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Protein

Lipoyl synthase

Gene

lipA

Organism
Streptomyces lividans TK24
Status
Unreviewed-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 N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

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: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Octanoyltransferase (lipB)
  2. Lipoyl synthase (lipA)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi56Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi61Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi67Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi82Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi86Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi89Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotationImported
Ligand4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-synUniRule annotation
Short name:
LSUniRule annotation
Lipoate synthaseUniRule annotation
Lipoic acid synthaseUniRule annotation
Sulfur insertion protein LipAUniRule annotation
Gene namesi
Name:lipAUniRule annotationImported
ORF Names:SLIV_26745Imported
OrganismiStreptomyces lividans TK24Imported
Taxonomic identifieri457428 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
Proteomesi
  • UP000028682 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliD6EHK7.
SMRiD6EHK7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 286Elp3InterPro annotationAdd BLAST215

Sequence similaritiesi

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

Phylogenomic databases

KOiK03644.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
PfamiView protein in Pfam
PF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SFLDiSFLDG01058. lipoyl_synthase_like. 1 hit.
SFLDS00029. Radical_SAM. 1 hit.
SMARTiView protein in SMART
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

D6EHK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVAPDGRK MLRLEVRNSQ TPIERKPEWI KTRAKMGPEY TKMQNLVKSE
60 70 80 90 100
GLHTVCQEAG CPNIYECWED REATFLIGGD QCTRRCDFCQ IDTGKPEALD
110 120 130 140 150
RDEPRRVGES VVTMDLNYAT ITGVARDDLP DGGAWLYAET VRQIHEQTAG
160 170 180 190 200
REAGRTKVEL LAPDFNAVPE LLREVFESRP EVFAHNVETV PRIFKRIRPG
210 220 230 240 250
FRYERSLKVI TDARDFGLVT KSNLILGMGE TREEISEALK QLHEAGCELI
260 270 280 290 300
TITQYLRPSV RHHPVERWVK PQEFVELKEE AEQIGFSGVM SGPLVRSSYR
310
AGRLYGMAME QRRSATV
Length:317
Mass (Da):36,085
Last modified:July 13, 2010 - v1
Checksum:i43C62FD6AEBAB177
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP009124 Genomic DNA. Translation: AIJ16260.1.
RefSeqiWP_003976621.1. NZ_GG657756.1.

Genome annotation databases

EnsemblBacteriaiAIJ16260; AIJ16260; SLIV_26745.
GeneIDi29661798.
KEGGislv:SLIV_26745.
PATRICifig|457428.16.peg.5499.

Similar proteinsi

Entry informationi

Entry nameiD6EHK7_STRLI
AccessioniPrimary (citable) accession number: D6EHK7
Entry historyiIntegrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: October 25, 2017
This is version 55 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported