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Protein

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

Gene

dbt-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2 (By similarity). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component (By similarity). Required for the catabolism of branched-chain amino acids and the subsequent synthesis of monomethyl branched-chain fatty acids, which are important for regulating postembryonic growth (PubMed:26683372).By similarity1 Publication

Catalytic activityi

2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei418Sequence analysis1
Active sitei422Sequence analysis1

GO - Molecular functioni

GO - Biological processi

  • fatty acid biosynthetic process Source: UniProtKB-KW
  • positive regulation of embryonic development Source: UniProtKB
  • positive regulation of fatty acid biosynthetic process Source: UniProtKB
  • positive regulation of nematode larval development Source: UniProtKB
  • positive regulation of oviposition Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-CEL-389661. Glyoxylate metabolism and glycine degradation.
R-CEL-70895. Branched-chain amino acid catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC:2.3.1.168)
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase complex component E2
Dihydrolipoamide branched-chain transacylase E2Imported
Gene namesi
Name:dbt-11 PublicationImported
ORF Names:ZK669.4Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiZK669.4; CE01115; WBGene00014054; dbt-1.

Subcellular locationi

  • Mitochondrion matrix By similarity
  • Cytoplasmcytosol 1 Publication
  • Cell projectiondendrite 1 Publication
  • Cell projectioncilium 1 Publication

  • Note: Localizes to puncta within the cytosol which is consistent with its expected location in mitochondria.1 Publication

GO - Cellular componenti

  • cilium Source: UniProtKB
  • cytosol Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB-SubCell
  • neuron projection Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown results in reduced monomethyl branched-chain fatty acid generation and also results in larval arrest in the subsequent generation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000421275? – 448Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei71N6-lipoyllysinePROSITE-ProRule annotation1

Proteomic databases

EPDiQ23571.
PaxDbiQ23571.
PeptideAtlasiQ23571.
PRIDEiQ23571.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiWBGene00014054.

Interactioni

Protein-protein interaction databases

BioGridi39612. 1 interactor.
DIPiDIP-26430N.
IntActiQ23571. 2 interactors.
MINTiMINT-1052999.
STRINGi6239.ZK669.4.1.

Structurei

3D structure databases

ProteinModelPortaliQ23571.
SMRiQ23571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 105Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini143 – 181E3-bindingAdd BLAST39

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0558. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133743.
HOGENOMiHOG000281564.
InParanoidiQ23571.
KOiK09699.
OMAiTIPHFTY.
OrthoDBiEOG091G0FJ3.
PhylomeDBiQ23571.

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.
IPR015761. BCKDC_E2.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR23151:SF71. PTHR23151:SF71. 1 hit.
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q23571-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAARLLGTS SRIFKLNKHL HTSKVAFMPV VQFKLSDIGE GIAEVQVKEW
60 70 80 90 100
YVKEGDTISQ FDKVCEVQSD KAAVTISCRY DGIVKKLYHE VDGMARVGQA
110 120 130 140 150
LIDVEIEGNV EEPEQPKKEA ASSSPEAPKS SAPKAPESAH SEGKVLATPA
160 170 180 190 200
VRRIAIENKI KLAEVRGTGK DGRVLKEDVL KFLGQVPADH TSGSTNIRTT
210 220 230 240 250
HQAPQPSSKS YEPLKEDVAV PIRGYTRAMV KTMTEALKIP HFGYNDEINV
260 270 280 290 300
DSLVKYRAEL KEFAKERHIK LSYMPFFIKA ASLALLEYPS LNSTTDEKME
310 320 330 340 350
NVIHKASHNI CLAMDTPGGL VVPNIKNCEQ RSIFEIAQEL NRLLEAGKKQ
360 370 380 390 400
QIKREDLIDG TFSLSNIGNI GGTYASPVVF PPQVAIGAIG KIEKLPRFDK
410 420 430 440
HDNVIPVNIM KVSWCADHRV VDGATMARFS NRWKFYLEHP SAMLAQLK
Length:448
Mass (Da):49,691
Last modified:November 1, 1996 - v1
Checksum:iE3C0FC5B2C5946AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37093 Genomic DNA. Translation: CAA85465.1.
PIRiT27955.
RefSeqiNP_495670.1. NM_063269.5.
UniGeneiCel.6097.

Genome annotation databases

EnsemblMetazoaiZK669.4; ZK669.4; WBGene00014054.
GeneIDi174279.
KEGGicel:CELE_ZK669.4.
UCSCiZK669.4.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37093 Genomic DNA. Translation: CAA85465.1.
PIRiT27955.
RefSeqiNP_495670.1. NM_063269.5.
UniGeneiCel.6097.

3D structure databases

ProteinModelPortaliQ23571.
SMRiQ23571.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi39612. 1 interactor.
DIPiDIP-26430N.
IntActiQ23571. 2 interactors.
MINTiMINT-1052999.
STRINGi6239.ZK669.4.1.

Proteomic databases

EPDiQ23571.
PaxDbiQ23571.
PeptideAtlasiQ23571.
PRIDEiQ23571.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiZK669.4; ZK669.4; WBGene00014054.
GeneIDi174279.
KEGGicel:CELE_ZK669.4.
UCSCiZK669.4.1. c. elegans.

Organism-specific databases

CTDi174279.
WormBaseiZK669.4; CE01115; WBGene00014054; dbt-1.

Phylogenomic databases

eggNOGiKOG0558. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133743.
HOGENOMiHOG000281564.
InParanoidiQ23571.
KOiK09699.
OMAiTIPHFTY.
OrthoDBiEOG091G0FJ3.
PhylomeDBiQ23571.

Enzyme and pathway databases

ReactomeiR-CEL-389661. Glyoxylate metabolism and glycine degradation.
R-CEL-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

PROiQ23571.

Gene expression databases

BgeeiWBGene00014054.

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.
IPR015761. BCKDC_E2.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR23151:SF71. PTHR23151:SF71. 1 hit.
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODB2_CAEEL
AccessioniPrimary (citable) accession number: Q23571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.