P65634 (ODP2_MYCBO) 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
Pyruvate dehydrogenase complex component E2
Short name=PDH component E2

Gene names

Name:	dlaT
Synonyms:	sucB
Ordered Locus Names:	Mb2238

Organism

Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]

Taxonomic identifier

233413 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 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. Makes part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3) By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 E3-binding domain. Contains 2 lipoyl-binding domains.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Lipoyl Repeat
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 553	553	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162267
Regions
	Domain	1 – 76	76	Lipoyl-binding 1
	Domain	122 – 195	74	Lipoyl-binding 2
	Domain	241 – 278	38	E3-binding
Sites
	Active site	523	1	By similarity
	Active site	527	1	By similarity
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine Potential
	Modified residue	162	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	P65634 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 54B6E70D23B804A7	FASTA	553	57,088
	10 20 30 40 50 60 MAFSVQMPAL GESVTEGTVT RWLKQEGDTV ELDEPLVEVS TDKVDTEIPS PAAGVLTKII 70 80 90 100 110 120 AQEDDTVEVG GELAVIGDAK DAGEAAAPAP EKVPAAQPES KPAPEPPPVQ PTSGAPAGGD 130 140 150 160 170 180 AKPVLMPELG ESVTEGTVIR WLKKIGDSVQ VDEPLVEVST DKVDTEIPSP VAGVLVSISA 190 200 210 220 230 240 DEDATVPVGG ELARIGVAAD IGAAPAPKPA PKPVPEPAPT PKAEPAPSPP AAQPAGAAEG 250 260 270 280 290 300 APYVTPLVRK LASENNIDLA GVTGTGVGGR IRKQDVLAAA EQKKRAKAPA PAAQAAAAPA 310 320 330 340 350 360 PKAPPAPAPA LAHLRGTTQK ASRIRQITAN KTRESLQATA QLTQTHEVDM TKIVGLRARA 370 380 390 400 410 420 KAAFAEREGV NLTFLPFFAK AVIDALKIHP NINASYNEDT KEITYYDAEH LGFAVDTEQG 430 440 450 460 470 480 LLSPVIHDAG DLSLAGLARA IADIAARARS GNLKPDELSG GTFTITNIGS QGALFDTPIL 490 500 510 520 530 540 VPPQAAMLGT GAIVKRPRVV VDASGNESIG VRSVCYLPLT YDHRLIDGAD AGRFLTTIKH 550 RLEEGAFEAD LGL

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248341 Genomic DNA. Translation: CAD97091.1.
RefSeq	NP_855887.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P65634.
SMR	P65634. Positions 3-76, 126-195, 243-278, 322-544.
ModBase	Search...
Protein-protein interaction databases
STRING	233413.Mb2238.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD97091; CAD97091; Mb2238.
GeneID	1091362.
KEGG	mbo:Mb2238.
PATRIC	18006616. VBIMycBov88188_2454.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281564.
KO	K00658.
OMA	TEGTITQ.
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. IPR014276. 2-oxoglutarate_DH_E2. 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	TIGR02927. SucB_Actino. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_MYCBO

Accession

Primary (citable) accession number: P65634
Secondary accession number(s): Q10381

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program