Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei523By similarity1
Active sitei527By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

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:BQ2027_MB2238
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001419 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622671 – 553Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei162N6-lipoyllysinePROSITE-ProRule annotation1

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST76
Domaini121 – 196Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST76
Domaini243 – 280Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

HOGENOMiHOG000281564.
KOiK00658.
OMAiMKVPSPG.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiView protein in InterPro
IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR014276. 2-oxoglutarate_DH_E2.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
PfamiView protein in Pfam
PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR02927. SucB_Actino. 1 hit.
PROSITEiView protein in PROSITE
PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
PS51826. PSBD. 1 hit.

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
LT708304 Genomic DNA. Translation: SIU00846.1.
RefSeqiNP_855887.1. NC_002945.3.
WP_003411450.1. NC_002945.4.

Genome annotation databases

EnsemblBacteriaiCDO43492; CDO43492; Mb2238.
KEGGimbo:Mb2238.
PATRICifig|233413.5.peg.2454.

Similar proteinsi

Entry informationi

Entry nameiODP2_MYCBO
AccessioniPrimary (citable) accession number: P65634
Secondary accession number(s): A0A1R3Y0P9, Q10381, X2BJM2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: August 30, 2017
This is version 92 of the entry and version 1 of the sequence. See 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