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Protein

Lipoyl synthase

Gene

lipA

Organism
Bacteroides fragilis (strain YCH46)
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 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 bindingi39Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi44Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi50Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi65Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi69Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi72Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

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 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 annotation
Ordered Locus Names:BF0976
OrganismiBacteroides fragilis (strain YCH46)
Taxonomic identifieri295405 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
Proteomesi
  • UP000002197 Componenti: Chromosome

Subcellular locationi

Q64XQ0:
  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003252331 – 288Lipoyl synthaseAdd BLAST288

Structurei

3D structure databases

ProteinModelPortaliQ64XQ0.
SMRiQ64XQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000235997.
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.

Q64XQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNDKRVRKP EWLKISIGAN ERYTETKRIV ESHCLHTICS SGRCPNMGEC
60 70 80 90 100
WGKGTATFMI AGDICTRSCK FCNTQTGRPL PLDPDEPAHV AESIALMKLS
110 120 130 140 150
HAVITSVDRD DLPDLGAAHW AQTIREIKRL NPETTTEVLI PDFQGRKELI
160 170 180 190 200
DQVIKACPEI ISHNMETVKR ISPQVRSAAN YHTSLEVIRQ IAESGITAKS
210 220 230 240 250
GIMVGLGETP AEVEELMDDL ISVGCKILTI GQYLQPTHKH FPVAAYITPE
260 270 280
QFAVYKETGL KKGFEQVESA PLVRSSYHAE KHIRFNNK
Length:288
Mass (Da):32,092
Last modified:October 25, 2004 - v1
Checksum:i546C89DE515F08D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006841 Genomic DNA. Translation: BAD47726.1.
RefSeqiWP_008767975.1. NC_006347.1.
YP_098260.1. NC_006347.1.

Genome annotation databases

EnsemblBacteriaiBAD47726; BAD47726; BF0976.
GeneIDi3081276.
KEGGibfr:BF0976.
PATRICifig|295405.11.peg.976.

Similar proteinsi

Entry informationi

Entry nameiLIPA_BACFR
AccessioniPrimary (citable) accession number: Q64XQ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 25, 2004
Last modified: October 25, 2017
This is version 80 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

Documents

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