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Protein

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

Gene

ZK669.4

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). 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).By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei418 – 4181Sequence analysis
Active sitei422 – 4221Sequence analysis

GO - Molecular functioni

GO - Biological processi

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
Gene namesi
ORF Names:ZK669.4
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiZK669.4; CE01115; WBGene00014054.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 448Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrialPRO_0000421275
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711N6-lipoyllysinePROSITE-ProRule annotationBy similarity
Modified residuei261 – 2611N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ23571.
PaxDbiQ23571.

Interactioni

Protein-protein interaction databases

BioGridi39612. 1 interaction.
DIPiDIP-26430N.
IntActiQ23571. 2 interactions.
MINTiMINT-1052999.
STRINGi6239.ZK669.4.1.

Structurei

3D structure databases

ProteinModelPortaliQ23571.
SMRiQ23571. Positions 30-108, 144-183, 216-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 10576Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini143 – 18139E3-bindingAdd
BLAST

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.
GeneTreeiENSGT00810000125418.
HOGENOMiHOG000281564.
InParanoidiQ23571.
KOiK09699.
OMAiTIPHFTY.
OrthoDBiEOG7GFB4W.
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. Positions 30-108, 144-183, 216-448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi39612. 1 interaction.
DIPiDIP-26430N.
IntActiQ23571. 2 interactions.
MINTiMINT-1052999.
STRINGi6239.ZK669.4.1.

Proteomic databases

EPDiQ23571.
PaxDbiQ23571.

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.

Phylogenomic databases

eggNOGiKOG0558. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00810000125418.
HOGENOMiHOG000281564.
InParanoidiQ23571.
KOiK09699.
OMAiTIPHFTY.
OrthoDBiEOG7GFB4W.
PhylomeDBiQ23571.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi883345.
PROiQ23571.

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...

Publicationsi

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

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: March 16, 2016
This is version 123 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.