P45118 (ODP2_HAEIN) 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

Gene names

Name:	aceF
Ordered Locus Names:	HI_1232

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
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 2 lipoyl cofactors 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 2 lipoyl-binding domains.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Lipoyl Repeat
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
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
	Chain	1 – 567	567	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162279
Regions
	Domain	1 – 74	74	Lipoyl-binding 1
	Domain	109 – 180	72	Lipoyl-binding 2
	Region	247 – 567	321	Subunit binding, catalytic
Sites
	Active site	484	1	Potential
	Active site	540	1	Potential
	Active site	544	1	Potential
Amino acid modifications
	Modified residue	41	1	N6-lipoyllysine By similarity
	Modified residue	147	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45118 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 891DBCDEB388C5B0	FASTA	567	59,411
	10 20 30 40 50 60 MSKQIQIPDI GSDEVTVTEV MVNVGDTISV DQSIINVEGD KASMEVPAPE AGVVKEILVK 70 80 90 100 110 120 VGDKVSTGTP MLVLEAAGAA PAADEPTAPV ADAPTAPVVA TAPTASAIVE VNVPDIGGDE 130 140 150 160 170 180 VNVTEIMVAV GDTITEEQSL ITVEGDKASM EVPAPFGGVV KEILVKSGDK VSTGSLIMRF 190 200 210 220 230 240 EVLGAAPAES ASAPASTSAP QTAAPATTAQ APQAAAPDTT AQAPQAAAPD TTAQAAQSNN 250 260 270 280 290 300 NVSGLSQEQV EASTGYAHAT PVIRRLAREF GVNLDKVKGT GRKGRIVKED IEAYVKTAVK 310 320 330 340 350 360 AYESGATAQA TGNGVANGAG LGLLPWPKVD FSKFGEIEEV ELSRINKISG ANLHRNWVII 370 380 390 400 410 420 PHVTHFDKAD ITDLEAFRKE QNALREKQKL GVKITPVVFI MKAVAKALEA YPRFNSSITE 430 440 450 460 470 480 DAQRLILKKY INIGVAVDTP NGLVVPVFKN VNKKGIIELS RELMEVSKKA REGKLTASDM 490 500 510 520 530 540 QGGCFTISSL GGIGTTHFAP IVNAPEVAIL GVSKSSMEPV WNGKEFAPRL ILPMSLSFDH 550 560 RVIDGADGAR FISYLGSVLA DLRRLVM

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22885.1.
PIR	I64111.
RefSeq	NP_439388.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P45118.
SMR	P45118. Positions 1-80, 108-186, 324-567.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI1232.
Proteomic databases
PRIDE	P45118.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22885; AAC22885; HI_1232.
GeneID	949836.
KEGG	hin:HI1232.
PATRIC	20191143. VBIHaeInf48452_1284.
Phylogenomic databases
eggNOG	COG0508.
KO	K00627.
OMA	PLSMSYD.
ProtClustDB	PRK11855.
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. 2 hits. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 2 hits.
TIGRFAMs	TIGR01348. PDHac_trf_long. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_HAEIN

Accession

Primary (citable) accession number: P45118

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program