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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

dlaT

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.By similarity

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 2 lipoyl cofactors covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei523 – 5231By similarity
Active sitei527 – 5271By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Names & Taxonomyi

Protein namesi
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 namesi
Name:dlaT
Synonyms:sucB
Ordered Locus Names:Mb2238
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001419 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysinePROSITE-ProRule annotation
Modified residuei162 – 1621N6-lipoyllysinePROSITE-ProRule annotation

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry. Part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3).By similarity

Structurei

3D structure databases

ProteinModelPortaliP65634.
SMRiP65634. Positions 3-76, 126-195, 243-278, 322-544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7776Lipoyl-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini121 – 19676Lipoyl-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini241 – 27838E3-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 E3-binding domain.Curated
Contains 2 lipoyl-binding domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281564.
KOiK00658.
OMAiQEDETVE.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR02927. SucB_Actino. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P65634-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFSVQMPAL GESVTEGTVT RWLKQEGDTV ELDEPLVEVS TDKVDTEIPS
60 70 80 90 100
PAAGVLTKII AQEDDTVEVG GELAVIGDAK DAGEAAAPAP EKVPAAQPES
110 120 130 140 150
KPAPEPPPVQ PTSGAPAGGD AKPVLMPELG ESVTEGTVIR WLKKIGDSVQ
160 170 180 190 200
VDEPLVEVST DKVDTEIPSP VAGVLVSISA DEDATVPVGG ELARIGVAAD
210 220 230 240 250
IGAAPAPKPA PKPVPEPAPT PKAEPAPSPP AAQPAGAAEG APYVTPLVRK
260 270 280 290 300
LASENNIDLA GVTGTGVGGR IRKQDVLAAA EQKKRAKAPA PAAQAAAAPA
310 320 330 340 350
PKAPPAPAPA LAHLRGTTQK ASRIRQITAN KTRESLQATA QLTQTHEVDM
360 370 380 390 400
TKIVGLRARA KAAFAEREGV NLTFLPFFAK AVIDALKIHP NINASYNEDT
410 420 430 440 450
KEITYYDAEH LGFAVDTEQG LLSPVIHDAG DLSLAGLARA IADIAARARS
460 470 480 490 500
GNLKPDELSG GTFTITNIGS QGALFDTPIL VPPQAAMLGT GAIVKRPRVV
510 520 530 540 550
VDASGNESIG VRSVCYLPLT YDHRLIDGAD AGRFLTTIKH RLEEGAFEAD

LGL
Length:553
Mass (Da):57,088
Last modified:October 11, 2004 - v1
Checksum:i54B6E70D23B804A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO43492.1.
RefSeqiNP_855887.1. NC_002945.3.
WP_003411450.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO43492; CDO43492; Mb2238.
GeneIDi1091362.
KEGGimbo:Mb2238.
PATRICi18006616. VBIMycBov88188_2454.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO43492.1.
RefSeqiNP_855887.1. NC_002945.3.
WP_003411450.1. NC_002945.3.

3D structure databases

ProteinModelPortaliP65634.
SMRiP65634. Positions 3-76, 126-195, 243-278, 322-544.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO43492; CDO43492; Mb2238.
GeneIDi1091362.
KEGGimbo:Mb2238.
PATRICi18006616. VBIMycBov88188_2454.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281564.
KOiK00658.
OMAiQEDETVE.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR02927. SucB_Actino. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-935 / AF2122/97.

Entry informationi

Entry nameiODP2_MYCBO
AccessioniPrimary (citable) accession number: P65634
Secondary accession number(s): Q10381, X2BJM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 22, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.