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Protein

Lipoyl synthase

Gene

lipA

Organism
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
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 bindingi39Iron-sulfur 1 (4Fe-4S)1
Metal bindingi44Iron-sulfur 1 (4Fe-4S)1
Metal bindingi50Iron-sulfur 1 (4Fe-4S)1
Metal bindingi65Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi69Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi72Iron-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

BioCyciBFRA272559:GKF0-865-MONOMER.
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:BF0898
OrganismiBacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
Taxonomic identifieri272559 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
Proteomesi
  • UP000006731 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003252341 – 288Lipoyl synthaseAdd BLAST288

Interactioni

Protein-protein interaction databases

STRINGi272559.BF0898.

Structurei

3D structure databases

ProteinModelPortaliQ5LGU6.
SMRiQ5LGU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235997.
KOiK03644.
OMAiPYCDIDF.

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.

Q5LGU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNDKRVRKP EWLKISIGAN ERYTETKRIV ESHCLHTICS SGRCPNMGEC
60 70 80 90 100
WGKGTATFMI AGDICTRSCK FCNTQTGRPL PLDPDEPTHV AESIALMKLS
110 120 130 140 150
HAVITSVDRD DLPDLGAAHW AQTIREIKRL NPETTTEVLI PDFQGRKELV
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):32,108
Last modified:June 21, 2005 - v1
Checksum:i48A0ED0A235CB9C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR626927 Genomic DNA. Translation: CAH06641.1.
RefSeqiWP_005795984.1. NC_003228.3.

Genome annotation databases

EnsemblBacteriaiCAH06641; CAH06641; BF9343_0860.
KEGGibfs:BF9343_0860.

Similar proteinsi

Entry informationi

Entry nameiLIPA_BACFN
AccessioniPrimary (citable) accession number: Q5LGU6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 21, 2005
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, Reference proteome

Documents

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