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Protein

Lipoyl synthase

Gene

lipA

Organism
Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)
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.

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.

Cofactori

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

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].
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 bindingi37Iron-sulfur 1 (4Fe-4S)1
Metal bindingi42Iron-sulfur 1 (4Fe-4S)1
Metal bindingi48Iron-sulfur 1 (4Fe-4S)1
Metal bindingi63Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi67Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi70Iron-sulfur 2 (4Fe-4S-S-AdoMet)1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase (EC:2.8.1.8)
Alternative name(s):
Lip-syn
Short name:
LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene namesi
Name:lipA
Ordered Locus Names:BDI_2192
OrganismiParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)
Taxonomic identifieri435591 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesTannerellaceaeParabacteroides
Proteomesi
  • UP000000566 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000122501 – 281Lipoyl synthaseAdd BLAST281

Interactioni

Protein-protein interaction databases

STRINGi435591.BDI_2192.

Structurei

3D structure databases

ProteinModelPortaliA6LE09.
SMRiA6LE09.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235998.
KOiK03644.
OMAiPYCDIDF.
OrthoDBiPOG091H069D.

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.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
PfamiView protein in Pfam
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.

A6LE09-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQHLRKPDW LKIRLGGNEQ FTKTKSIVES HCLHTICTSG KCPNMGECWS
60 70 80 90 100
RGTATFMIGG EICTRSCRFC NTLTGKPLPL DPKEPANVAE SIRLMNLKHA
110 120 130 140 150
VITSVDRDDL PDLGASHWVN TIRTIKEVNP QTTVEVLIPD FQGRLDLVDQ
160 170 180 190 200
VVDAAPEIIS HNMETVRRIS PQVRSAAKYD VSLSVLRRIA ERGVVAKTGI
210 220 230 240 250
MVGLGETEDE VLELMDDVLQ AGVSVLTIGQ YLQPSRKNIP VSEYVTPERF
260 270 280
EYYRQQAVNK GFKKVESAPL VRSSYHAEKH I
Length:281
Mass (Da):31,394
Last modified:July 24, 2007 - v1
Checksum:iB15D90B412461572
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000140 Genomic DNA. Translation: ABR43923.1.
RefSeqiWP_005854269.1. NC_009615.1.

Genome annotation databases

EnsemblBacteriaiABR43923; ABR43923; BDI_2192.
GeneIDi5307341.
KEGGipdi:BDI_2192.

Similar proteinsi

Entry informationi

Entry nameiLIPA_PARD8
AccessioniPrimary (citable) accession number: A6LE09
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: October 25, 2017
This is version 67 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families