Reviewed, UniProtKB/Swiss-Prot Q6ABX9 (ODP2_LEIXX)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
    EC=2.3.1.12
Alternative name(s):
    E2
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Gene names

Name:	pdhC
Ordered Locus Names:	Lxx25050

Organism

Leifsonia xyli subsp. xyli [Complete proteome] [HAMAP]

Taxonomic identifier

59736 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Leifsonia

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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) By similarity.
Catalytic activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 452	452	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000232458
Regions
	Domain	4 – 77	74	Lipoyl-binding
Sites
	Active site	425	1	Potential
Amino acid modifications
	Modified residue	44	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6ABX9-1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: E82E69643536926A	FASTA	452	47,427
	10 20 30 40 50 60 MRESQFLLPD VGEGLTEAEI VSWKVAPGDS VAVNQVIVEI ETAKSLVELP SPFEGTVGEL 70 80 90 100 110 120 LVVEGQTVEV GTPIFTVNGG EADHGVTEPA GEAEQAAVDA AASVTHESEE PKAGAVIVGY 130 140 150 160 170 180 GSAGHGTSRR RVTHPGAAAR PAAFPPAESA AEPGRAPSTP VPPSGGGPVI AKPPIRKLAK 190 200 210 220 230 240 DLGVDLSTVT ATGAIGEVTR EDVLREGTQA SVFRNIQTPE WPDDREERIL VKGVRKAIAN 250 260 270 280 290 300 AMVTSAFSAP HVSVFVDVDA TRTMEFVKRL KSAPDFVGVK VSPLLIMAKA IVWAVRRNPT 310 320 330 340 350 360 VNSTWTDEEI IVRHYVNLGI AAATPRGLIV PNVKEAQGMS LLELAGALEE LTLTAREGKT 370 380 390 400 410 420 QPADMANGTI TITNIGVFGM DTGTPILNPG EVGIVALGTI KQKPWVVDGE VRPRFVTTLG 430 440 450 GSFDHRVVDG DVASRFLADV ASIIEEPALL LD

References

[1]

"The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli subsp. xyli." Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P., Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D., de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R., Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H. , Coutinho L.L., El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S., Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F., Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A., Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C. Mol. Plant Microbe Interact. 17:827-836(2004) [PubMed: 15305603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CTCB07.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016822 Genomic DNA. Translation: AAT90113.1.
RefSeq	YP_063218.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2940497.
GenomeReviews	Gene locus Lxx25050 in contig AE016822_GR.
KEGG	lxx:Lxx25050.
NMPDR	fig|281090.3.peg.2005.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6ABX9.
OMA	FVDVDAT.
Enzyme and pathway databases
BioCyc	LXYL281090:LXX25050-MON.
BRENDA	2.3.1.12. 297084.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view]
Gene3D	G3DSA:4.10.320.10. E3_bd. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_LEIXX

Accession

Primary (citable) accession number: Q6ABX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	September 13, 2004
Last modified:	November 3, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)