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Protein

Lipoyl synthase, mitochondrial

Gene

v1g225637

Organism
Nematostella vectensis (Starlet sea anemone)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi50 – 501Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi56 – 561Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi71 – 711Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi75 – 751Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi78 – 781Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
ORF Names:v1g225637
OrganismiNematostella vectensis (Starlet sea anemone)
Taxonomic identifieri45351 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaEdwardsiidaeNematostella
ProteomesiUP000001593: Unassembled WGS sequence

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 291Lipoyl synthase, mitochondrialPRO_0000398226
Transit peptidei1 – ?MitochondrionUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi45351.JGI225637.

Structurei

3D structure databases

ProteinModelPortaliA7TDI2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiA7TDI2.
KOiK03644.
OMAiHAGDDFR.
OrthoDBiEOG7P2XS7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A7TDI2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNTVTENVFP PREPKPKWLR VKLPTGKNYT ELRGLVDKYK LNTICASGSC
60 70 80 90 100
PNMGECWGEG TATFMILGNI CTRSCGFCGV KTGRPETVDW DEPEKVARSI
110 120 130 140 150
KLMKIKHAVI TSVDRDDLKD MGSIIWAETV KAIRRMNPNT TLETLIPDFQ
160 170 180 190 200
GNTRNLDRII EVAPEVVSHN METVKRLTRE VRIQAKYEKS LEVLRYLKAQ
210 220 230 240 250
GIKRTKSGIM LGLGEKEEEV IQVLHDLRDA NVDIVTIGQY LQPSKKHLPV
260 270 280 290
KEYISPEQFE KYEKIGKELG FRHVESGALV RSSYHAEKHI H
Length:291
Mass (Da):33,132
Last modified:October 2, 2007 - v1
Checksum:i974657A99F1109DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS477892 Genomic DNA. Translation: EDO25859.1.
RefSeqiXP_001617959.1. XM_001617909.1.

Genome annotation databases

EnsemblMetazoaiEDO25859; EDO25859; NEMVEDRAFT_v1g225637.
GeneIDi5496152.
KEGGinve:NEMVE_v1g225637.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS477892 Genomic DNA. Translation: EDO25859.1.
RefSeqiXP_001617959.1. XM_001617909.1.

3D structure databases

ProteinModelPortaliA7TDI2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi45351.JGI225637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiEDO25859; EDO25859; NEMVEDRAFT_v1g225637.
GeneIDi5496152.
KEGGinve:NEMVE_v1g225637.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiA7TDI2.
KOiK03644.
OMAiHAGDDFR.
OrthoDBiEOG7P2XS7.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CH2 X CH6.

Entry informationi

Entry nameiLIAS_NEMVE
AccessioniPrimary (citable) accession number: A7TDI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 2, 2007
Last modified: January 7, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.