Reviewed, UniProtKB/Swiss-Prot O66119 (ODP2_ZYMMO)

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
Synonyms:	pdhB
Ordered Locus Names:	ZMO0510

Organism

Zymomonas mobilis [Complete proteome] [HAMAP]

Taxonomic identifier

542 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas

Protein attributes

Sequence length	440 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 pyruvate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	pyruvate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
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 – 440	440	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162296
Regions
	Domain	1 – 77	77	Lipoyl-binding
Sites
	Active site	412	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine Potential
Experimental info
	Sequence conflict	169	1	N → S in CAA63808. Ref.1
	Sequence conflict	186 – 188	3	IAE → VTG in CAA63808. Ref.1
	Sequence conflict	203	1	A → V in CAA63808. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O66119-1 [UniParc]. Last modified February 15, 2005. Version 2. Checksum: 6BC8A592FC0AF6B3	FASTA	440	46,833
	10 20 30 40 50 60 MSIEVKMPAL SPTMTEGTLA KWLVKEGDAV KAGDILAEIE TDKAIMEFET VDAGIIAKIL 70 80 90 100 110 120 VPEGSENIAV GQVIAVMAEA GEDVSQVAAS ASSQISEPSE KADVAQKETA DSETISIDAS 130 140 150 160 170 180 LDKAISNAGY GNKTENMTAS YQEKAGRIKA SPLAKRLAKK NHVDLKQVNG SGPHGRIIKA 190 200 210 220 230 240 DIEAFIAEAN QASSNPSVST PEASGKITHD TPHNSIKLSN MRRVIARRLT ESKQNIPHIY 250 260 270 280 290 300 LTVDVQMDAL LKLRSELNES LAVQNIKISV NDMLIKAQAL ALKATPNVNV AFDGDQMLQF 310 320 330 340 350 360 SQADISVAVS VEGGLITPIL KQADTKSLSA LSVEMKELIA RAREGRLQPQ EYQGGTSSIS 370 380 390 400 410 420 NMGMFGIKQF NAVINPPQAS ILAIGSGERR PWVIDDAITI ATVATITGSF DHRVIDGADA 430 440 AAFMSAFKHL VEKPLGILAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification of the pyruvate dehydrogenase multienzyme complex of Zymomonas mobilis and identification and sequence analysis of the corresponding genes." Neveling U., Klasen R., Bringer-Meyer S., Sahm H. J. Bacteriol. 180:1540-1548(1998) [PubMed: 9515924] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 29191 / DSM 3580 / IFO 13756 / NCIB 11199 / ZM6.
[2]	"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4." Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. , Kang H.L., Lee S.Y., Lee K.J., Kang H.S. Nat. Biotechnol. 23:63-68(2005) [PubMed: 15592456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X93605 Genomic DNA. Translation: CAA63808.1. AE008692 Genomic DNA. Translation: AAV89134.1.
RefSeq	YP_162245.1.
3D structure databases
HSSP	HSSP built from PDB template 1FYC based on UniProtKB P10515.
ModBase	Search...
Genome annotation databases
GeneID	3189399.
GenomeReviews	Gene locus ZMO0510 in contig AE008692_GR.
KEGG	zmo:ZMO0510.
NMPDR	fig|264203.3.peg.1006.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O66119.
OMA	KWGLTME.
Enzyme and pathway databases
BioCyc	ZMOB264203:ZMO0510-MON.
BRENDA	2.3.1.12. 1658.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. 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]
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_ZYMMO

Accession

Primary (citable) accession number: O66119
Secondary accession number(s): Q5NQ71

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 15, 2005
Last modified:	November 3, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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