

6

Turn

562 – 564

3

Beta strand

577 – 583

7

Beta strand

587 – 592

6

Beta strand

594 – 610

17

Turn

611 – 613

3

Helix

616 – 631

16

Helix

633 – 637

5

Sequences

	Sequence		Length	Mass (Da)
	P10802 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8B92CB5ADEA0BEA1	FASTA	638	65,045
	10 20 30 40 50 60 MSEIIRVPDI GGDGEVIELL VKTGDLIEVE QGLVVLESAK ASMEVPSPKA GVVKSVSVKL 70 80 90 100 110 120 GDKLKEGDAI IELEPAAGAA AAPAEAAAVP AAPTQAVDEA EAPSPGASAT PAPAAASQEV 130 140 150 160 170 180 RVPDIGSAGK ARVIEVLVKA GDQVQAEQSL IVLESDKASM EIPSPASGVV ESVAIQLNAE 190 200 210 220 230 240 VGTGDLILTL RTTGAQAQPT APAAAAAASP APAPLAPAAA GPQEVKVPDI GSAGKARVIE 250 260 270 280 290 300 VLVKAGDQVQ AEQSLIVLES DKASMEIPSP AAGVVESVAV QLNAEVGTGD QILTLRVAGA 310 320 330 340 350 360 APSGPRARGS PGQAAAAPGA APAPAPVGAP SRNGAKVHAG PAVRQLAREF GVELAAINST 370 380 390 400 410 420 GPRGRILKED VQAYVKAMMQ KAKEAPAAGA ASGAGIPPIP PVDFAKYGEI EEVPMTRLMQ 430 440 450 460 470 480 IGATNLHRSW LNVPHVTQFE SADITELEAF RVAQKAVAEK AGVKLTVLPL LLKACAYLLK 490 500 510 520 530 540 ELPDFNSSLA PSGQALIRKK YVHIGFAVDT PDGLLVPVIR NVDQKSLLQL AAEAAELAEK 550 560 570 580 590 600 ARSKKLGADA MQGACFTISS LGHIGGTAFT PIVNAPEVAI LGVSKASMQP VWDGKAFQPR 610 620 630 LMLPLSLSYD HRVINGAAAA RFTKRLGDLL ADIRAILL

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12455 Genomic DNA. Translation: CAA30987.1. Different initiation.

PIR

XXAV. S01017.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DPB	X-ray	2.50	A	396-637	[»]
1DPC	X-ray	2.60	A	396-637	[»]
1DPD	X-ray	2.70	A	396-637	[»]
1EAA	X-ray	2.60	A	396-637	[»]
1EAB	X-ray	2.60	A	396-637	[»]
1EAC	X-ray	2.60	A	396-637	[»]
1EAD	X-ray	2.60	A	396-637	[»]
1EAE	X-ray	2.60	A	396-637	[»]
1EAF	X-ray	2.60	A	396-637	[»]
1IYU	NMR	-	A	2-79	[»]
1IYV	NMR	-	A	2-79	[»]

ProteinModelPortal

P10802.

SMR

P10802. Positions 2-79, 396-638.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.30.559.10. 1 hit.
4.10.320.10. 1 hit.

InterPro

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]

Pfam

PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]

SUPFAM

SSF47005. E3_bd. 1 hit.
SSF51230. Hybrid_motif. 3 hits.

TIGRFAMs

TIGR01348. PDHac_trf_long. 1 hit.

PROSITE

PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10802.

Entry information

Entry name

ODP2_AZOVI

Accession

Primary (citable) accession number: P10802

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program